Saturday, October 28, 2023

How to deal with visual misinformation circulating in the Israel-Hamas war and other conflicts

Social media is often used during times of conflict to spread fake news. Jonathan Raa/NurPhoto via Getty Images
Paul Morrow, University of Dayton

In the three weeks since war began between Israel and Hamas, social media has been taken over with images and stories of attacks, many of which proved false.

For example, within hours of Hamas’ surprise attack on Oct. 7, 2023, screen grabs from a popular video game were shared by thousands of social media users as if depicting real scenes of violence against Israeli troops in Gaza. Five days later, a real explosion at a hospital in Gaza spurred further sharing of such spurious images to buttress various claims and counterclaims about responsibility for the casualties.

It’s not just this war. Over the past decade, international commissions and tribunals working to mediate conflicts in Syria, Myanmar, Ukraine and elsewhere have struggled to verify the large amount of digital evidence.

As a human rights scholar, I have, of late, been studying the ethics of viewing photos and videos of war and atrocities in situations where falsification of imagery is widespread. A principal lesson of this research is that users of social media have significant power to influence the content they receive and thus bear some responsibility when they consume and share false information.

Defining misinformation and disinformation

Scholars and policymakers distinguish misinformation from disinformation based on the intentions behind their creation and circulation. Misinformation consists of false information that is not created or circulated with the intent to deceive. Disinformation consists of false information, including visual information, that is intended to deceive and do harm.

At the start of any war, misinformation proliferates. Rumors that Ukrainian President Volodymyr Zelenskyy had fled Kyiv spread quickly after Russian forces invaded that country, only to be rebutted by videos posted from the streets of the capital. The difficulty of sifting reports on the ground, along with the reality that Zelenskyy was personally at risk, made many people accept and share those rumors.

Increasingly, however, false information about conflicts comes from actors – whether governments, military officials, separatist groups or private citizens – intentionally using texts and images to deceive. In Myanmar, for example, military propaganda officers published photographs supposedly depicting Rohingya people arriving in the country under British colonial rule in the mid-20th century. In actuality, these photographs, shared to support the military’s claim that the Rohingya had no right to live in Myanmar, depicted refugees from the 1994 Rwandan genocide.

Conditions for ethical responsibility

As social media becomes saturated with falsified images of mass violence in the Israel-Hamas war, the Ukraine war and other regions of the globe, individuals should ask what ethical responsibility they bear for their consumption of misinformation and disinformation.

Some might deny that users of digital media bear any such responsibility, since they are merely the passive recipients of content created by others. Philosopher Gideon Rosen claims that when people are passive toward some occurrence, they generally don’t bear ethical responsibility for it. Anyone scrolling the internet will passively encounter hundreds of images and related texts, and it is tempting to assume they bear no responsibility for the images of war and mass violence that they see but only for how they respond to them.

However, users of digital media are not merely passive recipients of falsified images and stories. Instead, they have power to influence the kinds of images that show up on their screens. This means, in turn, that users bear some ethical responsibility for their consumption of visual misinformation and disinformation.

Algorithms and influence

A woman sits facing two computer screens while scrolling through news stories.
Digital media relies on algorithms to deliver content. Noah Berger/AFP via Getty Images

Digital media platforms deliver content to users on the basis of complex decision-making procedures known as algorithms. Through both online and offline behaviors, users help determine what these algorithms deliver.

It is helpful to distinguish between influence and control. Having control over content would mean either encountering only images and stories that one consciously chooses or having the power to screen out any and all unwanted images. It is typical of digital communications, as philosopher Onora O'Neill has pointed out, that users lack the ability to control content in these ways.

Nevertheless, users can significantly influence the material they encounter in digital spaces. The algorithms by which social media platforms and other digital networks deliver content to users are not fully transparent, but neither are they wholly mysterious. In most cases, they are propelled by users’ past engagement with a platform’s content – a fact reflected in the very name of the “For You” page on TikTok.

Liking, tagging, commenting on or merely continuing to watch images of war and atrocities tends to lead to additional encounters with such content. The potential risks of this algorithmic process became apparent in the mid-2010s, when YouTube’s algorithm was found to be leading users into progressively more extreme videos related to jihadist violence.

Although major social media platforms have community guidelines prohibiting incitement to violence and sharing of graphic content, those prohibitions are difficult to enforce. In the context of some ongoing wars, they have even been relaxed – with Facebook temporarily allowing posts calling for violence against Russian troops and paramilitary groups occupying parts of Ukraine, for example. Taken together, these processes and policies have opened the door to substantial misinformation and disinformation about armed conflict.

Hiding, reporting or simply disengaging with violent content, by contrast, tends to lead to fewer such messages coming in. It may also reduce the odds that such content will reach others. If one knows that a Facebook friend or TikTok content creator has shared false information before, it is possible to block that friend or unfollow that creator.

Because users have these means of influencing the images they receive, it is reasonable to assign them some responsibility for algorithmically generated misinformation and disinformation.

Verifying images

Altering patterns of engagement with digital content can decrease users’ exposure to misinformation in wartime. But how can users verify the images they do receive before directing others to them?

One simple protocol, promoted by educators and public health groups, is known by the acronym SIFT: stop, investigate, find, trace. The four stages of this protocol ask users to stop, investigate the source of a message, find better coverage, and trace quotes and claims back to their original contexts.

Images, like quotes, can often be traced to their original contexts. Google makes available its reverse image search tool, which allows users to select an image – or parts of it – and find where else it appears online. I found this tool helpful during the first months of the COVID pandemic, when Holocaust photographs were circulated online in posts comparing mask mandates to deportation trains. Of course, as journalists and forensic researchers are quick to point out, such tools can only be applied to a small portion of the images we encounter in our daily lives.

No technique or protocol will give users absolute control of the images they see in wartime or provide complete assurance against sharing false information. But by understanding users’ power to influence content, it may be possible to mitigate these risks and promote a more truthful future.

Paul Morrow, Human Rights Fellow, University of Dayton

This article is republished from The Conversation under a Creative Commons license. 

Tuesday, October 24, 2023

Your immune system makes its own antiviral drug − and it’s likely one of the most ancient

Blocking viruses from replicating their RNA is one way antivirals work. CROCOTHERY/iStock via Getty Images Plus
Neil Marsh, University of Michigan

Antiviral drugs are generally considered to be a 20th century invention. But recent research has uncovered an unexpected facet to your immune system: It can synthesize its own antiviral molecules in response to viral infections.

My laboratory studies a protein that makes these natural antiviral molecules. Far from a modern human invention, nature evolved cells to make their own “drugs” as the earliest defense against viruses.

How antivirals work

Viruses have no independent life cycle – they are completely dependent on the cells they infect to supply all the chemical building blocks needed to replicate themselves. Once inside a cell, the virus hijacks its machinery and turns it into a factory to make hundreds of new viruses.

Antiviral drugs are molecules that inactivate proteins essential to the functioning of the virus by exploiting the fundamental differences in the way that cells and viruses replicate.

One key difference between cells and most viruses is how they store their genetic information. All cells use DNA to store their genetic information. DNA is a long, chainlike molecule built from four different chemical building blocks, each representing a different “letter” of the genetic code. These building blocks are connected by chemical bonds in a head-to-tail fashion to produce strings of millions of letters. The order of these letters spells out the genetic blueprint for building a new cell.

Many viruses, however, store their genetic information using RNA. RNA is built from a chain of four chemical letters, just like DNA, but the letters have slightly different molecular structures. RNA is single-stranded, while DNA is double-stranded. Viral genomes are also much smaller than cellular genomes, typically only a few thousand letters long.

Diagram of the mechanisms of four classes of HIV antivirals
This diagram shows how four different classes of antiviral drugs inhibit HIV. One stops viruses from entering cells, and three inhibit different viral enzymes. Thomas Splettstoesser/Wikimedia Commons, CC BY-SA

When a virus replicates, it makes many copies of its RNA genome using a protein called RNA polymerase. The polymerase starts at one end of the existing RNA chain and “reads” the string of chemical letters one at a time, selecting the appropriate building block and adding it to the growing strand of RNA. This process is repeated until the entire sequence of letters has been copied to form a new RNA chain.

One class of antiviral drugs interferes with the RNA copying process in a cunning way. The head-to-tail construction of the RNA chain requires each chemical letter to have two connection points – a head to connect to the previous letter and a tail to allow the following letter to be added on. These antivirals mimic one of the chemical letters but crucially lack the tail connection point. If the RNA polymerase mistakes the drug for the intended chemical letter and adds it to the growing RNA chain, the copying process stops because there is nothing to attach the next letter to. For this reason, this type of antiviral drug is called a chain-terminating inhibitor.

Viperin as antiviral producer

Previously, researchers thought that chain-terminating antiviral drugs were strictly a product of human ingenuity, developed from advances in scientific understanding of viral replication. However, the discovery that a protein in your cells named viperin synthesizes a natural chain-terminating antiviral has revealed a new side of your immune system.

Viperin works by chemically removing the tail connection point from one of the four RNA building blocks of a virus’s genome. This converts the building block into a chain-terminating antiviral drug.

This strategy has proved to be highly effective for treating viral infections. For example, the COVID-19 antiviral remdesivir works in this way. A viral RNA polymerase has to join together many thousands of letters to copy a virus’s genome, but an antiviral drug has to fool it only once to derail its copying. An incomplete genome lacks the necessary instructions to make a new virus and becomes useless.

Illustration of Remdesivir blocking a viral RNA polymerase from replicating RNA
Remdesivir (red, center) works by blocking a viral RNA polymerase (blue) from replicating RNA (violet and orange). Juan Gaertner/Science Photo Library via Getty Images

Moreover, although cells also have their own polymerases, they never replicate RNA like viruses do. This potentially allows chain-terminating antiviral drugs to selectively inhibit viral replication, reducing unwanted side effects.

Clearly, viperin does not fully protect against all RNA viruses – otherwise no RNA viruses would make you sick. It seems that some viral RNA polymerases, such as those in poliovirus, have evolved to discriminate against the antiviral molecules that viperin synthesizes and blunt their effect. However, viperin is only one arm of your immune system, which includes specialized cells and proteins that protect you from infection in other ways.

Ancient antivirals

Scientists discovered viperin about 20 years ago while searching for genes that turn on in response to viral infections. However, figuring out what viperin actually does proved very challenging.

Viperin’s function was particularly puzzling because it resembles an ancient group of proteins called radical SAM enzymes that are usually found in bacteria and molds. Notably, radical SAM enzymes are extremely rare in animals. Exposure to air rapidly inactivates them, and researchers thought they likely didn’t work in people. It’s still unclear how viperin avoids inactivation.

Diagram showing structure of viperin without (left) and with (right) an antiviral bound in its center. The structure with the antiviral is more tightly wound in its center.
This illustration shows the structure of viperin without (left) and with (right) an antiviral bound in its center. Soumi Ghosh and Neil Marsh/Journal of Biological Chemistry, CC BY-SA

Researchers were clued in to viperin’s function when they noticed that the gene coding for viperin is next to a gene involved in synthesizing one of RNA’s building blocks. This observation led them to examine whether viperin might modify this RNA building block.

Following this discovery, researchers identified viperinlike proteins across all kingdoms of life, from ancient bacteria to modern plants and animals. This meant that viperin is a very ancient protein that evolved early in life, probably well before the advent of multicellular organisms – because even bacteria must fight viral infections.

As more complex life forms evolved, viperin was retained and integrated into the complex immune systems of modern animals. Thus, this most recently discovered arm of your immune system’s defenses against viruses is likely the most ancient.

Neil Marsh, Professor of Chemistry and Biological Chemistry, University of Michigan

This article is republished from The Conversation under a Creative Commons license. 

Does chicken soup really help when you’re sick? A nutrition specialist explains what’s behind the beloved comfort food

A bowl of chicken soup typically contains protein, vegetables and soothing broth. Westend61 via Getty Images
Colby Teeman, University of Dayton

Preparing a bowl of chicken soup for a loved one when they’re sick has been a common practice throughout the world for centuries. Today, generations from virtually every culture swear to the benefits of chicken soup. In the U.S., the dish is typically made with noodles, but different cultures prepare the soothing remedy their own way.

Chicken soup as a therapy can be traced back to 60 A.D. and Pedanius Dioscorides, an army surgeon who served under the Roman emperor Nero, and whose five-volume medical encyclopedia was consulted by early healers for more than a millennium. But the origins of chicken soup go back thousands of years earlier, to ancient China.

So, with cold and flu season in full swing, it’s worth asking: Is there any science to back the belief that it helps? Or does chicken soup serve as just a comforting placebo, that is, providing psychological benefit while we’re sick, without an actual therapeutic benefit?

As a registered dietitian and professor of dietetics and nutrition, I’m well aware of the appeal of chicken soup: the warmth of the broth and the rich, savory flavors of the chicken, vegetables and noodles. What gives the soup that distinctive taste is “umami” – the fifth category of taste sensations, along with sweet, salty, sour and bitter. It is often described as having a “meaty” taste.

The notion that chicken soup is an elixir goes back centuries.

Improved appetite, better digestion

All that makes sense, because amino acids are the building blocks of proteins, and the amino acid glutamate is found in foods with the umami taste. Not all umami foods are meat or poultry, however; cheese, mushrooms, miso and soy sauce have it too.

Studies show that taste, it turns out, is critical to the healing properties of chicken soup. When I see patients with upper respiratory illnesses, I notice many of them are suddenly eating less or not eating at all. This is because acute illnesses ignite an inflammatory response that can decrease your appetite. Not feeling like eating means you’re unlikely to get the nutrition you need, which is hardly an optimal recipe for immune health and recovery from illness.

But evidence suggests that the umami taste in chicken soup may help spur a bigger appetite. Participants in one study said they felt hungrier after their first taste of a soup with umami flavor added in by researchers.

Other studies say umami may also improve nutrient digestion. Once our brains sense umami through the taste receptors on our tongues, our bodies prime our digestive tracts to absorb protein more easily.

This can reduce gastrointestinal symptoms, which many people experience when they’re under the weather. Although most people don’t associate upper respiratory infections with gastrointestinal symptoms, research in children has found that the flu virus increased abdominal pain, nausea, vomiting and diarrhea symptoms.

There are many ways to make chicken soup.

May reduce inflammation and stuffy nose

Inflammation is part of the body’s natural response to injury or illness; inflammation occurs when white blood cells migrate to inflamed tissue to assist with healing. When this inflammatory process occurs in the upper airway, it results in common cold and flu symptoms, such as a stuffy or runny nose, sneezing, coughing and thickened mucus.

Conversely, lower white blood cell activity in the nasal passages can reduce inflammation. And interestingly, research shows that chicken soup can in fact lower the number of white blood cells traveling to inflamed tissues. It does this by directly inhibiting the ability of neutrophils, a type of white blood cell, to travel to the inflamed tissue.

Key ingredients

To truly understand the soothing and healing effects of chicken soup, it’s important to consider the soup’s ingredients. Not all chicken soups are packed with nutritious healing properties. For instance, the ultraprocessed canned versions of chicken soup, both with and without noodles, lack many of the antioxidants found in homemade versions. Most canned versions of chicken soup are nearly devoid of hearty vegetables.

The core nutrients in homemade versions of the soup are what set these varieties apart from canned versions. Chicken provides the body with a complete source of protein to combat infection. Vegetables supply a wide array of vitamins, minerals and antioxidants. If prepared the American way, noodles provide an easily digestible source of carbohydrate that your body uses for energy and recovery.

Even the warmth of chicken soup can help. Drinking the liquid and inhaling the vapors increase the temperature of nasal and respiratory passages, which loosens the thick mucus that often accompanies respiratory illnesses. Compared with hot water alone, studies show chicken soup is more effective at loosening mucus.

The herbs and spices sometimes used in chicken soup, such as pepper and garlic, also loosen mucus. The broth, which contains water and electrolytes, helps with rehydration.

So, to maximize the health benefits of chicken soup, I recommend a homemade variety, which can be prepared with carrots, celery, fresh garlic, herbs and spices, to name a few ingredients. But if you need a more convenient option, look at the ingredients and nutrition facts label, and choose soups with a variety of vegetables over an ultraprocessed, nutrient-depleted kind.

In short, the latest science suggests that chicken soup – though not an out-and-out cure for colds and flu – really helps with healing. Looks like Grandma was right again.

Colby Teeman, Assistant Professor of Dietetics and Nutrition, University of Dayton

This article is republished from The Conversation under a Creative Commons license. 

A Full Menu of Festive Holiday Flavor

Cooking up a successful holiday gathering calls for everyone’s favorite recipes. From the centerpiece main dish to fresh salads and appetizers, roasted sides and baked sweets, you can take seasonal get-togethers up a notch by mixing traditional classics with newfound favorites.

Consider this full-fledged menu of flavor to give guests a memorable holiday experience from beginning to end and find more festive recipe ideas at Culinary.net.

Fresh Flavors for Holiday Festivities

With the festive season arriving, bring together family and friends for a delicious feast you can feel good about serving. One standout recipe is this Cornish Game Hen with Kale Sweet Potato Salad that pairs fresh, leafy kale with roasted sweet potatoes and tender Cornish game hens for a truly elegant meal.

Elevate your cooking during the holidays with inspiration from Fresh Express and its more than 100 varieties of fresh, healthy and convenient ready-to-eat salads like the Sweet Kale Chopped Kit. It’s a perfect blend of a nutrient-dense salad mix of leafy kale, green cabbage, shredded broccoli and Brussels sprouts, as well as crunchy pumpkin seeds and dried cranberries, topped with a tasty poppyseed dressing.

Visit FreshExpress.com to discover more fresh, easy and healthy recipes for the holiday season.

Cornish Game Hen with Kale Sweet Potato Salad

Prep time: 20 minutes
Cook time: 1 hour, 10 minutes
Servings: 4

  • 1 package (6 ounces) stovetop stuffing
  • 2 cups chopped apples, divided
  • 4 Cornish game hens (20 ounces each)
  • 1/2 cup butter
  • 2 teaspoons Italian seasoning, divided
  • 1 teaspoon paprika
  • 1 teaspoon salt, plus additional, to taste, divided
  • 1/2 teaspoon garlic powder
  • 1/4 teaspoon black pepper
  • 2 large sweet potatoes, peeled, cut into 1-inch cubes
  • 2 tablespoons olive oil
  • 1 package (10.9 ounces) Fresh Express Sweet Kale Chopped Kit
  1. Heat oven to 350 F.
  2. Prepare stuffing according to package directions. Add 1 cup apples and fluff stuffing with fork; cool 15 minutes.
  3. Remove anything inside hens, rinse cavity with cold water and pat dry.
  4. In small saucepan, melt butter over low heat. Add 1 teaspoon Italian seasoning, paprika, 1 teaspoon salt, garlic powder and pepper; mix well. Remove from heat.
  5. Fill cavity of each hen with apple stuffing.
  6. Place hens in 13-by-9-by-2-inch baking dish. Tie legs together and tuck wings under. Baste with butter mixture.
  7. Bake 50-60 minutes, or until thermometer inserted in thickest part of thigh reads 165 F and stuffing temperature reads 165 F. Baste with butter mixture every 15-20 minutes.
  8. In bowl, toss sweet potatoes with remaining Italian seasoning and olive oil. Arrange in single layer on sheet pan. Sprinkle with salt, to taste.
  9. Bake with hens 25 minutes, or until tender. Remove from oven and cool. Tent hens with foil and let rest 10 minutes.
  10. Place greens from salad kit in large bowl. Add remaining apples and sweet potatoes; mix well. Toss with salad dressing. Add toppings; toss to combine.
  11. Serve Cornish game hens with sweet potato kale salad.

A Festive, Everyday Side Dish

While the busy holiday season can be loads of fun, you still need to get dinner on the table between parties. When you find yourself in a pinch this holiday season, squeezed for time and searching for a quick solution for dinner, turn to an easy side dish that can appease everyone. Potatoes are a nearly unanimous favorite.

Make putting dinner on the table a breeze with a solution like little potatoes from The Little Potato Company, which can help bring holiday happiness to mealtime. Ready in as little as 5 minutes, they come pre-washed and require no peeling or cutting, making them the perfect time-saving solution for the holiday season.

Ideal for this Perfect Roasted Little Potatoes recipe, these little potatoes are a tasty, fresh whole food that you can feel good about serving. Ready in half an hour with minimal prep and a few simple ingredients, it’s a perfect side dish for any occasion.

Visit littlepotatoes.com for more information and holiday inspiration.

Perfect Roasted Little Potatoes

Prep time: 5 minutes
Cook time: 30 minutes
Servings: 6

  • 1 1/2 pounds The Little Potato Company Little Potatoes
  • 1 tablespoon vegetable oil
  • 1/2 teaspoon salt
  • 1/4 teaspoon pepper
  • 1-2 tablespoons fresh parsley, chopped
  1. Preheat oven to 400 F.
  2. In large bowl, toss little potatoes with oil, salt and pepper until coated.
  3. Spread potatoes in single layer on rimmed baking sheet lined with parchment paper. Bake 30 minutes, or until tender.
  4. Sprinkle with parsley and serve.

Tip: For extra holiday flavor, add paprika, garlic and fresh herbs.

Get Creative with Delicious, Decorative Cookies

A decadent holiday meal isn’t complete without a sweet dessert to cap off the evening. When in doubt, go with a traditional treat that’s perfect for sharing: cookies.

These Ornament Cookies can be shaped any way you like to celebrate the holidays. The royal icing adorning these festive favorites is made with powdered sugar and meringue powder; just use food coloring to add a personal touch.

For more than 120 years, Domino Sugar has helped millions bake special recipes like these cookies made with non-GMO, vegan, kosher and gluten-free Golden Sugar that’s free flowing and easy to scoop, spoon and pour. The sugar retains a hint of molasses flavor, giving it a golden color and providing a perfect way to add less processed sweetness to your loved ones’ favorite desserts.

Find holiday recipes, baking tips and more at dominosugar.com.

Ornament Cookies

Prep time: 25 minutes plus 1 hour to decorate
Cook time: 20 minutes
Yield: 2 dozen cookies

Cookies:

  • 1 1/2 cups (3 sticks) unsalted butter, at room temperature
  • 1 cup Domino Golden Sugar
  • 1 teaspoon pure vanilla extract
  • 1 large egg
  • 3 1/2 cups all-purpose flour
  • 1/4 teaspoon salt

Royal Icing:

  • 4 cups Domino Powdered Sugar
  • 3 tablespoons meringue powder
  • 1/3 cup, plus 2-3 tablespoons, warm water, divided
  • desired food coloring
  1. To prepare cookies: In large bowl, beat butter and sugar until light and fluffy. Add vanilla and egg; beat until well combined. Scrape sides of bowl as needed. Add flour and salt; beat until just combined.
  2. Dump mixture onto lightly floured surface and divide in half. Shape each half into disks and wrap with plastic wrap. Refrigerate 30 minutes.
  3. Preheat oven to 350 F. Line two baking sheets with parchment paper.
  4. Working on lightly floured surface, roll dough to 1/2-inch thick. Cut cookies using ornament-shaped cookie cutter. Place cookies on prepared pans and bake 18-20 minutes, or until golden brown. Remove from oven and cool at room temperature.
  5. To make royal icing: In large mixing bowl, combine powdered sugar, meringue powder and 1/3 cup water. Beat on low speed until combined. Increase speed to medium-high and beat 8-10 minutes, adding 2-3 tablespoons warm water, as necessary. Icing should be stiff enough to hold peak when tested.
  6. Color royal icing with food coloring and decorate cookies.

 

SOURCE:
Fresh Express
Little Potato Company
Domino Sugar
 

Sunday, October 22, 2023

Tex-Mex Sweetpotato Beef Skillet

For busy families, it’s hard to beat a one-skillet dish that cuts down on cleanup without sacrificing flavor. Especially during the hectic fall season when cool, crisp days call for comforting food, you can warm up the evening with a hot Tex-Mex meal that’s sure to occupy a permanent spot on the menu.

Start with a versatile comfort food staple like sweetpotatoes, which provide the body for this filling Tex-Mex Sweetpotato Beef Skillet. As a versatile veggie that’s easy to add to a variety of recipes for enhanced flavor and nutrition content, they can become a pantry must in your home for simple and elevated recipes alike. To maximize their already-lengthy shelf life (up to 4 weeks), simply store in a cool, dry, well-ventilated area away from heat sources – never in the refrigerator, which can cause “chill damage.”

Because they can be cooked and prepared in a skillet, baked, grilled, slow-cooked, microwaved, air-fried and more, they provide a crowd favorite that’s a breeze to use in the kitchen. In this delicious dish, they’re combined with peppers, onions, ground beef, broth, tomatoes, corn, Southwest seasoning and more to keep chilly days at bay.

Consider this fun fact to share with your loved ones at the dinner table: The one-word spelling of “sweetpotato” was officially adopted by the National Sweetpotato Collaborators in 1989 to avoid confusion with equally unique and distinctive potatoes, which are also grown and marketed commercially in the United States.

Find more comfort food favorites by visiting ncsweetpotatoes.com.

Watch video to see how to make this recipe!


Tex-Mex Sweetpotato Beef Skillet

Recipe courtesy of Meredith Bernard of “This Farm Wife” on behalf of the North Carolina Sweetpotato Commission

Servings: 6

  • 2          medium sweetpotatoes
  • 3          bell peppers (combination of red, yellow and orange)
  • 1          small onion
  • 2          tablespoons olive oil or butter, divided
  • 2          garlic cloves, minced
  • 1          pound lean ground beef
  • 1/2       cup beef broth
  • 1          can diced tomatoes
  • 8          ounces tomato sauce
  • 1          can Mexi-corn or Southwest corn
  • 1          tablespoon Southwest seasoning
  • salt, to taste
  • pepper, to taste
  1. Rinse and scrub sweetpotatoes to clean. Chop into 1/2-inch cubes. Dice bell pepper and onion. Set aside.
  2. In skillet over medium heat, heat 1 tablespoon oil or butter.
  3. Add garlic and saute until fragrant, being careful not to burn.
  4. Add ground beef, breaking apart and stirring until cooked through, 5-7 minutes. Remove garlic and beef to covered bowl or plate; set aside.
  5. In same skillet, add remaining oil or butter. Saute peppers, onion and sweetpotatoes until slightly tender.
  6. Pour in broth, diced tomatoes and tomato sauce; cover and simmer 12-15 minutes.
  7. Stir in cooked beef and corn. Cook until liquid reduces and mixture thickens slightly. Add seasoning and salt and pepper, to taste.
SOURCE:
North Carolina Sweetpotato Commission

House speaker paralysis is confusing – a political scientist explains what’s happening

Jim Jordan, center, has been working feverishly to line up support for his speakership. AP Photo/J. Scott Applewhite
Charles R. Hunt, Boise State University

Political observers, most Americans and even members of Congress can’t remember a battle for the post of speaker of the U.S. House as fraught as the one that began back in January 2023 and continues still, 10 months later.

On Jan. 7, California Republican Rep. Kevin McCarthy finally became speaker after 15 rounds of voting. But on Oct. 3, he was ousted. On Oct. 17 and again on Oct. 18, Ohio Republican Jim Jordan came up short in two rounds of voting to replace McCarthy.

The reason it’s so hard to recall a parallel is that there isn’t one – at least not since the 1850s, which saw a fight over the speakership that took nearly two months and 133 rounds of voting.

Along with all manner of other inauspicious “firsts” in American politics over the last few years – a violent attempt to overturn a presidential election in the halls of Congress and a former president being indicted for the attempt, to name just two – the century-long tradition of House speakers being quickly and unanimously elected by their party has been similarly blown to pieces.

It can be hard to understand what’s going on. But as a political scientist who co-authored a textbook called “Congress Explained,” I have an obligation to give it my best shot. Here are three of the most revealing elements of the ongoing speaker kerfuffle, and how political science can help people – including me – understand them.

1. Jordan’s attempts to win over his conference

For a member of Congress with a reputation as a far-right “attack dog,” Jordan has spent a lot of the past few days on what congressional experts like to call “herding cats” – leaders getting their rank-and-file party members in alignment for a vote, even when many of those members want different things.

To get members to go their way, party leaders in Congress frequently use a combination of offers and threats. They can, for example, offer rank-and-filers desired committee assignments or attention to their pet issues.

Alternatively, they can encourage – implicitly or explicitly – someone to challenge the member in a primary, or withhold fundraising support, which is a main responsibility of party leadership. So far, Jordan appears to have favored this more aggressive approach in what The New York Times called a “pressure campaign” to round up support from moderate members still unsure about him.

Whether the pressure tactics end up being enough for Jordan to become speaker is an open question. But if he does win the gavel, he’ll need to work even harder to win over his colleagues for impending budget negotiations and to deal with international crises in the Middle East and Ukraine. And fundraising promises or threats may not be enough.

2. The votes cast for non-Jordan Republicans

In a first round of voting on Oct. 17, Jordan fell short of the majority required to become speaker of the house. Not surprisingly, no Democrats backed him. But he also faced 20 Republican holdouts. Even more Republicans voted for someone else on Oct. 18. And those holdouts didn’t all vote for the same person. Who they did vote for can reveal a lot about the internal dynamics in the Republican Party.

Most of the Republican holdouts voted for either McCarthy or House Majority Leader Steve Scalise of Louisiana, who as recently as last week was touted as McCarthy’s heir. Those members have been extensively quoted as having major problems not just with Jordan as a potential speaker but with the chaos introduced to the broader legislative process by far-right members like Jordan ally Florida Rep. Matt Gaetz.

Several Republicans from the New York delegation voted for someone who had first appeared to be a bit of a head-scratcher: New York Republican Lee Zeldin, who is no longer a member of Congress.

Although Zeldin – or any other person, even if they are not a member of the House – can be elected speaker under House rules, the votes cast in his direction were purely symbolic. But they were also telling.

These New York Republican representatives, many of whom come from districts won by Democratic President Joe Biden, are sending the message that they and other Republicans elected in competitive districts are the only reason Republicans have a majority in the House at all. They have a point: There is significant evidence that in the 2022 election, farther right candidates, particularly those who denied the outcome of the 2020 election, were less popular with voters than their moderate counterparts – and almost cost Republicans the House majority.

The votes for Zeldin, therefore, are a warning to fellow Republicans from the moderates in New York, insisting they not be taken for granted.

3. The floor action of Congress’ most extreme members

C-SPAN is not known for its exciting television, but political observers on Tuesday afternoon were treated to a few dramatic moments that – aside from their entertainment value – are emblematic of some of the larger dysfunction and political dynamics that have come to define both parties in recent years.

One instance came during California Democrat Pete Aguilar’s Oct. 17 nomination speech for Democratic speaker candidate Hakeem Jeffries of New York, in which Aguilar noted that Jordan has yet to pass a bill out of the chamber since 2007, when he was first sworn in.

California Democrat Pete Aguilar nominates Hakeem Jeffries and criticizes Jim Jordan.

In response, far-right Republican members Gaetz and Lauren Boebert of Colorado reportedly applauded.

According to the research, Aguilar is not wrong about Jordan’s reputation: The Center for Effective Lawmaking, an academic research center out of Vanderbilt University, ranks Jordan near the bottom of his Republican conference on a whole battery of figures measuring legislative effectiveness.

That doesn’t mean that Jordan can’t be an effective speaker. But the willingness of the party to nominate someone with such a thin record of achievement – and Gaetz’s and Boebert’s open enthusiasm for the comment about Jordan’s lack of action – is a monument to the increasingly obstructionist politics that continue to plague Congress.

Charles R. Hunt, Assistant Professor of Political Science, Boise State University

This article is republished from The Conversation under a Creative Commons license. 

Saturday, October 21, 2023

Comets 101 − everything you need to know about the snow cones of space

Comet Hale-Bopp was visible from Earth in 1997. E. Kolmhofer, H. Raab; Johannes-Kepler-Observatory, Linz, Austria, CC BY-NC
Shannon Schmoll, Michigan State University

When you hear the word comet, you might imagine a bright streak moving across the sky. You may have a family member who saw a comet before you were born, or you may have seen one yourself when comet Nishimura passed by Earth in September 2023. But what are these special celestial objects made of? Where do they come from, and why do they have such long tails?

As a planetarium director, I spend most of my time getting people excited about and interested in space. Nothing piques people’s interest in Earth’s place in the universe quite like comets. They’re unpredictable, and they often go undetected until they get close to the Sun. I still get excited when one comes into view.

What exactly is a comet?

Comets are leftover material from the formation of the solar system. As the solar system formed about 4.5 billion years ago, most gas, dust, rock and metal ended up in the Sun or the planets. What did not get captured was left over as comets and asteroids.

Because comets are clumps of rock, dust, ice and the frozen forms of various gases and molecules, they’re often called “dirty snowballs” or “icy dirtballs” by astronomers. Theses clumps of ice and dirt make up what’s called the comet nucleus.

A diagram showing comet nuclei, which look like gray rocks, of progressively larger sizes.
Size comparison of various comet nuclei. NASA, ESA, Zena Levy (STScI)

Outside the nucleus is a porous, almost fluffy layer of ice, kind of like a snow cone. This layer is surrounded by a dense crystalline crust, which forms when the comet passes near the Sun and its outer layers heat up. With a crispy outside and a fluffy inside, astronomers have compared comets to deep-fried ice cream.

Most comets are a few miles wide, and the largest known is about 85 miles wide. Because they are relatively small and dark compared with other objects in the solar system, people can’t see them unless the comet gets close to the Sun.

Pin the tail on the comet

Starry sky with a comet in the mid left portion of the image and a tree in the foreground
Comet Hale-Bopp as seen from Earth in 1997. The blue ion tail is visible to the top left of the comet. Philipp Salzgeber, CC BY-ND

As a comet moves close to the Sun, it heats up. The various frozen gases and molecules making up the comet change directly from solid ice to gas in a process called sublimation. This sublimation process releases dust particles trapped under the comet’s surface.

The dust and released gas form a cloud around the comet called a coma. This gas and dust interact with the Sun to form two different tails.

The first tail, made up of gas, is called the ion tail. The Sun’s radiation strips electrons from the gases in the coma, leaving them with a positive charge. These charged gases are called ions. Wind from the Sun then pushes these charged gas particles directly away from the Sun, forming a tail that appears blue in color. The blue color comes from large numbers of carbon monoxide ions in the tail.

The dust tail forms from the dust particles released during sublimation. These are pushed away from the Sun by pressure caused by the Sun’s light. The tail reflects the sunlight and swoops behind the comet as it moves, giving the comet’s tail a curve.

The closer a comet gets to the Sun, the longer and brighter its tail will grow. The tail can grow significantly longer than the nucleus and clock in around half a million miles long.

Where do comets come from?

All comets have highly eccentric orbits. Their paths are elongated ovals with extreme trajectories that take them both very close to and very far from the Sun.

Comets’ orbits can be very long, meaning they may spend most of their time in far-off reaches of the solar system.

An object will orbit faster the closer it is to the Sun, as angular momentum is conserved. Think about how an ice skater spins faster when they bring their arms in closer to their body – similarly, comets speed up when they get close to the Sun. Otherwise, comets spend most of their time moving relatively slowly through the outer reaches of the solar system.

A lot of comets likely originate in a far-out region of our solar system called the Oort cloud.

The Oort cloud is predicted to be a round shell of small solar system bodies that surround the Earth’s solar system with an innermost boundary about 2,000 times farther from the Sun than Earth. For reference, Pluto is only about 40 times farther.

Sphere of small particles with a disk like structure in the middle. A tiny rectangle in the center points to a zoomed in image of the Sun and planet orbits
A NASA diagram of the Oort cloud’s structure. The term KBO refers to Kuiper Belt objects near where Pluto lies. NASA

Comets from the Oort cloud take over 200 years to complete their orbits, a metric called the orbital period. Because of their long periods, they’re called long-period comets. Astronomers often don’t know much about these comets until they get close to the inner solar system.

Short-period comets, on the other hand, have orbital periods of less than 200 years. Halley’s comet is a famous comet that comes close to the Sun every 75 years.

While that’s a long time for a human, that’s a short period for a comet. Short-period comets generally come from the Kuiper Belt, an asteroid belt out beyond Neptune and, most famously, the home of Pluto.

There’s a subset of short-period comets that get only to about Jupiter’s orbit at their farthest point from the Sun. These have orbital periods of less than 20 years and are called Jupiter-family comets.

Comets’ time in the inner solar system is relatively short, generally on the order of weeks to months. As they approach the Sun, their tails grow and they brighten before fading on their way back to the outer solar system.

But even the short-period comets don’t come around often, and their porous interior means they can sometimes fall apart. All of this makes their behavior difficult to predict. Astronomers can track comets when they are coming toward the inner solar system and make predictions based on observations. But they never quite know if a comet will get bright enough to be seen with the naked eye as it passes Earth, or if it will fall apart and fizzle out as it enters the inner solar system.

Either way, comets will keep people looking up at the skies for years to come.

Shannon Schmoll, Director of the Abrams Planetarium, Michigan State University

This article is republished from The Conversation under a Creative Commons license. 

The living things that feast on plastic

Scientists are scouring garbage sites around the world for bacteria, fungi and even insects that harbor enzymes that could be harnessed for breaking down various polymers. It’s early days, but if the efforts can be efficiently scaled-up, such biological recycling could put a dent in the plastic waste problem.

On an overcast spring morning in 2012, Federica Bertocchini was tending to her honeybees close to where she lived in Santander, on Spain’s picturesque northern coast. One of the honeycombs “was plagued with worms,” says the amateur apiarist, referring to the pesky larvae of wax moths that have a voracious — and destructive — appetite.

Bertocchini picked out the worms, placed them in a plastic bag, and carried on with her beekeeping chores. When she retrieved the bag a few hours later, she noticed something strange: It was full of tiny holes.

The scientist’s interest was piqued. Had the hungry worms simply chewed up the plastic, or had they changed its chemical makeup too? Quick tests in her lab confirmed, surprisingly, the latter: Something in the worms’ saliva had degraded the plastic. “From that point, the research started,” says Bertocchini, a developmental biologist formerly with the Spanish National Research Council.

She is now the cofounder of Plasticentropy — one of the numerous startups and research groups that have sprouted in recent years seeking bio-inspired means to recycle plastic. This biological recycling, as it’s called, could offer more effective and environmentally friendly alternatives to some of today’s problem-riddled recycling methods.

The effort has scientists scouring landfills, auto wrecking yards and other sites teeming with plastic pollution in search of organisms that might be able to break down plastic into its component pieces. By taking these microbes and enhancing their polymer-munching abilities in the lab, scientists hope to find an efficient way of reclaiming the building blocks of plastics. They would then use these subunits to manufacture new materials, thus creating an “infinite recycling” loop.

It’s early days, and finding enzymes fit for the task is just a first step. But biological recycling could be a valuable tool for fighting the ever-growing plastics problem.

“There are groups all over the world working on this — hundreds of groups, thousands of scientists — it’s really quite amazing,” says structural biologist John McGeehan, a consultant in plastics deconstruction who specializes in the discovery and engineering of enzymes for plastic recycling.

Recycling woes

These efforts could not come soon enough. Ever since plastics manufacturing began in earnest in the 1950s, production has soared. Estimates suggest that we make close to 460 million tons of plastic annually, equivalent to the weight of roughly 2.3 million blue whales.

Unfortunately, most of that plastic ends up burned, buried in landfills or dumped in the environment. It’s no wonder that plastic has penetrated every corner of our planet — from the deep oceans to both poles, it even comes down in the rain. It’s also in our bodies, with traces reported in placentas, breast milk and human blood; the use and disposal of plastics has been linked with several health and environmental issues.

Despite these problems, demand remains unabated, with production forecast to hit more than 1,000 million tons by 2050. That’s largely because plastics are hard to substitute — the material is a manufacturer’s delight: lightweight and easy to shape, with near-endless possibilities of properties it can be imbued with.

Given that replacing all plastics isn’t realistic, a next-best option is to make less virgin material from fossil fuels and to recapture more of what already exists. In other words, raise global plastic recycling rates from their present, dismal figure of roughly 9 percent.

The reasons behind that low rate are plentiful: Plastic is tough to break down; it can absorb harmful chemicals in the recycling process; and there are thousands of plastic types, each with its own composition, chemical additives and colorants. Many of these types cannot be recycled together.

“We have this major plastics circularity problem,” says Johan Kers, a synthetic biologist and cofounder of the Oregon-based enzymatic recycling company Birch Biosciences. “We can recycle aluminum; we can recycle paper; but we cannot, to save our lives, do a good job of recycling plastic.”

Nature offers a blueprint

Biological recycling could put a dent in the plastics problem. It involves using enzymes — the workhorses of biochemistry that speed up reactions — to break down plastic polymers into their subunits, called monomers. These monomers can then be used to make new plastics.

“The nice thing about enzymes is you get the building blocks back,” says McGeehan. “That’s potentially an infinite process, so it’s really attractive.”

This approach could turn used plastics into a valuable resource, instead of a source of waste, says Ting Xu, a polymer scientist at the University of California, Berkeley, who cowrote an overview of biological-synthetic hybrid materials in the 2013 Annual Review of Physical Chemistry.

Research on plastic-eating enzymes goes back to at least the 1970s, but the field was reinvigorated in 2016, when a team of Japanese scientists published a landmark paper in Science describing a new strain of plastic-eating bacteria. Led by microbiologist Kohei Oda at the Kyoto Institute of Technology, the team found that the microbe, called Ideonella sakaiensis 201-F6, uses PET plastic — a polyester widely used in beverage bottles and fibers — as its major energy and food source.

The researchers came across the microbe in some scooped-up sediment when they were painstakingly shifting through 250 environmental samples they had collected from a bottle-recycling factory just outside of Osaka. Further testing revealed that I. sakaiensis could almost fully break down PET within six weeks.

Since then, scientists have discovered plastic-eating microbes at various sites around the world, including a compost heap at a cemetery in Leipzig, Germany; a waste disposal site in Pakistan’s capital, Islamabad; and weathered debris washed up on two beaches in Chania, Greece. A large-scale analysis of more than 200 million genes found in free-floating DNA in environments including the oceans, Arctic tundra topsoil, savannas and various forests turned up 30,000 different enzymes with plastic-degrading potential, a team reported in 2021.

Discovering enzymes, however, is only the first step. While many of the ones now under study are quick-acting and function well under mild conditions, scientists typically have to tweak them to perform better. For example, McGeehan, along with colleagues at the National Renewable Energy Laboratory in Colorado and elsewhere, engineered two enzymes responsible for the plastic-eating abilities of I. sakaiensis to dial up their performance and then linked them, creating an enzyme cocktail that can break down PET six times quicker than previously possible.

Scientists are also using artificial intelligence to dial up desirable attributes in the enzymes that depolymerize plastics quicker, are less picky about target substrates, and can withstand a wider range of temperatures.

Early data suggest that biological recycling could have a smaller carbon footprint than making plastics anew. For example, using enzymes to break down PET to get one of its monomers, terephthalic acid (TPA), cut greenhouse gas emissions by as much as 43 percent compared with making TPA from scratch, according to a 2021 estimate.

Good targets for enzymes

Of course, PET is just one of many kinds of plastic — they are generally divided into seven or more classes, depending on factors like their chemical structure. On one end of the scale sit plastics with mixed-carbon backbones — polymers with a central spine comprising carbon interlaced with other atoms such as oxygen and nitrogen. For now, these plastics are most suited to biological recycling largely because the enzymes available can chew through the type of chemical bond in that mixed carbon backbone. It’s “a kind of Achilles’ heel” for the material says Andy Pickford, a molecular biophysicist at the University of Portsmouth in the United Kingdom.

PETs have such a backbone — in this case, carbon interlaced with oxygen. Commonly found in textiles and soda bottles and accounting for roughly one-fifth of plastics created every year, PETs are a popular first target among biological recyclers and the closest to implementation at a commercial scale. The French firm Carbios, for example, plans to open a bio-recycling plant in northern France in 2025, with the aim of recycling 50,000 tons of PET waste annually.

The company is using a proprietary enzyme first identified in a pile of compost that researchers then modified to enhance its PET-bond-breaking ability and to withstand the higher temperatures at which the plastic becomes molten and soft. The enzyme can depolymerize 90 percent of PET in 10 hours, scientists from Carbios and its academic partner, the Toulouse Biotechnology Institute, reported in Nature in 2020.

Another startup, Australia-based Samsara Eco, plans to launch a similar 20,000-ton facility in Melbourne in 2024 that will also focus on PET.

Plastics with a similar chemical makeup to PET, the polyamides and polyurethanes, are also promising targets for enzymatic recycling, as they are intrinsically susceptible to breakdown by enzymes, says Pickford, whose team at Portsmouth works on all three plastic types.

In addition to PET, Samsara now works on nylon, a type of synthetic polyamide commonly found in fabrics and textiles. In May, the firm announced a multiyear partnership with popular athletic brand Lululemon to produce “the world’s first infinitely recycled” nylon-polyester apparel from discarded clothes.

Researchers are also investigating polyurethanes, which comprise roughly 8 percent, or 25 million tons, of the global plastics pie and are common in foams such as furniture cushions and in diapers, sponges and sneakers. Various microbes can degrade some kinds of polyurethanes and Kers’ team at Birch Biosciences has zeroed in on some 50 different polyurethane-eating enzymes for testing, but the polymers are a structurally diverse group and will probably require diverse strategies.

Some tougher problems

While enzymatic recycling looks promising for plastics with mixed backbones, the outlook isn’t as rosy for those at the other end of the scale: plastics with backbones of pure carbon. This is an eclectic group that includes polyvinyl chloride (PVC), polyvinyl alcohol (PVA), polystyrene and polyethylene, which is used to make the ubiquitous plastic bag. Biological recycling of these plastics is far more challenging, says Pickford. “They’re kind of greasy, in a way, for enzymes. There’s not really much for an enzyme to grab hold of.”

Still, some scientists are working on these recalcitrant plastics — among them, Spain’s Bertocchini. “For some reason, I fixed on plastic bags, which are polyethylene-based,” she says. Also commonly used in food packaging film and takeout containers, polyethylene is by far the largest class of plastics manufactured today, accounting for more than 25 percent of the market. A decade on from their serendipitous discovery, Bertocchini and her team at Plasticentropy have identified the plastic-degrading enzymes in wax worm saliva — and have named them Demetra and Ceres. The enzymes degrade polyethylene within a matter of hours at room temperature by introducing oxygen into the carbon backbone.

Enzymes found in insects may hold the key for these tougher plastics. Microbiologist Chris Rinke at the University of Queensland in Australia, who works on polystyrene, commonly found in takeout food containers and disposable cutlery, is among the scientists looking at insect larvae, which have tough mouthparts that make them “very good at chewing through things” and breaking them down into smaller particles. “Then the microbes in the guts take it from there,” Rinke says.

Rinke came across the larva of a beetle called Zophobas morio — dubbed the Superworm — that breaks down polystyrene via a twofold process: mechanically shredding the plastic into smaller pieces, which “ages” it by introducing oxygen atoms, and then depolymerizing those bits using special bacterial gut enzymes that have yet to be identified.

But some experts are less optimistic about the outlook for biological recycling — especially for tackling plastics with harder-to-break backbones. “I’ve yet to be convinced that polyolefins like polyethylene and polypropylene and PVC will ever be realistic targets for enzymatic recycling at scale,” says Pickford. “There have been some interesting observations but converting those into an industrial process is going to be extremely difficult. I hope I’m wrong.”

There are hints of progress for PVC, but for now the brittle plastic, along with its cousins PVA and polylactic acid (PLA), remains largely unconquerable by enzymes. For such cases, it might be more feasible to shift toward creating new plastics that are recyclable, says Pickford.

Yet the findings keep coming: In 2020, a team from South Korea reported on a gut bacterium, Serratia fonticola, that conferred polystyrene-digesting abilities to the larvae of a black beetle called Plesiophthalmus davidis. Another group reported finding two cold-adapted fungal strains — Lachnellula and Neodevriesia, isolated from alpine soil and the Arctic shore, respectively — that could break down certain types of biodegradable plastic, including PLA.

Still, enzymes are only part of the battle. It’s unclear how easy it would be to scale up processes that harness these enzymes and what that scaled-up environmental footprint might look like.

“I think there’s never going to be one solution to all this,” says Vanessa Vongsouthi, head of protein engineering and research founder at Samsara Eco. “We have to work on advanced recycling, but in addition to that, policy, product redesign, reuse and even elimination … are all part of the bigger picture.”

Some policy changes are in the works. The United Nations is set to create the world’s first global plastic pollution treaty in 2024. It is aimed at curbing plastic pollution, and is expected to introduce new rules for production and the design of plastic products to make recycling easier, among other measures. And in the following year, laws mandating that 25 percent of the material in plastic containers and beverage bottles be recycled plastic will kick in in Washington, California and the European Union. But without additional changes and incentives, those efforts may be a drop in the bucket. As long as virgin plastic remains cheap due to the low price of fossil fuels, biological enzymes might not be able to compete.

“The main problem is cost,” says McGeehan. “Fossil-derived plastics are really cheap because they’re made at huge scale on a global market that’s very mature.” It also doesn’t help that some governments still incentivize producing plastics in this way, he says. “We need to really switch our thinking there and start incentivizing the PET or the other biodegradable processes in the way that the oil and gas industry benefited from in the past.”

McGeehan remains optimistic that once the technology for biological recycling improves, it will quickly become cost-efficient enough to compete with virgin plastic. Until then, researchers like Bertocchini will keep plugging away. She gave up her beloved beehives when she moved to Madrid in 2019, but today continues to expand her firm’s enzyme portfolio with moth and butterfly larvae. Enzymes will not solve the entire plastics problem, she says — “but this is a start.”

Editor’s note: This story was updated on August 25, 2023, to clarify that enzymes from insects that help break down certain plastics could be microbial in origin.

This article originally appeared in Knowable Magazine, an independent journalistic endeavor from Annual Reviews.