The plastic that biodegrades in your home compost

This episode explores new biodegradable plastics that can decompose in home composting conditions, a significant step forward in managing plastic waste sustainably.

1. Biodegradable plastics can now decompose in home compost conditions within 26 weeks.
2. Embedding specialized enzymes into PLA is key to lowering the temperature required for biodegradation.
3. The development faced challenges, such as maintaining enzyme activity during the high-temperature plastic production process.
4. This innovation could significantly reduce the environmental impact of plastic waste.
5. The episode emphasizes the importance of sustainable material science in addressing global waste issues.

1: Introduction

Hosts introduce the topic and discuss the significance of biodegradable plastics. Emily Bates: "It's absolutely fantastic to be here, looking forward to discussing sustainable plastics."

2: Biodegradable Plastic Innovations

Discussion on how embedded enzymes can help PLA plastics decompose at lower temperatures. Matthew Gibson: "We tackled this with a gel that slows down protein interactions, preventing aggregation."

3: Challenges in Plastic Production

Exploration of the technical challenges in embedding enzymes into PLA. Isabel Andre: "We had to engineer the enzyme to withstand the production process's high temperatures."

4: Future Implications

Consideration of how this technology could change plastic production and disposal. Alan Marty: "This represents a revolution in how we manage plastic waste, aiming to replace non-biodegradable options like polyethylene."

1. Opt for products packaged in biodegradable plastics when available.
2. Support companies and initiatives that invest in sustainable packaging technologies.
3. Educate others about the benefits of compostable plastics.
4. Consider setting up a home compost system to manage biodegradable waste.
5. Stay informed about advancements in biodegradable materials and environmental sustainability.

A gel that encases proteins could be a new way to safely transport medicines without requiring them to be kept cold, according to new research. To test it, the team behind the work posted themselves a protein suspended in this gel, showing that it was perfectly preserved and retained its activity, despite being dropped in transit and exposed to varying temperatures. The researchers hope this gel will help overcome the need to freeze protein-based medicines, which can be expensive to do and difficult to maintain during transportation.

People

Matthew Gibson, Isabel Andre, Alan Marty, Ting Xu

Companies

Carbios, University of Toulouse

Books

Leave blank if none.

Guest Name(s):

Alan Marty, Isabel Andre, Ting Xu

Content Warnings:

None

Nature Podcast
The Nature podcast is supported by Nature Plus, a flexible monthly subscription that grants immediate online access to the science journal Nature and over 50 other journals from the Nature portfolio.

More information at go dot nature.com.

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Plus, we all belong outside. We're drawn to nature. Whether it's the recorded sounds of the ocean we doze off to or the succulents that adorn our homes, nature makes all of our lives, well, better. Despite all this, we often go about our busy lives removed from it. But the outdoors is closer than we realize. With alltrails, you can discover trails nearby and explore confidently with offline maps and on trail navigation. Download the free app today and make the most of your summer with alltrails.

Benjamin Thompson
In an experiment.

Emily Bates
Why is light so far like it.

Nature
Sounds so simple, but now the data. I find this not only refreshing, but at some level, astounding.

Nature.

Benjamin Thompson
Welcome back to the Nature podcast. This week, a protective gel that lets.

Emily Bates
You post proteins and a plastic that you can compost at home. I'm Emily Bates.

Benjamin Thompson
And I am Benjamin Thompson.

First up, then this week, I just wanted to introduce Emily Bates. You might have heard her reading the research highlights last week, but Emily is here to host the show for the first time. Emily, hi.

Emily Bates
Hello Ben. How are you doing?

Benjamin Thompson
I am doing a ok. It's great to have you with us in the hosting chair for the first time.

Emily Bates
Absolutely fantastic to be here. Looking forward to it.

Benjamin Thompson
Excellent. Well, let's start with our first story this week, which seems like the right place to do so. And we're all used to the idea of reaching into the fridge when we want milk for our tea or opening the freezer when we want some peas for our dinner. Now, these technologies help us store food for longer so it's still fresh when we want it. And the same thing applies to many of our modern medicines. Protein based therapeutics like insulin or antibodies used to treat cancer are often frozen or freeze dried to keep them in optimum condition for when they reach their destination.

But while these methods are effective, they can be expensive, time consuming, and not conducive to low resource settings. But this week in nature, researchers are presenting an alternative way to get these vital proteins where they need to go, a gel that can store them that is quick, simple, and cheap.

Reporter Anand Jagatia spoke to one of the paper's authors, Matthew Gibson, about the research and started by asking him to explain what goes wrong with proteins if they aren't stored properly.

Matthew Gibson
Protein isn't alive. It's essentially a big macromolecule piece of spaghetti. If you like that folds itself into a structure that then gives the function which we all know proteins can perform.

So really it was about how do you stop them from unfolding, but in particular, how do you stop them from aggregating?

So one protein on its own will normally function, but when they start to stick together with themselves, you find that they lose a bit of their activity, or they become insoluble, and this is made worse by shaking them. So one of the most famous examples of this is in insulin. When you prepare it, if you shake it vigorously, that actually promotes this aggregation.

Nature
I think people will probably remember from the pandemic that there was a lot of talk about cold chain technology, or cold chain management, and that it's not enough to create a vaccine, or could be a protein or an antibody or whatever, you have to be able to store it and transport it. And so we do have ways of doing that. But it's difficult, isn't it?

Matthew Gibson
Yeah, so the cold chain works really well.

The example in Covid was the mRNA vaccines, for example, so not proteins. So a bit of an aside from what we've done, one of the things when they first emerged was how everyone had planned for them to be delivered in -80 degrees C freezes.

So these use an awful lot of energy. So your one -80 degrees C freezer can use as much as, say, someone who's living in a small house on their own.

Nature
So freezing proteins comes with considerable energy costs. Are there any other downsides to the way that we currently store proteins and other molecules?

Matthew Gibson
Yeah, so the freeze thaw process itself is pretty strenuous. Once frozen, things store well, but getting down to temperature and get it up to temperature is where an awful lot of the damage can occur. On some proteins, if you freeze thaw them, you do get some aggregation. But really the other really good way for storing proteins is freeze drying. So a bit like with freeze dried coffee, remove all the water, and then you got a nice stable solid powder. It's a solid protein, and that's not what goes into someone. So you've got to crack open the liquid, get that into the solid, and you've got to dissolve it, and you've got to follow those instructions. So this is where we're wondering, what other technologies can we bring to it, which are as universally useful as some of the freeze drying and freezing methods, but are really, really simple, but have the benefit, where the user doesn't have to decide how concentrated it would be by mixing different components together.

Nature
What was your approach then? How did you decide to tackle this problem.

Matthew Gibson
So the way we tackled this was with our collaborators at Glasgow University, professor David Adams. He's really an expert on making gelatinous molecules. So what we mean by this gelato, small molecules, when you put them in the right conditions, they sort of stick together and they form these big networks, and that stops the movement and it becomes a gel, a bit like a gel. So by slowing down the molecular motions within the gel, the proteins won't come across each other, and then we can switch off the aggregation.

Nature
So if I sort of try and scale this up by analogy to, like, human level, if me and you were sort of floating around in a big, like, swimming pool of jelly or gel, it would be quite difficult for us to move through it and to reach each other, and so we'd kind of just be stuck separate. Is that kind of what's happening with the gel and the proteins?

Matthew Gibson
Exactly. So if we're in a normal swimming pool, if we just swam at random, we're going to run into each other eventually. If you and I try and swim in some jelly, it would take us a while to run into each other and the frequency of that would be significantly decreased. But, of course, then we've got the problem. We're going to want to get out of the swimming pool at some point.

Nature
So how do you get the proteins out of the gel, then? How did you solve the second issue?

Matthew Gibson
These gels, they have a unique property in that we'd say they're quite stiff, they're almost a bit brittle. When we push the gel out of a syringe with a small filter on the end, we sort of shatter the internal network of the gel. And as you push, none of the gel came out of the syringe. So all we got was pure protein in the salts and buffer.

Nature
So how did you actually go about testing the performance of these storage gels, and how well did they do at protecting the proteins?

Matthew Gibson
We took an enzyme, it's called beta galactozidase. We actually showed that if we even heat it up to 50 degrees c, we retain some of that protein function.

And we also stored some insulin. We showed that when it's in our gel, if you shake it at 600 revolutions per minute, insulin that comes out is not aggregated. The experiment we were most proud of was we put a temperature tracker in with one of our gels, and we thought we'd subject it to a random test. So we just used the post. So we put these things in the post and sent them back to ourselves to collect them. We could see it's been through quite a range of temperatures. It's probably been dropped.

Benjamin Thompson
Right.

Matthew Gibson
We got dropped into a post box and the protein we recovered was perfect. So that was the thing which made us most confident this worked.

Nature
Now you've done the proof of concept. What's next for your lab in terms of getting these gels tweaked and finalized and potentially out into the real world?

Matthew Gibson
We can change the structure of the gels a lot. So we are looking a little bit to really make sure we're on the optimum gel and that we can use this in as many different types of protein as possible. So that's the first thing which we're really having to check also the long term. So how far can we go? Is this for something that you might want to bank for six months, or is it three or four years?

Nature
And one of the potential areas where this could be really impactful is in low resource settings, you know, countries that, where they don't really have reliable electricity, there's no way they're going to be able to keep a -80 degree fridge running constantly. And often they're the places where you need to send some of these therapeutic molecules.

Matthew Gibson
This is really where we want to be looking at. So are there protein vaccines which would respond really well in our scenario, so they can be all dosed and metered at production, and then when they're sent to their final location, you don't need the high electricity storage conditions, but you also don't have the worry of transient warming events. And those combinations is where we really think for these low resource environments, for both human and maybe animal health as well.

Benjamin Thompson
That was Matthew Gibson from the University of Manchester here in the UK.

For more on that story, check out the show notes for some links.

Emily Bates
Coming up, how embedded enzymes could make plastic more biodegradable. Right now, though, it's time for the research highlights with Dan Fox.

Dan Fox
In 2021, a huge cicada emergence had an unexpected knock on effect.

Extra raccoon activity.

Cicadas are insects that spend most of their lives underground, only to emerge en masse at the end of their life cycle to reproduce. One of the largest emergence events in recent history occurred in 2021, when three cicada species on a 17 year cycle emerged in the space of just two months in the eastern United States.

A team of researchers wanted to know what effect this emergence might have on the local mammal populations, and set up camera traps and audio recording devices across two areas of Indiana. The team looked at eight species and found most of them carried on as usual during the cicada invasion, but raccoons became more active during the event, possibly so they could feast on the readily available insects. Meanwhile, white tailed deer appeared less frequently, perhaps avoiding areas where the hum of insects could make it harder to hit predators.

You don't need a camera trap to catch that research. It's in the Journal of Mammology.

Records of the quality of annual wine grape harvests can be used to estimate historical summertime temperatures across western Europe.

Weather and harvest quality are interlinked. Grapevines like their summers hot and sunny, and their favourite weather leads to production of grapes with high sugar levels.

A team of researchers analysed records of the sugar content of wine must the mashed grape juice before it's fermented in western Europe from 1420 to 2019, combining this analysis with climate records to build a model that estimates harvest quality, summertime, temperature and precipitation at locations where the wine was produced. Their analysis shows that the quality of grape harvests oscillated for more than 500 years before increasing sharply in the latter part of the 20th century, as human induced global warming resulted in longer and hotter summers.

Better wine grapes.

You can pick up that vintage research in climates of the past.

Emily Bates
Next up on the show, reporter Nick Perch Howe has been finding out about a new plastic that can biodegrade in a home compost heap.

Nick Perch Howe
I probably don't have to tell you that plastic waste is a huge problem, with millions of tonnes of the stuff being produced and thrown away every year.

What's more, plastic often lingers in the environment for hundreds of years.

To avoid a continued buildup of plastic rubbish, manufacturers have been increasingly turning to polylactide, or pla, a plastic derived from plant materials that should completely break down over time, but only under certain conditions.

Nature
It is considered as biodegradable at high temperature and high temperature means higher than 60 degrees.

Nick Perch Howe
This is Alan Marty, the chief scientific officer at the biochemistry company Carbius, who has been working to find a way to get PLA to biodegrade at lower temperatures.

And this would be useful because currently this plastic can only be broken down in special industrial facilities.

So PLA cant just be chucked onto someones compost heap as these dont get above 60 degrees.

Alan and his colleagues have been investigating if enzymes could help break down PLA more efficiently. These little proteins have shown promise at breaking down plastics, and the team wondered if embedding an enzyme into PLA could reduce the temperature where it breaks down.

There is evidence that this works for other plastics, but while straightforward on paper for PLA. The reality was somewhat different.

Nature
When the CEO of Carbios twelve years ago proposed me this challenge, my first question was how to introduce an enzyme in a plastic, because I was not familiar with plastic industry.

And the answer was, we will melt the polymer and we will introduce this enzyme. And my second question was, what is the melting temperature of pla?

And the answer is 170 degrees celsius.

And I said, I think it will not be possible.

Nick Perch Howe
But Alan was not going to be defeated that easily. Previous studies have found enzymes that can break down plaenjief, but these wouldn't be able to withstand the high temperatures in the plastic production process.

So the team set about looking for an enzyme that could.

They started with a known PLA eating enzyme that is found in a bacterial species, and then they isolated it and tried to figure out how to make it work a bit better, as Isabel Andre, part of the team from the University of Toulouse, explains.

Nature
And we started to engineer this enzyme. So that's where actually we used molecular modeling to understand how the PLA could be recognized by the enzyme and identify some residues that could be key and that actually could be mutated to improve the activity of the enzyme.

Nick Perch Howe
The team were able to find the key amino acids in the enzyme that they could change to improve how well it works. They then used this knowledge to make a beefed up version of the enzyme, which was great at breaking down PlA.

Sadly, though, it still couldn't survive the high temperatures that it would encounter during the plastic production process.

Nature
So that's when actually we decided to also search for homologues in the natural biodiversity.

So we used bioinformatics tools to identify some enzymes, and we came up with an enzyme that was less efficient, but that actually showed higher thermostat.

Nick Perch Howe
So now the team had two similar enzymes, one that could break down PLA a bit, but survive at higher temperatures, and one that couldn't, but was very good at breaking down pla. The next step was to combine them to create a new enzyme that could do both.

The team did exactly this and ended up with an enzyme that could break down PLA well and withstand the high temperatures. But then they were faced with a different problem.

How do they get it into the plastic?

Enzymes have been embedded in plastics before, but previous attempts have used enzymes in powder form, which limits how thin the final plastic can be, making it difficult to use for things like shopping bags or food packaging.

To get around this, the team introduced the enzyme into the plastic molding process as part of a liquid formulation.

This had a dual benefit. It mixed better in the melted plastic and further protected the enzyme from heat.

With all that in place, the next question was how well the enzyme infused PLA broke down.

Nature
What we proved is that, first of all, this plastic is only biodegradable in presence of water. It means that during the storage, there is no biodegradation at all, and then it is just when the plastic ends up in a compost. We demonstrate is that the total biodegradation is realized in less than 26 weeks.

Nick Perch Howe
When in warm, wet conditions, like a home compost bin, the plastic will break down in about 26 weeks. A big improvement over just regular PLA, which would still need a long time in special industrial conditions to break down.

Ting Chu, a materials scientist who's also worked on enzymes to break down plastics, was impressed by the research.

Ting Chu
The work is definitely very important and has a lot of relevance for years to come.

Nick Perch Howe
Ting believes that being able to program when a plastic is broken down is going to be important to deal with plastic waste. And by embedding an enzyme like the team did here, you can achieve that and in a more efficient manner, by having dedicated enzymes to break down the plastic.

Ting Chu
First of all, you really make the enzyme to be accessible to the plastic that is buried deep down, instead of just having a surface erosion.

The other thing is that you can have a lot of enzymes working at the same time for you instead of just relying on whatever the environment have at the time. That's a really large variable. But by putting the enzyme inside of the plastic, you know where they are.

Nick Perch Howe
The one caveat ting did have, though, was with this being an engineered enzyme rather than a naturally occurring one, she'd like to know what would happen to it in the long term.

Ting Chu
So if they reach out to the environment, what is going to be their impact for the long term? Personally, I think they should be pretty safe because enzyme is not particularly stable. Nature may have different ways to deactivate, but I. That's the part that I think the community probably should spend some effort to investigate on.

Nick Perch Howe
Alan and the team say that the enzyme will degrade in the environment, and recently they gained authorization for the product to be used in the United States, which means they had to go through various checks to make sure the enzyme is safe to use and doesn't transfer to food.

In fact, come 2025, we may start to see this kind of enzyme embedded PLA plastic available, which Alan thinks will really start to change how plastic waste.

Nature
Accumulates for single use plastic. I think this work is a revolution because it will enable to replace, for instance, polyethylene packaging. And you cannot imagine biodegradation with polyethylene. Then the challenge is to replace polyethylene by pla.

But this innovation offers a way to make packaging fully biodegradable.

Emily Bates
That was Alain Marti from carbios in France. You also heard from Isabella Andre from the University of Toulouse, also in France, and Ting Xu from the University of California, Berkeley in the US.

For more on this story, check out the show notes for some links.

Benjamin Thompson
Finally on the show, it's time for the briefing chat, where we discuss a couple of articles from the nature briefing. Emily, why don't you go first this week? What have you been reading?

Emily Bates
So I've got a story I read about in nature, and it's based on a nature communications paper all about making lab grown meat actually tastes, well, like meat.

Benjamin Thompson
All right, so lab grown meat then. So this isn't fake meat, but it's also not real meat. How are we defining lab grown meat here?

Emily Bates
Yeah, so it's cultured meat. It's produced by growing animal cells in the lab. So normally they take stem cells and turn them into muscle cells, and that's what they use to create these, what we call lab grown meats. Some people believe that this is the future. There's no need to slaughter an animal, and it could, in the future, have a lower carbon footprint than rearing livestock does, if we can get the technology right.

Benjamin Thompson
And one of the things to overcome then, is to make this lab grown meat taste meatier. Is that right?

Emily Bates
So they've really focused on the texture and making it look like meat. So you get things like steak and meatballs. But matching the taste has always been quite challenging. The traditional meat flavors are very complex, and they don't do particularly well in a lab setting.

Benjamin Thompson
Well, researchers are getting towards getting the look down then, but I guess a lot of eating is in the smell and the taste. And this has been hard to recreate the real deal then.

Emily Bates
Yeah. So when conventional meat is cooked at high temperatures, it undergoes something called the Maillard reaction. And this is when amino acids and sugars react with each other. And it's what gives the meat that recognizable aroma and taste and also that kind of golden brown color that you get, you know, the crispy bits that make you go, oh, that looks quite nice, actually. So what the researchers have done is they've developed a compound that contains a, a product of the Maillard reaction that is known to contribute towards the sort of savory profile of meat. And they made it what they call switchable, meaning that the flavor would only be released when the meat was heated to around 150 degrees c. So there's.

Benjamin Thompson
Kind of a mirror there, too, then. So almost the process of heating, of cooking, releases what it's supposed to taste or smell like. Is that right?

Emily Bates
Yeah. So they tested it by using what's called an electronic nose, which is a device that analyzes the chemical makeup of smells. And they found when they heated this lab grain, it produced compounds that were associated with savory, fruity and meaty flavors. But it wasn't until it's heated up. So before then, the nose was like, this is just some weird gel, which is another thing we should probably talk about. They added this compound that they created to a hydrogel, which is a sort of jelly like material that's used as the scaffold for the stem cells that they grow into muscle tissue. It's what allows the sort of meat to begin, but it means that it's not the most appetizing looking thing in this situation. It kind of looks like a translucent pink gel disc. It doesn't scream of a hamburger or a steak or anything like that.

Benjamin Thompson
So it seems then there's one strand, which is getting it to look right, and there's another which is getting it to taste right. Is it going to be straightforward to kind of combine the two things together?

Emily Bates
Well, there's a slight issue with this study in that the materials and the culture medium that they used have not been approved as edible. So this meat isn't going to be used to nourish and humans. It's not going to be the be all and end all. But it's just a proof of concept, and maybe in the future they'll be able to make it edible.

Benjamin Thompson
Well, that does seem like a fairly important bridge to cross, then, in terms of getting this lab grown meat to look and smell like the real thing, as we say there. But let's move on to my story this week, Emily, and it's a story that I read about in the Guardian, and it's based on a paper in nature astronomy, and it's about an underground cave on the moon. I think this has got a few people quite excited.

Emily Bates
I wasn't aware that there were caves on the moon.

Benjamin Thompson
Well, that's totally reasonable. I think for a long time, researchers, you know, speculated that there was caves and tunnels under the lunar surface. It was thought then that this underground system was formed by lava flow. Right, making these things called lava tubes. But there was no real direct proof. Right. It was kind of hard to come by. Now, there have been a bunch of images of hits on the surface of the moon, right at different elevations and different locations, several hundred of them, from what I understand.

It was kind of speculated that these were collapses of this underground network. But as I say, this has been kind of inconclusive. But that's where this paper comes in and have maybe kind of tipped the balance the other way a little bit.

Emily Bates
Interesting. And so how did they actually discover this one? What was the process?

Benjamin Thompson
Well, in 2010, actually, this hit was detected by NASA's lunar reconnaissance orbiter. Okay. And what the team here have done is they've actually gone back and reanalyzed some of the data from this mission, obviously, several years later and using new techniques. And what they've discovered is that there were some radar reflections from inside this pit. And they put forward that the likely explanation for this is that there is an underground cave. Now, it seems like quite a substantial sized thing, right? And it's accessible from this pit, which is in this area of the moon called the mare tranquillitatis. Okay. The sea of tranquility, which is, of course, where the Apollo astronauts first set foot mode. And this is an ancient lava plain. And it turns out then that this cave, if that's what it is, is 150 meters below the surface, maybe 45 meters wide, and potentially up to 80 meters long. And in this article, they say that's about the size of 14 tennis courts. So a pretty big space.

Emily Bates
So is this the kind of thing that we might be looking to set a base up on, or is that fanciful?

Benjamin Thompson
Potentially fanciful, but it's what a lot of people have been speculating for a lot of time. Before we get into that, let me do the sensible thing right now. I think research is a super interesting, because the rocks inside this cave will probably be an absolute goldmine, if you'll pardon the pun, for the history of the moon and the volcanic activity there. But you're right, it seems that the way the wind is blowing is that humans want to set up bases on the moon. Now, the moon is a pretty inhospitable place. We covered it on a book podcast not so long ago, so I'll put a link to that in the show notes. And there's these absolutely huge temperature swings. It's absolutely battered by radiation, and the threat of meteorite strikes is kind of ever present. So these geodesic domes on the surface that we were promised in the 1960s seemed very, very unlikely. But if you could live underground, that could mitigate a lot of these issues. Right. Much more stable temperature, more protection from impacts and radiation. So that's what's been put forward. But it's always been tough to actually prove that these things are there and find one. And that's what they've done in this instance.

Emily Bates
This almost feels too good to be true.

Benjamin Thompson
I mean, yes, that's fair. I think there are a bunch of issues here, right? And of course, the first one is researchers have got absolutely no idea what this underground cave looks like. You know, jagged rocks abound. So having a cave that's full of those will make it more difficult to potentially live there. And also to get into it is a drop of over 100 meters.

Emily Bates
Oh, okay.

Benjamin Thompson
And a bunch of steep slopes that, yeah. Could potentially make avalanches happen for the people at the bottom. So it might be fanciful that this is the one. But of course, while this is n equals one, it does show that potential collapses of these tubes that form entrances to this underground world do exist. And so I think researchers will be going back and looking a lot harder at previous data and looking for other evidence of this. But, you know, as we've said there, you know, it seems like lunar exploration is huge business right now for private companies and for various governments and nations around the world. So finding somewhere that folk could stay relatively safely, I think relatively is an important word to use. There would be a real boon for these missions moving forwards.

Emily Bates
Holiday to the moon just yet, but maybe in the future. Some research going on underneath the surface.

Benjamin Thompson
Yes, I mean, that seems like a reasonable thing to say and also a reasonable place to end this briefing chat. Thank you, Emily, for making it your debut this week and for listeners for more on those stories and where you can sign up to get more like them directly to your inbox. Check out the show notes for some links.

Emily Bates
And that's all for this week. As always, you can keep in touch with us on xDev. We're at Naturepodcast, or you can send an email to podcastature.com. i'm Emily Bates.

Benjamin Thompson
And I'm Benjamin Thompson. See you next time.

Nature Podcast
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nature plus the key to unlocking the world's most significant scientific advances. Subscribe today at go dot nature.com plus.

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