The Climate Biotech Podcast
Are you fascinated by the power and potential of biotechnology? Do you want to learn about cutting-edge innovations that can address climate change?
The Climate Biotech Podcast explores the most pressing problems at the intersection of climate and biology, and most importantly, how to solve them. Hosted by Dan Goodwin, a neuroscientist turned biotech enthusiast, the podcast features interviews with leading experts diving deep into topics like plant synthetic biology, mitochondrial engineering, gene editing, and more.
This podcast is powered by Homeworld Collective, a non-profit whose mission is to ignite the field of climate biotechnology.
The Climate Biotech Podcast
The Global Plastics Problem and Protein Engineering with Cesar Ramirez-Sarmiento
The solution to plastic waste looks different depending on where you stand in the world. While Northern Hemisphere biotech approaches to plastic recycling focus on high-temperature enzymes designed to regenerate plastic monomers (which works when you produce lots of plastic), Cesar's lab has engineered a completely different solution. Starting with microorganisms from Antarctica, his team uses AI and deep learning to design enzymes that work efficiently at low temperatures - not to recycle plastic into more plastic, but to transform it into valuable fragrances and other products that actually have market demand in Latin America.
The conversation weaves between technical enzyme design challenges and broader themes of democratizing biotechnology across the Global South. During the COVID pandemic, when reagent shortages hit Latin America particularly hard, Cesar co-founded initiatives to produce essential molecular biology enzymes locally. This experience crystallized his vision of combining open science with practical innovation - making biotechnology tools accessible while simultaneously developing commercial applications.
Follow Cesar's work at the Institute for Biological and Medical Engineering ath the Pontificia Universidad Católica de Chile.
@cxarramirez
We thought that it was a good idea to keep working on designing that will operate at low temperatures Instead of using the enzymes as the means of degrading the plastic. It will be wholesale organisms that could do that. They can uptake the process of degradation of the plastic and can bioconvert that into something else, Something that could actually make sense for the market in our countries.
Speaker 2:Welcome to the Climate Biotech Podcast, where we explore the most important problems at the intersection of climate and biology and, most importantly, how we can solve them. I'm Dan Goodwin, a technologist who spent years transitioning from software and neuroscience to a career in climate biotechnology. As your host, I will interview our sector's most creative voices, from scientists and entrepreneurs to policymakers and investors. All right, cesar, I'm so excited to finally have this conversation. So we are thrilled to welcome Cesar Ramirez Sarmiento for a discussion about climate biotech. Cesar is a professor of biological and medical engineering at Universidad Católica in Chile. We got to know him through the Homeworld Garden Grants program and from there we've learned a lot of amazing things, both on his ideas for better protein engineering, but then also for better ways of doing science in Latin America. Cesar's work that we knew him for originally was building a cold temperature pet ace, which is a very important part of the problem of solving the global plastics problem. So before we go into it, I just want to give a couple of formal lines about Cesar, and then we'll hear it from the man himself.
Speaker 2:Cesar is an associate professor at the Institute for Biological and Medical Engineering from Pontifica Universidad Católica de Chile, an adjunct researcher at the Millennium Institute for Integrative Biology. A biologist by education, he obtained his PhD in molecular and cellular biology and neurosciences at the University of Chile and received training in biochemistry, biophysics and computational biology as a visiting grad student at the University of California, san Diego. His lab works on engineering and designing proteins with different functions, including enzymes that hydrolyze pet plastics. Beyond research, he's the organizer of the Latin American Workshop for AI on Protein Design in Chile and has just been announced as a TED Fellow in 2025. I swear, cesar, you have more frequent flyer miles than, I think, any scientist I know, and I can't wait to hear about where you've been traveling, for all our listeners to get to meet you. Cesar, who are you? Where did you grow up?
Speaker 1:Yeah, so I'm a scientist from Chile. I'm a very humble scientist from Santiago. Actually, I was born and raised in Santiago and I did all of my education and careers as a scientist in there. Most of my childhood that I spent outside Santiago, in the outskirts of Santiago, in the perimeter of Santiago. We actually have the countryside, and so most of my time as a child I would actually spend with my family over there over weekends, visiting my other family relatives, and I was very exposed to nature. I was very exposed to go grab milk from a cow and then going back home and then making butter at home and having no electricity and no water during those years. This was in 1985 until 1992. We ended up having potable water by then. But, yeah, like, my first experience as a child was like, very exposed to nature. It was very exploratory in that sense.
Speaker 2:Wow, so your first wet lab work was making butter.
Speaker 1:It was like making butter, making bread, getting everything ready for doing that. A lot of cooking. My family's pretty good at cooking. Exposed to a lot of things when I was a child Very cool.
Speaker 2:So when young Cesar was making butter, do you think he'd always know that one day he'd be traveling the world to find and engineer proteins?
Speaker 1:Not really so. Actually, what happened was that I was very intrigued by arts when I was a kid, and the reason for that was that, since I was exposed to nature, I had an appreciation of colors and distinguishing different silhouettes of different animals in different landscapes, and so I was very attracted by that. And then my mom, when I was like eight or seven years old, she took me to a course on painting after class. So, like after elementary school, I would actually go into this for a few hours and I would do oil on canvas. I would do a lot of paintings and drawings, and I did that until I was maybe 14 years old or something like that. So I was like deciding on I'm gonna pursue arts as what I wanted to do.
Speaker 1:Then I even got deeper into arts by starting acting theater in high school, which was even more stressful because I had to learn all of my lines, and then practicing everything about communicating emotions, including crying, which was really tough for me by that time to actually manipulate myself into crying in front of an audience.
Speaker 1:But I actually achieved all of those things. So it was entertaining, but at the same time I was figuring out that being an artist in Chile is not easy and I think, like everywhere, it's not easy right Finding something that was similar in terms of having a space for creativity but, at the same time, that could allow me to go for bigger things. And I found out science was that playground. You can be as creative as you want, regardless of the field that you're experiencing. You can be just your regular people doing biology, just learning about different animals, or you can do the cutting edge biotech stuff that many of us hear about in the news. Regardless of your position in the science landscape, you have to undergo a creative endeavor in order to actually achieve something, and so I switched from arts to science just because of that, because I thought it was like a similar space for being creative and doing great things.
Speaker 2:I love it. Do you still paint now, by the way?
Speaker 1:I do some drawings from now. Sometimes I do it. I don't do much painting, though I don't have much time for it. As you said, I'm traveling a lot to different places so I don't have. I kind of go around with an oil and canvas to everywhere that I travel.
Speaker 2:My friendly challenge to you is for your next paper, for your figure one, to be an oil on canvas rather than a screenshot off PowerPoint.
Speaker 1:Yeah, that would be really cool actually. So I've been. I've been trying to go back to like drawing and painting. I might go back into that when I go back to chile, but I'm not in chile now unfortunately the other thing that I actually did.
Speaker 1:Also that it's shocking for people is that I played the guitar for quite a few years and I actually was a so for paying for my studies. When I was in college, I was a roadie for bands for national bands and for international ones and so, among other things, when I was like learning about science and everything, I was also going around with bands all across the country and then, when they were supporting bands for these big bands from outside, I would have the chance to meet some of my biggest bands ever. So I had the chance of meeting with Nine Inch Nails once I met them. I also met Rammor and Chris Cornell, so that was pretty amazing.
Speaker 1:I learned many things from that experience and one of them was about how to manage everything, about what you're doing yourself. How to manage everything about what you're doing yourself, so going from guitar to set up a guitar, to set up a stage, to whatever you have to do that comes up with staging a band so that they can play. I actually took a lot of that knowledge now into science and to like knowing what you're doing, then being able to present that to your students and then trying to have a foot in every place so that everything works smoothly, trying to make sure that everything works the way it should work. So it was a great experience.
Speaker 2:There's a really surprising commonality here. So the last guest on the podcast was Chris Iben, who just started a company called GigaCrop, and I've known him for years and that's when he told me he also played the guitar at a very high level for 10 years, practicing four hours a day. And actually, if you went through a lot of the guests on this podcast, they had the same thing some deep history in arts. And then the other side of that also surprising is they're the best engineers. I know people who did something that was really nitty gritty. So I built fences as a high schooler, right? Or, like one of my best friends from college, he was a short order cook in the breakfast kitchen and he was one of the most ferocious people I ever worked with because he just had that eye for a thousand little details and he had no patience for those not to get done.
Speaker 2:So I love these commonalities. That's part of your background. What was the shifting point, then? From going from these expressions? I would say I was going to say from creative things, but biology is just as creative as oil painting, right? But was there a phase change moment or a fold switching moment, to be cheesy about it in your career?
Speaker 1:Yeah, there were many instances that drew me to that. So the first one was that my mom once said, when I was maybe eight years old, she mentioned that she was gardening and she had some of these plastic bags for keeping your flowering first and then you transplant that into the soil afterwards, and she mentioned that the snails were eating through the plastic. And I was like there's no way that's happening. Mom, you're crazy. But the unanswered question got stuck in my head forever. It's one one of those things that you remember forever. And so then, when I was studying biology in universidad de chile, in my alma mater, we were having biochemistry and so we were like hanging around with a bunch of friends and we were like talking about the enzymes and that among the things that they presented to us. To be honest, I didn't like everything about biochemistry. There were things that I liked and there were things that I didn't. So metabolism was like a no-go for me. I was like this is upsetting. I don't want to learn about all of these metabolic pathways, maybe the important ones, but not about all of them. I did. I did get intrigued by enzymes, and we were having a coffee with some friends and we were having a conversation about like enzymes. They were somewhat cool and they did like great things. And then somebody asked, like one of my friends said, oh, what if they actually can end up like degrading other things, like eating through plastics. And again it was like the second time that somebody mentioned that. But biology can be involved into degrading things that were not supposed to be biodegradable. And so those two things gravitated into trying to search for literature associated to that and then deciding on doing biochemistry as the thing that I wanted to do. So I was not the person with the good grades in biochemistry, but I decided I was challenging enough for tackling that problem.
Speaker 1:Yeah, that's how I decided to join the lab of the PI that was teaching biochemistry. So Victoria Giche was my advisor to learn more about enzymes. Then after that, I learned more about biophysics. So first biochemistry and then how proteins come together in different shapes. So I learned biophysics and I had the chance to go to, as you mentioned, to the University of California, san Diego, in which I had one of the most amazing advisors that I've ever had in my life, which is Elizabeth Cummings. Betsy, she was just great. She put me through every task about how to deal with proteins from experiments to computational efforts, and that was just great, because then I had this arsenal of tools for doing whatever I wanted with proteins pretty much, and so that was a great experience. So then, after that everything came together into, I'll work with proteins for the rest of my career.
Speaker 2:Awesome. And then it goes full circle back to mom's snails in the garden, which is really beautiful because we're the same age, right? And so I feel as if we live this phase change of biology. 20 years ago you would see that and you'd be like, ah, maybe I'll read in a book, but the idea of biology interacting with man-made chemical to me always felt like pretty foreign, pretty foreign, Whereas now, in 2025, it actually feels just that's one of our assumptions that there's so many bad things out there that is just a byproduct of the built world. We're going to need to figure out ways to get rid of it somehow, and so I love that you've chosen.
Speaker 2:One of the things that your lab works on is plastic degradation. So I think this is worth just giving a little bit of background, where everyone I think listens to this knows what Homeworld has done two rounds now of the Garden Grants program. And the Garden Grants program is we're just trying to create supportive funds to do de-risking, early stage experiments, and we frame this as a big problem. And if we care about the problem, then we care about the solution, and when we did approach engineering call, we were frankly really surprised that I think about 20% of our applications were all around plastics, and so we went through all of those and obviously yours stood out the most and I'm really excited to just get a chance to talk about that. And so let's start. We want to talk about the problem, want to talk about the solution, and then want to hear what the progress you've made over the past year or so. Let's just pass it over to you. So what is the problem that you are trying to solve in your lab around plastics?
Speaker 1:you are trying to solve in your lab around plastics. Yeah, that's awesome, yeah. So when I started my career as a professor at Catholic university in Chile, one of the projects that I started was a very humble project about trying to discover new enzymes that could degrade through plastic, particularly plastic bottles, pet. These enzymes are called PETases or PETases, depending on who you ask to, but there's a collection of them, and we were wondering whether they can operate at lower temperatures. And so we saw that Antarctica is a known source of animal organisms that are, like, amazing at thriving in this environment, so having very excellent enzymes that operate at low temperatures, and so we wonder whether we can actually get some enzymes from those organisms, and so we submitted a grant to the Chilean Antarctic Institute, which actually provides funds for that, and we got our first one, which is just figuring out whether there's an enzyme that can degrade through plastic at low temperatures coming from Antarctica, and we found two of them. One of them is actually similar to a well-known enzyme from an organism that was detected in Japan in terms of activity, so it will degrade like a plastic continuously upon time if you incubate with the enzyme and the plastic waste, and so we were excited about that one, and then by learning how to work with the enzymes, we also learned about the different caveats that we have in Latin America compared to the Northern Hemisphere. So the Northern Hemisphere was pretty focused on discovering incense that operated at very high temperatures, because the purpose for that was we can build the bioreactors that will consume high energy and will degrade the plastic fairly fast.
Speaker 1:So most of the kind of thermophilic or thermally stable enzymes are actually operating at very high temperatures, which is the temperature of which the plastic becomes from malleable and you can degrade it faster. So it's like ideal for that, but then the output of that will be the monomers that you can use for making new plastic afterwards. For that to happen, you have to have two things First, you have to have the enzymes that work at very high temperatures and the way the plastic pass, but then you also have to have an alliance with the plastic producers so that you can pass them on the products, the monomers, that you have afterwards. And so that's where the problem comes, which is that Latin America does not produce that amount of plastic. We, as Latin American countries, produce about 4% of the plastic that is produced worldwide, compared to what happens in Asia, the US or Europe, which is like all of the other percentage, and so we thought that it was a good idea to keep working on designing proteins that will operate at low temperatures Instead of using the enzymes as the means of degrading the plastic will be wholesale organisms that could do that.
Speaker 1:Then even though I hate metabolism, as I said before, they can uptake the produce of degradation of the plastic and can bioconvert that into something else, something that could actually make sense for the market in our countries, such as pregn, so that we can come up with something that our markets were actually prepared for putting out, rather than thinking about something that we're not working with, which is like making new polymers. So we are not making new polymers, but we do make fragrances. Maybe that's a bigger or better idea in terms of that.
Speaker 2:I love this. So if I could just play this back to, because I think there's so much subtlety in the way you're framing this problem, which is great and the way we think about recycling plastics in the Northern Hemisphere is we try to do it as fast as possible with proteins that are optimized for heat, with the intention that we're going to recycle those monomers from the pet ace, breaking polymers into monomers. We have a market to recycle those monomers into new products, to recycle those monomers into new products, whereas in the Southern hemisphere, where you guys have a few massive plastic dumps right, your vision is much more that you basically want to be able to ferment these plastics into a biomanufacturing pipeline that will produce high value goods. Is that kind of the way to think about it?
Speaker 1:Exactly. Yeah, that's the way it is, and so the idea was to like develop these enzymes that operate, that operate very efficiently, as efficiently as possible at low temperatures, so that we can put them back into bacteria and then the whole cell would be actually the biocatalyst for consuming the plastic and then converting it into something different, and so there's many fragrances that you can make. So there's a very beautiful work from Jo Satter, which is she's in the University of Edinburgh. She did metabolic engineering of E coli, so a bacteria to consume the products of degradation of one of these enzymes that works at very high temperature for degrading PET, and you take the products out of that reaction and you incubate your bacteria with the products of degradation and you can convert everything into vanillin, which was the first example of. Oh, we can do this.
Speaker 1:The intermediate molecule for making vanillin is producatequate, which, if you think about like the possibilities in terms of like metabolism, there's a lot of it for like different fragrances. So vanillin is one example that you can create. If you can continue aromatic biosynthesis. After that you can create other molecules, like raspberry ketones, which have like raspberry smells. You can create other types of fragrances that have like different types of smells for different circumstances. So that was great. It was like an opening door for, oh, we can put together like protein engineering with metabolic engineering and try to develop this like biocatalyst for different purposes.
Speaker 2:Great. So in your ideal world you walk into my house next time you're in Boston and say your house smells like plastic, dan, and I'll say thank you, cesar.
Speaker 1:Yeah, that would be the ideal thing. Yeah, the medicine that you're getting is actually from PET. That would be awesome.
Speaker 2:Yeah, I like this. I think, just in general, the metabolism of these awful chemicals is very important, especially with the microplastics problem that we see that get bioaccumulated.
Speaker 1:So I'm going to ask you the really annoying question, which is why is it hard or how is it hard? So it is hard because, when you think about the enzymes that naturally degrade the plastic at low temperatures, they're very inefficient, they're pretty bad. They also suffer from other things like poor stability, so they go bad. They lose their activity pretty quick. So the enzyme that we characterize as the activity like 60% of the activity in one day is just a pretty bad biocatalyst on its own, it just falls over and then stops catalyzing.
Speaker 1:Yeah yeah. It just starts like aggregating after a while, even if you have it in like the best kept conditions or like buffer conditions. We tried way too many and none of them seem to work. So you lose activity after a while. When you work with the thermophilic enzymes, like most of them are like able to withstand conditions for longer and they also have like much better efficiency for the degradation. And not only that, that, they seem to have very well-formed active sites for accommodating the plastic into the binding site.
Speaker 1:And that demonstration for that came from an article in, I think, 2021 from another group that actually are kind of the pioneers on developing the same sense for biological recycling of plastic, because they are a company it's called Carbios in France. They tried to take the active side of one of these thermophilic enzymes, select for all of the residues that are in contact with the substrate, and then took all of those residues and they changed for all other 19 alternatives to see if any of them could have an impact on activity. And from all of the changes that they did just 11 times 19, right, so many mutants three of them had higher activity, which for us, like my interpretation of that is that these active sites are really extremely good, and so what we need to focus on, rather than on improving activity or improving active sites, will be what if we can calibrate our enzyme to work now at different operation temperatures? And so the idea of the Homeward Garden Grant that we got was that we will use some deficient intelligence or a deep learning network in this case, to predict mutations that occur outside the active site but that compromise thermal stability, so that now the enzyme will operate at lower temperature, because there's a trade-off of stability and activity. So if you compromise thermal stability now, your optimum temperature for activity will also change because of that change in stability.
Speaker 1:And so if we destabilize the protein by introducing mutations in different parts away from the active side, the idea was oh, we can now create enzymes that now operate at lower temperatures, but has this? They have this really well defined active site for degradation, and we got a collection of them. That was pretty cool we got. We used two different well-known enzymes as a scaffold. We did the mutations, and out of 22 mutations that we tried for one of these enzymes and 26 that we tried for the other, a total of 10 mutants actually showed the profile that we wanted, which is that they are very active at temperatures that are like resembling the optimal growth temperature of E coli, so 37 degrees Celsius. And yeah, so we're still working on like characterizing now these enzymes against plastic to see efficiencies, but at least for now we know that they are active at lower temperatures compared to their natural counterparts.
Speaker 2:And is this? Taking the same enzymes that you've originally found in Antarctica and then increasing the temperature that it operates optimally at?
Speaker 1:We try that. So that's why we ended up saying maybe it's a good idea to work with very efficient thermophilic enzymes and not with the not so efficient cold active enzymes.
Speaker 1:We try to improve the activity of the ones that are operating at lower temperatures and make them go towards high temperatures, but the efficiency was never comparable to the thermophilic ones even when we we did like loop swapping, which is in this case, we took an active side loop of one thermophilic enzyme and we put it into our Antarctic enzyme, so just swapping these loops on the active site to try to see if we can increase activity by that.
Speaker 1:And we saw increases in activity about like fivefold, but they were still like, not comparable to what you have when you have a thermophilic enzyme. And so that's why we were like we're going to, we're going to keep working with the cold active ones for a little bit and we're going to work on the thermophilic ones and see if we can, yeah, make them worse in terms of like stability, but hoping that the activity remains there and it seems to be working so far. So we need we need to try out now with plastic films, like actual pieces of plastic, to see how they work at different temperatures. But we have a few promising candidates for it.
Speaker 2:That's awesome. So, to play it back, there's three approaches. The first one was you get something that works really cold and then bring it up. The other one is you take something that works really hot and bring it down. And then here's the third approach we haven't really talked about, which is just no, just alpha fold it, just de novo the whole thing. And I'm saying that kind of as a joke, but it's becoming less, it's becoming less silly, and so I'm curious, especially since you work so closely with AI. You know what AI means in project engineering is changing by the day, and so it used to be like you do it in super high dimensional and then just spit out some like a non homology solution for this. Or the other one is like doing the loop swapping for me right, like taking rational design approaches, but then doing that with kind of AI approaches, and I'm just kind of curious what your take is on where the frontier is, especially when we think about automation getting mixed into this idea.
Speaker 1:Yeah, that's a great question. With the advent of AI, many things have changed and they are changing by depending on your location. They might be changing by the month, by the day or by the hour. So nowadays I'm located in Seattle, I'm doing my sabbatical with the Institute of Printing Design, which is led by David Baker, who everyone knows like is the Nobel laureate from last year because of his work on printing design and in some designs, still like a difficult problem to tackle in terms of all of the metrics that we have, or many of the metrics that we have about how we say that we're confident about the structure that we're designing in the computer, about the sequence that fits into the structure. All of those predictors for like protein structure and like sequence design are not capturing what happens with enzyme activity, and so we have to come up with like new metrics for enzyme activity. So there's still, even though you can do you can replace, for example, direct evolution, which will be like your alternative in the lab for diversifying your enzyme and then see which one works best. The alternative in the lab for diversifying your enzyme and then see which one works best, the alternative in the realm of artificial intelligence will be redesign your protein to a bunch of sequences and then do some high throughput screening to check for which one has the desired activity. There's no way of saying, oh, this enzyme that I designed from this list of a hundred or thousands of enzymes that I designed in the computer is actually the best one. We still have to do the high throughput work. Ai is alleviating some of the troubles that we have in terms of diversifying our sequence space and also, if you think about designing, for instance, completed the Novo, if you're designing about new enzyme scaffold that is never seen in nature, you can do that too. But if you want to test for activity, you still have to do the work, and that's where what you mentioned, which is automation, comes very handy. So if you have a ways of doing automation or high throughput screening connected to like robotics and that's going to become much more easier.
Speaker 1:Funny enough, we got in touch with a company a few years ago. This happened during. This is actually a funny story, so I will tell the whole story. So we met with the, by that time, cso of the company, fritz Bahl. The company's name it's AI Proteins, and it's located in Boston. We went to the same meeting in Argentina and we are both nerds, and so what happened was that they put us together in the same room and we were like nerding around science for five days, right. And so by the end of that week we were like, oh, we should definitely collaborate. We were like, working on this plastic degrading essence, there was a student that was presenting the work in the conference and he was super excited, I was super excited, and then he also had ideas about working with plastic degrading essence, but he was still in academia, he was located in an institute in Harvard and then moved on to develop his own company afterwards, and so he was like, yeah, we should try that. And then, by the year after, we were already planning on how we're going to do this, how we're going to work on this, and so we started working on this.
Speaker 1:Last year, we started designing new sequences for non-thermophilic enzymes that degrade plastic and then setting up a high-triple screening method for sticking for the best enzyme from that pool. We ended up designing something about 72, or ordering 72 designs for testing of them, and you can see here the trouble, which is that you design the sequences. You're not designing for the new structure, you're just designing for the sequence and you're trying to keep the active site as it is. You're trying to keep, like many things fixed so that they don't change, even though you don't do that.
Speaker 1:The NSAIDs were. All of them were soluble, like most or 90% of them were soluble and they will have that protein expression, just that were much higher than the native ones. In terms of stability, most of them will have higher thermal stability. They will be optimal for enduring high temperatures. You can put them on 95 degrees Celsius and you can then lower the temperature and measure the secondary structure content. They will remain just the same, but in terms of activity, only five of them have activity.
Speaker 1:So you still have the string right. So there's no solution. It's like, with these scores, with these metrics, I know this enzyme works. Now we had to string all over them and then only five of them had activity and only one of them actually had allegedly, as far as we know. So the experience that we have done to this point better activity than the native enzymes that we were trying out to use as scaffolds. And so AI helps a lot in diversifying your sequences and exploring sequences that were not explored by other methods, but you still rely on a high throughput experiment to a certain activity efforts, and so enzyme design is hard.
Speaker 2:Yeah, I think. But what I love so much about your work, cesar, is that it's rooted in practicality, and I think to do anything under the umbrella of climate biotech, it has to have that so what at least conceptually thought through. Right, it's okay, we can make the world's best pet taste, so what? Okay, then we'll put it into a wholesale biocatalyst Okay, cool. And we'll make it work in a temperature that E coli we already know how to biomanufacture Cool. I love hearing that.
Speaker 2:I think that's what made your works just stand out. So much to the team, because everyone agrees plastics is a serious thing. No one's really solved it yet, and I think it's just pretty rare to see someone who's excellent on the Angstrom scale, like AI stack, and then also to say and when it works, we have our plan for scaling up. And so I think, with the time remaining before we go to the rapid fire questions at the end, I think it's worth just unpacking a little bit more about the awesome visions that you have for science, and specifically deployed science in Latin America. So you've been involved with a lot of open science and sustainability, and I would love to just shake the tree of your knowledge and let everyone hear about all the awesome stuff that you do and you think about for the future of science in Latin America.
Speaker 1:Yeah, sure. So something that was interesting and at the same time like very scary about the pandemic is that we learned that we in Latin America are very unprepared for this type of problems. In Latin America, are very unprepared for this type of problems, and one issue that we faced was that we were not prepared to being out of stock in terms of like reagents and kits for molecular diagnosis of the presence of viral infections overall in our country and in many other countries in Latin America. And so a friend that works on like open science I was not like a devoted open science kind of guy, but I had a friend, fernando Federici, that works on open science. He's been working on open science forever, his whole career, and he emailed me saying so the government is saying that we might run into trouble with the molecular kits, run in trouble with the molecular kits and they are asking us whether we can come up with a solution for that, whether we can make, we can come through the kits for diagnosing COVID-19 overall to the country. And so he was like I have the genes for the enzymes that we need for making this, which is just like your regular PCR or RT-PCR, so you need like a transcriptase, reverse transcriptase, and you need the polymerase. I have the genes. Can you make the enzymes? And I was like, yeah, sure, we can do the enzymes. That should be like no biggie. And so we were allowed by university. We got like a permit to go into the university during the pandemic, so we got into lockdown in March 2020.
Speaker 1:April 2020, we were assembling a team of postdocs and students very limited, we were just like five people and I had to go back to the lab to work on my own with night pipettes and everything, which was an amazing thing for me to do because I didn't do it for a while. But we assembled a team for, like, producing the enzymes, right, and so we tested the enzymes. We went through the whole thing and the enzymes works as good as the commercial ones. And so it came out to the notion that we can democratize the use of these reagents for the benefit of all people in Latin America, in terms of allowing for the localized diagnosis, without relying on buying those reagents from very well-known companies in the northern hemisphere pretty much the US and Europe that if they have a shortage of reagents, they are not going to sell to us. And so we continued that story by being part of a network that is headed by Jenny Molloy from the University of Cambridge, and also from the International Center for Genetic Engineering and Biotechnology and Fernan in Chile, as well as other folks from Argentina, peru and Brazil.
Speaker 1:We're assembling a network that is also connected with Africa, and so the idea is that we will have all of the parts, all of the genes that we need for making the enzymes, and a myriad number of protocols for producing your enzymes in every shape or form that you have, either if you're using the very wealthy lab for producing enzymes, or if you're like in the middle of nowhere and you're working with just like a piece of paper and a century that you make out of, like elastic bands, right, so like working on every possible scenario. So this network it's called Reclone and it's an open network that's for equitable access, for democratizing all of these reagents and DNA parts so that everybody can produce their enzymes, and so we detect that issue and we are working on that. The other thing that we're doing about open science is that we know that there's a disadvantage in terms of like how people are learning about artificial intelligence in the northern hemisphere compared to us, because in our countries, some people I'm not going to claim that I'm the guy saying it, but some people say that our lab is the only lab that is doing heavily artificial intelligence for printing design, and so we are aware of that issue, and so, in a way of democratizing our knowledge, we created a workshop that is called the Artificial Intelligence Workshop for Burning Design in Latin America. We run the first one in 2023. We're running the second one this year and we're super excited about it. So it's gonna happen in November and it's sponsored by the European Millicore Bio-Organization and also by Crescera Commons, which is the hub for burning design complementation of printing design in the world. So we're going to organize that with a bunch of people, including people from companies.
Speaker 1:So Chris Ball from Apprentices is also joining us, as he did in 2023. And the idea is that this is a big hackathon. This is not your typical. I go to conference and I learn a bunch of things from a slide kind of thing. This is a hackathon, so what we do is that we expose all of the attendees to all right, do your pretty nice things. This is how you work through the tutorials and we teach you how to do it, but then otherwise you're on your own, so you have to do your thing. You're going to have a set of instructors that will help you out, but that's it Like now. It's in your hands.
Speaker 2:I've got so many badges left over from random conferences. If you could just give people a pipette, I would keep that on my desk. Welcome to the hackathon. Here's your pipette. Make something cool. See you in a day.
Speaker 1:Yeah, so that's what we're trying to do with this workshop. So it's actually like a workshop first, but then it turns into a hackathon afterwards. And for the one that for Reclone, we got funding from the Chance Zuckerberg Initiative Great and we're now running workshops on that. So we're running workshops on like how to make your proteins, how you test for activity, how you do everything, how you do a PCR afterwards and then using like minimal resources for everything. So both of these things are like aiming at we can do things with open science.
Speaker 1:And the third thing that maybe you're not aware of and I'll tell you now about it is that open science is not in conflict with innovation in biotech. And the proof of that is that we co-founded a company that is now it's called Next Ensems and we're producing this off-patent, public domain Ensems for PCR and RT-PCR. We're making them as a product. We're like putting everything in packaging and we're now selling these to companies in the country for using that for their diagnosis or whatever they have to do with it. If they're doing research or if they're doing diagnosis, they can use it for that. And the reason that it works is that it's not a secret how to make these enzymes, and it's not a secret, because we're releasing all of the protocols for reclone, so everybody knows what we're doing. So everything is open.
Speaker 1:So what's the difference? The difference is that we're providing them with something that they can design with ourselves. So if they have a particular problem that they want to focus on in terms of oh, I want to make this PCR work, for like this thing they can work with us on like solving that. Oh, we will like work with you on designing the parameters that you need for optimizing for this. The second thing is that whenever they buy from outside, they pay for important taxes and they pay a lot of money for that.
Speaker 1:Since this is local production, we're saving a lot of money on that product, even though it comes from public domain, and SEMS is comparable in terms of efficiency, processivity and all of the things that you desire from a PCR or an RT-PCR that you're running. If everything matches what the market offers outside, then they will actually choose us for being their suppliers, and so that's the thing that we're doing now. We're actually like developing PCR kits and RT-PCR kits different types, like multiplex or master mix or whatever you name it. We're developing all of that and then diversifying into other areas as we go, so that's also a showcase of you can do open science and innovation at the same time.
Speaker 2:Right, and I don't want to put you on the spot by riffing too much on this, but I will just say that makes you even more somebody to watch for the next 5, 10, 20 years in biotech, when you're doing both protein engineering design and you're also building your own scaling capacity. So if you can build a transcriptase at massive scale, why not also make your new customs? So that's a really exciting combo, and I think the one thing to also laugh about a little bit is that the phrase we use a lot in America is oh, the Wild West, it's the Wild West of blah. Right, it's the Wild West of this, but maybe the Wild West is actually the super south, maybe we've gone as far left as we can, maybe we need to go down, and I really love that, and this is a totally inappropriate or maybe it's appropriate like riff, but is a totally inappropriate, or maybe it's appropriate like riff.
Speaker 2:But the prepper community is probably like a US based community that you would not normally think about open science. But when you think about what is it? What if the grid goes down? We can't produce insulin anymore and get it from Denmark. We'd have to produce it locally, right, and so, like locally sourced bioengineered insulin has been bubbling around in biohacker communities for a while, but I you could certainly imagine a future where you know that actually gets mixed into this too.
Speaker 1:Yeah, so, yeah, I think that it's a message for like investors and like VC that you should be like looking into what people in South America are doing now. So there's like exciting companies that are coming out in Chile Argentina, as far as I know, and also in Brazil. They're working, like many friends in biotech, doing what we're doing, which is like with open size, just making a bunch of enzymes and then selling for like better price same properties to different companies that need them for molecular diagnosis. Other people that are doing working on developing new ways of improving lab meat, which is a big thing that it's like coming up. So they're working on like formulations that allow for lab meat to be to grow better pretty much in the lab.
Speaker 1:So that company is called Sticta. We have CurabioTech, which is also one of the co-organizers for artificial intelligence, for protein design workshop in Chile. That is working on also like protein engineering and design for like different purposes, including diagnostics as well, and they have like proprietary enzymes for that. So there's just so many companies that you can look into and so there is an opportunity for investors to actually jump into these markets nowadays. So it will be great if we actually see them like looking at us a little bit more now that everything is happening, yeah.
Speaker 2:That's so exciting. All right, this is where we have to throttle it, otherwise we're going to talk about this forever and we're going to. We got to wrap. But I do want to just end on the punchline, which is that I'm really impressed by, once again, not only like the Angstrom scale work, but also now kind of the kilogram scale work and beyond, and I think it's just really awesome to always be thinking about, about how you bring it to scale. So we finished all these episodes with four rapid fire questions, and they're focused much more on personal development for the people listening. The first question for you, cesar, is what's a single book, paper, art piece or idea that blew your mind and shaped your development as a scientist?
Speaker 1:That's hard, but I will say everything about pointillism in terms of art. Just because of so pointillism, you have many artists that are like pretty good examples of it. Joe Surratt will be like one of them, but then Vincent van Gogh tried it out, camille Pissarro also tried it out, and the thing is that the idea about pointillism is that you do this like points of color, that when you see from afar, they mix together, right, but if you look closely to the painting, then they are separated and you see the different colors. So it was a work of science in terms of composition, color composition and also required a lot of patience, and I think that science requires both creativity and patience, and so that's why I will choose that one I love.
Speaker 2:It All right. Next question what's the best advice line that a mentor gave you?
Speaker 1:Betsy. Betsy Cummings from UCSD gave me one of the best advices, which was good ideas come from talking with colleagues, but also from reading the literature, which means that you have to keep up with reading the papers that come out, especially now, if you're thinking about AI. There's a new article coming out every day pretty much, and so keeping up with the literature is very important.
Speaker 2:If you had a magic wand to get more attention or resources into one part of bio, what would it be? Oh gosh, that's so hard.
Speaker 1:I will say that just for the practices of self-promotion. I will be like oh, if you put more money into what we're doing in terms of like open science plus innovation or open science plus education in South America, that would be awesome.
Speaker 2:Agreed. I think that's a good answer. And the last question is what's an aspect of personal development that you think biotechnologists could invest more time into?
Speaker 1:I will say that it's jumping into things that you were, according to your career, you were not supposed to take in. For example, I'm a strict scientist in terms of I do science and that's it. That's what I know. And so jumping into, oh, we will co-found a company, that was hard in terms of. I had the idea in my mind for years, but I was always frightened of taking that leap of faith of, oh, we will do it. I think when you have a good, good idea, you just have to take that leap of faith, that's it. And sometimes we don't do it.
Speaker 1:And it also happens with young scientists when they work on I don't know cell biology and they want to learn about, like, artificial intelligence and they're like oh, but should I go for artificial intelligence? I don't know anything about computers, just do it if you have the opportunity for it, especially if it comes for free. If you can just do it, just go for it. You actually go for it and you're gonna learn so much more and it's gonna be so much great for you when you learn about all of these things that you can combine in creative ways that never you could imagine before you try it out. So that would be like my advice never put yourself out of positions in which you can actually take proper risk and learn so much more about science overall.
Speaker 2:That's a great answer. All right, Cesar, this has been an absolute pleasure. The last question is that how can people find you on the internet or find your work? Where would you guide people's attention to?
Speaker 1:So I'm typically on X and Blue Sky for looking into me. You can also look at the website of the Institute for Biological and Medical Engineering, which is ibmcl, so there's a lot of information about what we do in there, including work on everything. Our Institute works on tissue engineering, optics, hardware development, software development, biofilms, biotechnology, whatever you name it. We work on many different things.
Speaker 2:Sounds great. Yeah, sounds great, cesar.
Speaker 1:Thank you so much for the opportunity of talking in the podcast that was.
Speaker 2:It was really fun and awesome. Dude, it's been such a pleasure. Thank you, cesar. Good luck, man.
Speaker 2:Good luck, take care. Thank you so much for tuning into this episode of the Climate Biotech Podcast. We hope this has been educational, inspirational and fun for you as you navigate your own journey and bring the best of biotech into planetary scale solutions. We'll be back with another one soon and in the meantime, stay in touch with Homeworld Collective on LinkedIn, twitter or Blue Sky. Links are all in the show notes. Huge thanks to our producer, dave Clark, and operations lead, paul Himmelstein.