A Helpful Fungus Among Us

A Helpful Fungus Among Us

Mine wastewater bioremediation on Minnesota’s Iron Range

By Evan Whiting

When people think of fungi, they typically conjure images of mushrooms: portobellos, oysters, truffles, or shiitakes. But a mushroom—the fruiting body we see above ground—is merely the tip of the iceberg when it comes to fungi. Most fungi are comprised of a tangled network of small thread-like structures called hyphae. Others, like yeasts, are microscopic, consisting only of single cells.

In fact, there is a huge diversity of fungi out there—some experts estimate that there are over two million species of fungi living on Earth today. And they’re important members of modern ecosystems. Excellent scavengers and nutrient recyclers, many fungi also gather materials from their surroundings and can even capture and store environmental contaminants. Experts are actively working to understand the underlying mechanisms, but scientists, engineers, and industry professionals also see the potential for using fungi in bioremediation—the cleanup of environmental contaminants or pollutants using living organisms, usually microbes.

Dr. Cara Santelli, an associate professor of Earth & Environmental Sciences and a member of the University of Minnesota Biotechnology Institute, is an expert on bioremediation and the interface between microbes and minerals. Santelli and her colleagues investigate organisms with the potential for bioremediation of mining waste, including several species of fungi. One of her ongoing projects, funded by MnDRIVE Environment, involves a species of fungus native to northern Minnesota’s Iron Range, where high concentrations of metals in the wastewater from an inactive underground iron mine could, if left untreated, threaten ecosystems and natural resources on the surface.

Located near Lake Vermilion and the Boundary Waters Canoe Area Wilderness, the Soudan Iron Mine was once a prolific source of iron ore. In the 1960s, when mining operations shut down, the mine became a research and educational facility. But more than fifty years later, there are still lingering issues with toxic metals in the mine’s wastewater, which is currently treated with expensive ion-exchange filters. Luckily, there may be a cheaper, local, and ‘organic’ solution to this problem: bioremediation with a native species of fungus (Periconia sp.) that grows in the salty, metal-rich waters in the depths of the Soudan Mine. Periconia is capable of producing manganese oxide minerals that incorporate metal ions in their chemical structures, much like blocks in a microscopic game of Tetris.

Dr. Brandy Stewart, a postdoctoral researcher in the Santelli Lab, has been studying this fungal bioremediation system in detail. Stewart is an expert in biogeochemistry, or the interplay between chemicals, microbes, and their environment. With additional background in environmental consulting, she brings a wealth of knowledge and experience to this new project. Currently, Stewart studies the optimal growth conditions for the project’s focal fungus, as well as how efficiently it produces manganese oxide minerals using nearby metal ions from the surrounding brine.

The fungus needs a cocktail of nutrients to grow and remain healthy, but the actual wastewater from the mine might not be the ideal growth medium. Even for this mighty fungus, certain metals, like copper, can be toxic at higher concentrations, so Stewart has set out to facilitate the removal of these metals without hurting the fungus itself. She likens this to our own dietary choices: “If you ate nothing but doughnuts, you probably wouldn’t be very healthy, but if you ate well and got plenty of fruits and veggies most of the time, you could still have a doughnut every once in a while and be okay.”

Thankfully, the fungus seems to grow quite well in the suboptimal, mine-like conditions simulated in the laboratory, especially when grown in the presence of carpet fibers. These fibers may be acting as a sort of ‘scaffolding’ upon which the fungus can grow, or even as an additional food source for the fungus. Regardless, Stewart has found that the presence of carpet fibers dramatically improves the growth and productivity of the fungus, which creates a thick biofilm where the manganese oxide minerals form and accumulate . As revealed by X-ray fluorescence images, these minerals are often laden with captured metals, demonstrating the efficiency of this system for removing metals from wastewater.


Periconia sp

X-ray fluorescence imagery showing very similar groupings of manganese oxide minerals (left) and copper ions (right) along strands of Periconia sp. fungal hyphae growing in the lab. Courtesy of Brandy Stewart, UMN.

Although still in the experimental stages, Santelli and Stewart eventually hope to build larger bioreactors to scale up their fungal bioremediation system for applications in the Soudan Mine. These bioreactors may be able to help prolong the lifespans of the ion-exchange filters already in use—or potentially replace them, if they prove to be at least as effective at removing metals like copper, cobalt, and nickel from the mine’s wastewater. These metals are not just potential environmental contaminants; they’re also economically important for myriad purposes, including electronics and battery production. If enough of these metals could be efficiently captured in manganese oxides produced by fungi and later recovered, we could potentially capitalize on them.

And mining wastewater might be just the beginning, according to Santelli. There are large amounts of dissolved solids in many types of industrial wastewaters, so there is great potential for using fungi (and/or other microbes) for bioremediation of contaminants in wastewaters well beyond the Iron Range. With such a huge diversity of fungi out there, it’s only a matter of time until another helpful fungus among us becomes the next big hit in bioremediation.

Evan Whiting is a PhD Candidate in the Department of Earth & Environmental Sciences at the University of Minnesota and an affiliate writer in the University of Minnesota Science Communication Lab. He can be reached at whiti101@umn.edu.

Feature photo: Photomicrograph of Periconia sp. fungal hyphae. Courtesy of Brandy Stewart, UMN

Tapping the Talents of Enzymes

Tapping the Talents of Enzymes

BTI researchers are working to discover, understand, and improve our ability to enlist the help of molecules that catalyze life.

by Mary Hoff

Enzymes are the movers and shakers of the biomolecular world. A class of proteins found in every cell of every living thing, they bring together molecules that would otherwise be reluctant to interact so they can combine, exchange parts, or otherwise alter each other.

In nature, enzymes facilitate thousands of processes from photosynthesis to decomposition. Enzymes speed up chemical reactions thousands of times faster than the reactions would occur on their own. Over the millennia, humans have found ways apply this superpower to accomplish a variety of useful goals from making beer and cheese, to making our laundry whiter and brighter, to cranking out millions of copies of a sample of DNA to solve crimes or find long-lost relatives.

“And that’s just the beginning,” says Romas Kazlauskas, professor in the department of Biochemistry, Molecular Biology, and Biophysics. “Enzymes can also learn how to do different things. We’re trying to figure out which parts are important and why they’re important, then design something different to do a reaction that doesn’t occur naturally.” By identifying enzymes, improving understanding of how they work, and applying them to new tasks, Kazlauskas and BTI colleagues are taking advantage of the billions of years of evolution that produced these molecules to make medicines, degrade pollutants, speed industrial processes, and more.


Trash to Treasure Kazlauskas is working with an enzyme found in nature that degrades PET plastic. First synthesized in the 1940s, PET (a form of polyethylene) is widely used for beverage and food containers with some 70 million tons generated every year—and much of that ending up in landfills and the ocean. Current efforts to recycle the material can only produce lower-quality plastics.

“One idea is to break down to component parts and resynthesize fresh plastic that would be just as good as what you started with,” he says.

Sound like a job for an enzyme? Kazlauskas thought so, too. But the likelihood of finding a suitable one in nature was slim because PET didn’t exist for most of evolutionary history. Nevertheless, in a compost heap in Japan, researchers recently found an enzyme that bacteria use to break down the waxy part of plants that could also break down PET.

Kazlauskas, along with graduate student Colin Pierce and colleagues, is working on modifying that enzyme known as cutinase, to improve its ability to degrade PET. The goal, ultimately, is to be able to develop a commercially viable way to turn old PET into new plastics without experiencing the loss of quality. This would not only reduce the load of plastic waste, it would also reduce pressure to produce more plastic, often from fossil fuels.

Kazlauskas sees huge opportunities beyond PET for efforts to extend nature’s ability to degrade compounds. “There are a lot of cases where we start making stuff and putting it out in nature, and people say it doesn’t degrade,” he says. “We’re finding bugs that can degrade these forever chemicals.” he says. By advancing the ability to modify such natural enzymes to make them do the job even better, the hope is to avoid the buildup of undesirable, manufactured compounds in the environment and reduce the need to make more from raw materials.


Life on the Edge

Turning somersaults in a sulfurous hot spring or clinging tenaciously to life on a glacier, the organisms studied by McKnight Presidential Fellow Trinity Hamilton, associate professor in the department of Plant and Microbial Biology, are the stars in microscopic world’s version of “Survivor.” Having evolved within living things, most enzymes work best under fairly mild conditions with respect to things like temperature and acidity. But not all. In the hot springs of Yellowstone National Park, Hamilton is studying how microbes—and the enzymes they use to carry out the activities of daily life—can survive regular temperature fluctuations of 40 degrees Celsius (104 degrees Fahrenheit) or more. And, on the other end of the spectrum, she’s also looking at how other microorganisms that live on ice maintain their function at low temperatures in the absence of liquid water.

Hamilton studies, among other things, enzymes that facilitate photosynthesis and function well up to 72 degrees Celsius, and then suddenly quit. “We have no idea why,” she says. “It’s really hard to perform autopsies on microbes.”

The ability of bacterial enzymes to function at various temperatures is behind the process that makes it possible to sequence DNA using what is called the polymerase chain reaction (PCR) technique. The enzyme used for this was isolated from bacteria in a hot spring in Yellowstone National Park. A better understanding of how bacteria keep these proteins active under extreme conditions could open the door to advancing our ability to solve other human challenges like preserving food or thriving in the face of climate change.

Molecular Assembly Line 

For Michael Smanski, a McKnight land grant professor in the department of Biochemistry, Molecular Biology, and Biophysics, the focus is on bringing together enzymes from different sources to create an efficient work team that can produce a specific molecule.

Most recently he’s been focusing on serofendic acid, a molecule found in the blood of fetal calves. In the early 2000s, researchers in Japan discovered that serofendic acid could prevent the untimely death of neurons and potentially serve as a therapy for minimizing damage from Parkinson’s disease, strokes, and other neurological trauma. The problem? It occurs in such small quantities that it would take 1,000 calves to make a minute 3 milligrams of active substance—providing dismal prospects for practical use.

Biosynthesis and enzymes to the rescue. Using databases describing enzymes from different organisms and the type of work each does, Smanski and colleagues designed a molecular assembly line that could make serofendic acid from readily available feedstock chemicals. Then they introduced the corresponding genes into a bacterium, enabling it to make the desired product.

As any industrial engineer would know, populating an assembly line with ready workers is only part of the solution, however. For efficiency’s sake, it’s also important to have the right capacity at every step of an assembly process to ensure that partially made products don’t pile up, or a slow step doesn’t drag down everything else. To optimize production of serofendic acid, Smanski has been tweaking the activity levels of the various enzymes relative to each other.

Even as he’s working on a strategy to improve outcomes for individuals with brain disorders, Smanski is also discovering principles that can be applied more broadly to optimizing artificial biosynthetic processes.

Optimizing a process means testing multiple levels of expression for the specific gene that’s coding for each enzyme along the way. If the assembly line consists of 15 enzymes, and researchers want to test five levels of expression for each, that would require 5 15 power—more than 30 billion—individual trials. Using combinatorial mathematics, Smanski is devising a strategy for selecting from those millions of possibilities, a mere 100 or so that are most likely to succeed, making the optimization process far more manageable.

“As improvements in the technical aspects of genetic engineering make it easier to rewrite the genetic blueprints of living organisms, learning how to efficiently sift through all of the possibilities of what-to-write is becoming more important,” Smanski says. “We think that our work at the interface of combinatorial mathematics and genetic engineering will benefit any application that requires more than one or a few genes working together.”


Self-Assembling Scaffold

Bringing multiple enzymes together in an assembly line is far more easily said than done. The molecules involved in sequential steps must be physically located close enough to each other to be able to pass a product-in-the-making down the line. They also must be positioned correctly at their stations so they can accomplish their task.

Distinguished McKnight University Professor Claudia Schmidt-Dannert is on it. Rather than identifying enzymes to string together to accomplish a molecule-making task, she is working on the assembly line itself.

Her goal is to not only design a stable assembly line of enzymes able to make a useful product but to genetically modify a microorganism—say, the bacterium E. coli—so that it can produce it on its own. Such a self-assembling scaffold, she believes, could dramatically improve the function of molecular assembly lines, reducing the cost of producing pharmaceuticals and other useful products.

“If we stabilize enzymes, we can make reactions more efficient,” she says.

Schmidt-Dannert and colleagues recently received a patent for a self-assembling, modular scaffold that co-locates enzymes in a way that enhances their ability to efficiently produce desired molecules. Her current focus is on developing scaffolds as materials that can correctly self-assemble into 3-dimensional architectures to organize and support enzyme functions. This would allow the manufacture of a broad range of chemicals including pharmaceutically active molecules—a process that can be extremely difficult using conventional chemical synthesis methods. 

She’s also applying her strategy to making molecular assembly lines more economical by including enzymes that recycle required co-factors, which are molecules or metals that assist enzymes in assembling a molecular product.

“You need to recycle the [co-factors]. Otherwise, the process is too expensive,” she says. “A scaffold helps make that possible.”


Understanding a Toxic Necessity

Understanding a Toxic Necessity

Jannell Bazurto, assistant professor of Plant and Microbial Biology at the University of Minnesota, is pursuing a better understanding of formaldehyde, a chemical that is carcinogenic, toxic, and produced by all living things.

By Reed Grumann

If you dissected a pig in high school biology, you might remember a sharp, acrid smell permeating the classroom and the teacher’s warning about a carcinogenic chemical called formaldehyde. Though often labeled a killer chemical, every organism on Earth, including humans, produces small amounts of formaldehyde. In very small quantities, it’s manageable. Produce or consume too much, and formaldehyde will kill otherwise healthy cells by attacking critical proteins and DNA.

While most organisms can neutralize small amounts of formaldehyde, researchers are just beginning to understand the mechanisms involved in formaldehyde regulation. Jannell Bazurto, a member of the BioTechnology Institute and an assistant professor of Plant and Microbial Biology, looks for clues in Methylobacterium, a type of bacteria that produces and neutralizes formaldehyde levels that would kill most other microbes.

As their name implies, methylobacteria have a unique ability to metabolize or breakdown, single-carbon molecules like methane and methanol. The process helps the cell maintain enough energy to survive, but also generates formaldehyde as an intermediate step. Fortunately, the bacteria are also uniquely equipped to handle sudden changes in concentrations of the toxin.

A key mechanism of Methylobacterium is an enzyme that converts formaldehyde into less harmful chemicals. While the enzyme is sufficient at normal levels of formaldehyde concentration, it’s not enough to handle exceptionally higher formaldehyde levels. To identify the function of two additional proteins suspected of playing a role in regulating formaldehyde levels, a group of researchers at the University of Idaho removed them from bacterial cells. And just like a cake without sugar and eggs, something was off. “If you don’t have [the two proteins] … you can see [the cells] accidentally overproduce formaldehyde, and they end up secreting it in the growth medium,” says Bazurto.

It’s still unclear exactly how these two proteins keep formaldehyde levels low in methylobacterium, but they aren’t alone in their efforts. Dozens of genes express proteins as formaldehyde levels change—a strong indicator of their importance in regulating the toxin. The challenge for Bazurto is knowing which of these genes, and the proteins they encode, actually play a role in formaldehyde metabolism. By manipulating each gene and looking at the results, Bazurto hopes to crack the code and establish which genes impact formaldehyde metabolism and their role in the process.

Once understood, these metabolic pathways could be hardwired into other microbes (like E. coli) through genetic engineering. Modified E. coli could consume methanol, neutralize formaldehyde, or produce marketable chemicals like biofuels and organic acids. In some facilities, formaldehyde is produced in large quantities as a building block for other chemicals. Wastewater remediation at these facilities would greatly benefit from bacteria genetically modified to directly consume formaldehyde and withstand toxic concentrations.

Throughout its industrial lifecycle, formaldehyde has the potential to creep into our air and water, putting humans at risk of exposure. The relationship between excessive formaldehyde exposure and human health issues—cancer, respiratory issues, and skin irritation—has been well established, yet we still know very little about how humans (and other organisms) sense and handle exposure to formaldehyde. As the search for practical applications in biotechnology, medicine, and environmental remediation continues, Bazurto remains fascinated by the basic science and “scenario where we actually know how to resolve formaldehyde toxicity itself.”

Reed Grumann is a writing intern in the Science Communication Lab, majoring in microbiology and political science. He can be reached at gruma017@umn.edu.

Image courtesy of Janelle Buzurto. Timecourse of Methylobacterium chemotaxing toward a capillary tube that has a formaldehyde plug in it. (Zero and five minutes). Cells seen faintly in the background at zero minutes begin to move toward the plug by the five minute point, forming a halo around the end of the tube.


The Fight for Safer Food

The Fight for Safer Food

To confront the threat of persistent foodborne pathogens, Steve Bowden turns to novel techniques to understand and take down those threats.

By Kyle Wong

Nearly one in six Americans suffer from foodborne illnesses each year, according to the Centers for Disease Control and Prevention (CDC). Scientists like the University of Minnesota’s Steve Bowden are working to change that.

Standard food-safety processes like pasteurization, freezing, and fermentation kill foodborne pathogenic bacteria, but these pathogens evolve to survive. Through mutation and the acquisition of new genes, pathogens can cause outbreaks from unfamiliar sources such as fresh produce, spices, and peanut butter. Bowden, an assistant professor in the Department of Food Science and Nutrition and a member of the BioTechnology Institute, is developing strategies to eliminate new and persistent pathogens.

One common offender is Salmonella, a bacterial species that infects millions of Americans each year, leading to thousands of hospitalizations and hundreds of deaths. Bowden studies how Salmonella responds to stresses in the food environments where it thrives. He seeks to identify common genetic traits that enable Salmonella to survive and grow under varied conditions. Ultimately, he hopes to develop procedures that eliminate harmful bacteria from the food system. “We want to understand why certain outbreaks occur in specific types of food and if there is a correlation with the genes found in those specific types of bacteria,” says Bowden.

To target specific foodborne pathogens, Bowden’s lab engineers a type of virus called a bacteriophage that infects and then kills bacteria. But identifying phages that work is only half the battle. Because pathogens are so diverse, effective treatment requires the right combination of phages to remove all of the pathogen targets and ensure food safety. To make things more complicated, the food matrix can also affect the phage’s efficacy. One cocktail of phages might succeed on one food but fail to remove the same pathogen in another.

Nonetheless, the Food and Drug Administration (FDA) has approved some phage cocktails. They are entirely harmless to humans and assist in the control of foodborne pathogenic bacteria during food processing. Their potential use as a safe, natural method to improve food safety is garnering interest in the food industry. Still, further research is required to enhance their efficacy and improve manufacturing methods.

Despite these challenges, Bowden’s longstanding fascination with molecular biology and microbiology keeps him motivated: “I was surprised by how many foodborne illnesses there are. I want to make use of genome sequencing to try and control these pathogens. What’s interesting about molecular biology is how we can apply it to make the world safer.”

Bowden’s drive to understand foodborne pathogens couldn’t have come at a better time. Addressing global threats to food safety, such as climate change and antibiotic resistance, requires broad thinking and a flexible approach. Bowden brings a global perspective to his work. After earning his Ph.D. in biochemistry at the University of Cambridge, he worked as a postdoc in the United Kingdom and Japan. “I feel lucky to have been in so many labs and learn different perspectives,” he says. “It’s helped broaden my appreciation for different ways to do research.”

The experience helped prepare Bowden for his research at the University of Minnesota. “The drive to understand a problem and develop techniques to study that problem has kept me in academia,” he says. “I’m excited to see what direction it takes.”

Kyle Wong is a writing intern in the University of Minnesota Science Communications Lab, majoring in Microbiology. He can be reached at wong0511@umn.edu

A Micro Lens on a Macroscopic Question

A Micro Lens on a Macroscopic Question

A Q&A with PhD Candidate Anna Bennett
By Reed Grumann 

Anna Bennett, a PhD candidate working in Trinity Hamilton’s lab, collects and studies photosynthetic bacteria that live in the extreme conditions found in Yellowstone’s hot springs. Bennett characterizes these cyanobacteria and their environment, providing data to inform evolutionary models of photosynthesis on Earth. 

How did you end up at the University of Minnesota?

At the time I began the application process for graduate school, I was working at an Air Force base in Ohio. I was researching synthetic biology with E. coli, and I knew that I wanted to get outside more, which is why I was looking into applying for environmental microbiology labs. I was accepted to study at the University of Cincinnati in the Hamilton Lab when she made the decision to move to the University of Minnesota. I decided to move too. I was really excited about her work with hot springs and extreme microbes, so it was the only lab that I interviewed with.

What stuck out to you about these extremophiles as compared to others?

I think it’s really interesting that these bacteria can perform photosynthesis. A lot of people only consider plants and a few types of algae when they think about photosynthesis, but these bacteria can do it, too. In fact, they were the first in Earth’s history to do it, but we still don’t know much about them.

Our basic question is “What did early organisms that performed photosynthesis look like?” I work to develop a better understanding of the physiology and ecology of their modern relatives to inform those evolutionary questions. 

What are the implications of your research?

The data we collect on the physiology and ecology of these cyanobacteria can be used to inform evolutionary models. To put it into broad terms, my results will help inform questions about the evolution of photosynthesis, and since photosynthesis led to oxygen on Earth, questions about the evolution of Earth as a whole. 

You work on the largest and smallest elements of biology—the environment and microbes. How do they complement each other?

Microbes are very important for large scale environmental cycles and tend to be important at the starting point of those cycles. Many of the microbes that we study fix carbon, which means they take carbon in a typically unusable form and make it usable. Since humans and animals are unable to do this for ourselves, we depend on the carbon that plants (and some microbes) fix. So microbes are critically essential for the rest of the environment. Without them we don’t have plants, we don’t have cows, and we don’t have us.


Reed Grumann is a writing intern in the Science Communications Lab, majoring in Microbiology and Political Science. He can be reached at gruma017@umn.edu

Synthesizing Sustainability

Synthesizing Sustainability

UMN scientists produce high-value beta-lactones from waste for use in antibiotic and anti-cancer therapies.

By: Katie Sabbia

From biofuels to antibiotics

Sustainability. It’s more than a buzzword. Recycling is a key component in a circular economy, where consumer and industrial waste become raw materials instead of landfill. University of Minnesota biochemist Larry Wackett sees high-value beta-lactones as ideal targets in a new circular economy. His laboratory works with genetically engineered strains of E. coli that convert fatty acids into beta-lactones – a key component of industrial products from pesticides to antibiotics and anti-cancer agents. Chemical synthesis of beta-lactones is painstaking and costly with yields as low as 1%. The Wackett lab’s technology could provide a reliable and efficient pipeline at a fraction of the cost.

An expert in biocatalysis, Wackett uses enzymes to transform organic compounds, whether breaking down environmental toxins or synthesizing chemicals for agriculture and industry. While working on a Department of Energy grant to develop ethanol substitutes, his lab inserted genes from soil bacteria into E. coli. They planned to use fatty acids to synthesize hydrocarbon fuels, but in the process, James Christenson, then a graduate student in the Wackett lab, made a crucial discovery.

While analyzing precursor molecules in hydrocarbon biosynthesis, he identified one intermediate molecule as a beta-lactone.

Christenson, who went on to earn his doctoral degree in Wackett’s lab, carefully isolated and identified the enzymes and other components of the chemical reactions and repeated the steps in vitro. Scientists already knew that some bacteria produced beta-lactones, but Christenson’s work revealed the biochemical mechanism by which they are created. For the first time, the beta-lactones could be made biologically by a directed process. Christenson presented his discovery at the Enzyme Mechanisms Conference in 2017 where he was sole recipient of the Founder’s Award in a competitive field of world class researchers.

“We have published a lot of papers on how to make hydrocarbons, so we did the work we set out to do,” Wackett explains. “But in the process, we discovered something else. Beta-lactones are highly valued as anti-cancer, anti-obesity, and antibiotic agents. As antibiotic resistance increases, this may be even more important than the biofuels project.”

Beta-lactones are similar in structure to the key components of antibiotics like penicillin that work by inhibiting cell wall production in the targeted bacteria. Antibiotic-resistant bacteria have evolved to resist these molecules, and rendering them ineffective. In the war on antibiotic resistance, beta-lactones could be our next line of defense.

Small molecule, big impact

“We can purify enzymes at very high yields, and we can make a lot of different structures with different properties.” To understand the structure of these complex enzymes and how they interact with other molecules, he turned to longtime collaborator Carrie Wilmot. Wilmot, an X-ray crystallographer and professor in the Department of Biochemistry, Molecular Biology, and Biophysics, helped identify the structures and mechanisms of the proteins producing the beta-lactones. Her lab produced three-dimensional models of the molecules using the diffraction patterns derived from exposing protein crystals to high energy X-rays. Viewing such models on a computer will help the team find and engineer the best enzymes to synthesize new and useful beta-lactones.

Wackett is committed to seeing his research applied outside the academic laboratory. He and his co-workers filed a patent for the process which can be used to make beta-lactones with different properties and ideally, some will be useful as drugs to treat cancer or bacterial infections.

With a seed grant from the MnDRIVE Environment Initiative, Wackett is partnering with Minnesota-based life science firm Bio-Techne to look at commercial processes for producing beta-lactones. The ultimate goal is to develop a key component of the circular economy: converting wastes to high value products.

Katie is an Industrial & Systems Engineering major in the University of Minnesota’s College of Science and Engineering and an intern in the BioTechnology Institute’s Science Communications Training Program

Photo taken by Mikaela Armstrong. Mikaela is a Graphic Design major in the University of Minnesota’s College of Design and an intern in the BioTechnology Institute’s Science Communications Training Program