Special to the Tribune-Star
TERRE HAUTE —
As students file into class this fall for their biochemistry course, Indiana State junior chemistry major Seth Lutjemeyer will have a head start after completing the Summer Undergraduate Research Experience.
Instead of spending summer away from campus, Lutjemeyer reported to the biochemistry laboratory on campus performing studies on mushroom tyrosinase. Tyrosinase is an enzyme found in fruits and vegetables and causes the browning of the foods. Lutjemeyer sought to get a better understanding of how the enzyme functions. As a byproduct of his examinations of the enzyme, Lutjemeyer has spent hours learning invaluable lab techniques specific to biochemistry and feels more prepared for his upcoming bio-chemistry course.
The SURE program is sponsored by the university and offers students the opportunity to participate in summer research. This summer, the program included 30 ISU students working with faculty members in a variety of research across the natural sciences.
“At the beginning, it was a whole new experience,” Lutjemeyer said. “I was skeptical at first but I learned so much now that it’s over and hope to do it again.”
Lutjemeyer said the experience built upon knowledge acquired in the classroom. He was interested in taking part in the program because he wanted to do more hands-on work in chemistry. The SURE program provided just that.
Despite having a career plan to attend dental school upon graduation, Lutjemeyer said he has taken a liking to doing research because of the program.
“It can be my back-up plan,” Lutjemeyer said.
Advised by William Flurkey, ISU chemistry and physics professor, Lutjemeyer conducted three studies on the mushroom tyrosinase during the 10-week program.
“This enzyme is involved in browning reactions in fruits and vegetables, so preventing this enzyme from working will theoretically improve food appearance and food quality,” Flurkey said.
Flurkey said researchers hoped to understand more about the enzyme but real-world applications of the research are still in the distant future.
The first study was to protect the latent form of the mushroom tyrosinase by adding protease inhibitors.
“We are trying to determine if there is a way to preserve the latent form,” Flurkey said. “If we can do that, we can do studies on the dormant form.”
The second study looked at activating the enzyme by using a detergent and then removing that detergent to see if it is possible to return it back to its latent form.
“It’s been proposed that once you activate it, it stays active but we are seeing if it is reversible,” Lutjemeyer said.
He said they were able to convert some back to latent but less than expected.
The third study focused on the separation of active and latent forms of tyrosinase using chromatography methods.
“Usually biochemists like to study different forms of enzymes,” Flurkey said. “So it would be nice to be able to separate them so you can study them individually.”