Enzymes serve as catalysts to many biological processes, and so they are not used up in reactions and they may be recovered and reused. However, in a laboratory setting, reactions involving enzymes can leave the enzyme unrecoverable. Kevin Boettger ’13 and Christopher Richardson ’14 will spend the summer working under Professor of Chemistry Tim Elgren to trap enzymes in Sol gels, making them more stable and recyclable. Their project is titled “Encapsulation of Enzymes.”
Both Boettger’s and Richardson’s research was funded through the Edward and Virginia Taylor Fund for Student/Faculty Research in Chemistry, established in 2008 through a gift from Ted ’46 and Virginia to inspire students interested in chemical research and to facilitate their work with outstanding faculty.
When enzymes and buffer are added to the sol precursor, a gel forms with the enzymes trapped inside the pores of the nanomaterial. This process makes the enzyme at once less reactive but more stable. The group is working with different gels and measuring the effectiveness of gels using a UV-Vis spectrophotometer.
Boettger’s task is to create gels out of alginic acid in water and encapsulate an enzyme called horseradish peroxidase. When exposed to this enzyme, the substrate ABTS and hydrogen peroxide react to produce ABTS radicals, which have a visible green color in solution. Boettger is comparing the reaction rate and the amount of ABTS radical product formed in this reaction to reactions in which the enzyme is encapsulated in sol gels. Boettger initially hypothesized that the alginate gels would leak more enzyme than the sol gels and would thus be a less effective medium, but his most recent data suggests that the alginate medium is in fact more reactive than the sol.
While Professor Elgren has done work with enzyme encapsulation in gels before, he has not yet worked with alginate gels, allowing Boettger the opportunity to conduct innovative experiments. Later in the summer, Boettger looks forward to working with nitrile hydratase, another enzyme that typically catalyzes the hydration of nitriles to amines.
Richardson is working with similar techniques to create a sensor for amines using the enzyme amine oxidase, which catalyzes the oxidation of biogenic amines. Amines can be found in certain foods that have been exposed to bacteria and in residues of some explosives. Richardson hopes that his findings may be useful to detecting when food is starting to rot.
Richardson is working with the enzyme glucose oxidase, which oxidizes glucose to hydrogen peroxide. This hydrogen peroxide can then react with horseradish peroxidase and ABTS to produce ABTS radicals, the reaction that Boettger is working with. After becoming well-acquainted with glucose oxidase, Richardson will begin work with amine oxidase. He will encapsulate the enzyme in sol-gel and analyze its reactivity.
In his free time, Boettger, a biochemistry major with a music minor, plays oboe and bass guitar. He participates in a chamber group and enjoys skiing. Richardson, who plans on pursuing a major in chemistry or biochemistry, plays violin in the Hamilton orchestra and works in the athletic training room.
Enzymes function as vital catalysts in biological functions, and these chemicals can be equally useful in a laboratory setting. Boettger’s and Richardson’s project promises to help make these catalysts as recyclable as possible, preventing unnecessary waste while stabilizing the enzymes.
Kevin Boettger is a graduate of Westwood High School in Massachusetts. Christopher Richardson is a graduate of Montpelier High School in Vermont.