Date of Award
5-2014
Level of Access Assigned by Author
Campus-Only Thesis
Degree Name
Master of Science (MS)
Department
Chemistry
Advisor
Barbara J.W. Cole
Second Committee Member
Raymond C. Fort, Jr.
Third Committee Member
Bruce L. Jensen
Abstract
Environmental concerns about chlorinated organics have created a need for new technologies to replace chlorine in pulp bleaching. One alternative is a biological bleaching that involves the oxidative enzyme laccase. Different factors affect the catalytic efficiency of the enzyme. Previous docking experiments in our group have shown that non-reducing sugar molecules like 4-methoxyphenyl-β-D-glucopyranoside can bind to the enzyme’s active site and have the potential to inhibit the activity of the enzyme. Therefore, to see the effect of such non-reducing sugars, different sets of kinetic experiments were carried out both in the presence and absence of sugar molecules. Comparison of the kinetic parameters Km and kcat obtained by preparing Lineweaver-Burk plots of their respective data were then used as the basis for the determination of the different types of enzyme inhibition. Determinations of the kinetic parameters were done using five different substrate concentrations but with the same enzyme and inhibitor concentrations. The reactions were carried out at 20°C ± 1°C and samples for analysis were quenched using NaOH prior to analysis.
Recommended Citation
Zerayesus, Tesfahiwet Adam, "Kinetic Studies of Laccase-Catalyzed Reactions" (2014). Electronic Theses and Dissertations. 2111.
https://digitalcommons.library.umaine.edu/etd/2111