Cutinase in organic media : preparing immobilized cutinase, studies of catalyst solvent tolerance, thermal stability, and structure-function relationship in enantioselective transesterifications

Authors
Su, An
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Other Contributors
Gross, Richard A.
Bystroff, Christopher, 1960-
Colón, Wilfredo
Linhardt, Robert J.
Makhatadze, George I.
Issue Date
2018-05
Keywords
Chemistry
Degree
PhD
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This electronic version is a licensed copy owned by Rensselaer Polytechnic Institute, Troy, NY. Copyright of original work retained by author.
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Abstract
Cutinase is an α/β hydrolase with a Ser-His-Asp catalytic triad that has been known to hydrolyze cutin as well as a variety of polyester and polyamides. Cutinase has been considered as a bridge between esterase and lipase because of its ability to catalyze in solution as well as in lipid phase. However, studies of cutinase in organic media are many fewer than those of lipase and esterase though an increasing number of cutinases are being discovered and characterized. Hence, this dissertation will focus on preparing cutinase as biocatalysts in organic media, characterizing the catalysts’ solvent tolerance and thermostability, and studying its structure-function relationship in enantioselective transesterifications.
Description
May 2018
School of Science
Department
Dept. of Chemistry and Chemical Biology
Publisher
Rensselaer Polytechnic Institute, Troy, NY
Relationships
Rensselaer Theses and Dissertations Online Collection
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