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Catalysts 2017, 7(1), 4; doi:10.3390/catal7010004

Synthesis and Characterization of Highly Stabilized Polymer–Trypsin Conjugates with Autolysis Resistance

1
Laboratory of Pharmaceutical Physical Chemistry, Department of Drug Delivery Technology and Sciences, Gifu Pharmaceutical University, 1-25-4, Daigaku-Nishi, Gifu 501-1196, Japan
2
Department of Pharmaceutical Physical Chemistry, College of Pharmaceutical Sciences, Matsuyama University, 4-2 Bunkyo-cho, Matsuyama, Ehime 790-8578, Japan
3
Faculty of Human Welfare, Chubu Gakuin University, 2-1 Kirigaoka, Sek-shi, Gifu 501-3993, Japan
*
Author to whom correspondence should be addressed.
Academic Editor: David D. Boehr
Received: 30 November 2016 / Revised: 20 December 2016 / Accepted: 22 December 2016 / Published: 26 December 2016
(This article belongs to the Special Issue Immobilized Enzymes: Strategies for Enzyme Stabilization)
View Full-Text   |   Download PDF [1806 KB, uploaded 26 December 2016]   |  

Abstract

Protein digestion by trypsin has been widely used in many industrial and research applications. However, extensive use of trypsin is limited because of the rapid decrease in enzymatic activity caused by autolysis at optimal pH and temperature. To improve the enzymatic performance of trypsin, we synthesized highly stabilized polymer–trypsin conjugates using vinylmethylether-maleic acid copolymer (VEMAC) via multi-point attachment. The VEMAC modification significantly enhanced the thermal stability of trypsin, and the resulting conjugates showed a strong resistance to autolysis. VEMAC-modified trypsin (VEMAC-Tryp) showed maximum activity at 55 °C and at 1.4-fold higher levels than that of unmodified trypsin. Bovine serum albumin was effectively digested by VEMAC-Tryp, indicating that the modified trypsin can be used for digestion of high molecular weight substrates. VEMAC modification is a simple and cost-effective strategy to obtain fully active modified enzymes, and may be used to develop bioreactors. View Full-Text
Keywords: trypsin; polymer–enzyme conjugate; vinylmethylether-maleic acid copolymer; enzymatic activity; protein digestion trypsin; polymer–enzyme conjugate; vinylmethylether-maleic acid copolymer; enzymatic activity; protein digestion
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Sasai, Y.; Kanno, H.; Doi, N.; Yamauchi, Y.; Kuzuya, M.; Kondo, S.-I. Synthesis and Characterization of Highly Stabilized Polymer–Trypsin Conjugates with Autolysis Resistance. Catalysts 2017, 7, 4.

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