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Covalent immobilization of ω-transaminase from Vibrio fluvialis JS17 on chitosan beads

Paper ID Volume ID Publish Year Pages File Format Full-Text
35995 45117 2007 4 PDF Available
Title
Covalent immobilization of ω-transaminase from Vibrio fluvialis JS17 on chitosan beads
Abstract

Chitosan beads were prepared by emulsion method and used for the immobilization of ω-transaminase of Vibrio fluvialis. The yield of enzyme immobilization (54.3%) and its residual activity (17.8%) were higher than those obtained with other commercial beads. ω-Transaminase was effectively immobilized on the chitosan beads at pH 6.0. The optimal pH of the immobilized enzyme was pH 9.0, which is the same as that of the free enzyme. The immobilized enzyme on chitosan beads retained ca. 77% of its conversion after five consecutive reactions with the 25 mM substrate, while the immobilized enzyme on Eupergit® C retained 12%. Also, the immobilized ω-transaminase on chitosan bead retained 70% of initial activity when it's stored at 4 °C for 3.5 weeks. Addition of the co-factor, pyridoxal 5-phosphate (PLP), was needed to maintain the stability of the immobilized ω-transaminase.

Keywords
Enzyme immobilization; Chitosan bead; Emulsion method; ω-Transaminase; Reusability; Vibrio fluvialis
First Page Preview
Covalent immobilization of ω-transaminase from Vibrio fluvialis JS17 on chitosan beads
Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 42, Issue 5, May 2007, Pages 895–898
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering