Journal
CHINESE JOURNAL OF CHEMICAL ENGINEERING
Volume 25, Issue 4, Pages 487-492Publisher
CHEMICAL INDUSTRY PRESS
DOI: 10.1016/j.cjche.2016.08.027
Keywords
Immobilization; Enzyme; Biocatalysis; Nitrile hydratase
Categories
Funding
- National Nature Science Foundation of China [21306039, 21276060, 21276062]
- Natural Science Foundation of Hebei Province [B2015202082, B2016202027]
- Tianjin City High School Science & Technology Fund Planning Project [20140513]
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Cross-linked enzymeaggregates (CLEAs) of nitrile hydratase (NHase) ES-NHT-118 from Escherichia coli were prepared by using ammonium sulfate as precipitating agent followed by cross-linking with dextran polyaldehyde for the first time. In this process, egg white was added as protein feeder for facilitating the formation of CLEAs. The optimal conditions of the immobilization process were determined. Michaelis constants (Km) of free NHase and NHase CLEAs were also determined. The NHase CLEAs exhibited increased stability at varied pH and temperature conditions compared to its free counterpart. When exposed to high concentrations of acrylamide, NHase CLEAs also exhibited effective catalytic activity. (C) 2016 The Chemical Industry and Engineering Society of China, and Chemical Industry Press. All rights reserved.
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