Preparation of cross-linked enzyme aggregates of nitrile hydratase ES-NHT-118 from <i>E. coli</i> by macromolecular cross-linking agent

Liya Zhou; Haixia Mou; Jing Gao; Li Ma; Ying He; Yanjun Jiang

doi:10.1016/j.cjche.2016.08.027

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Preparation of cross-linked enzyme aggregates of nitrile hydratase ES-NHT-118 from E. coli by macromolecular cross-linking agent

Biotechnology and Bioengineering | Updated：2026-01-06

- Preparation of cross-linked enzyme aggregates of nitrile hydratase ES-NHT-118 from E. coli by macromolecular cross-linking agent
- Preparation of cross-linked enzyme aggregates of nitrile hydratase ES-NHT-118 from E. coli by macromolecular cross-linking agent
- 中国化学工程学报（英文版） 2017年25卷第4期页码：487-492
- Affiliations：
  
  1. School of Chemical Engineering and Technology, Hebei University of Technology,Tianjin,China,300130
  2. Hebei Provincial Key Lab of Green Chemical Technology and High Efficient Energy Saving, Hebei University of Technology,Tianjin,China,300130
- Author bio：
- Funds：
- DOI：10.1016/j.cjche.2016.08.027
  中图分类号：
- 纸质出版：2017
- Accepted：
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Liya Zhou, Haixia Mou, Jing Gao, 等. Preparation of cross-linked enzyme aggregates of nitrile hydratase ES-NHT-118 from E. coli by macromolecular cross-linking agent[J]. 中国化学工程学报（英文版）, 2017,25(4):487-492. DOI: 10.1016/j.cjche.2016.08.027.

by macromolecular cross-linking agent[J]. , 2017, 25(4): 487-492.
Liya Zhou, Haixia Mou, Jing Gao, 等. Preparation of cross-linked enzyme aggregates of nitrile hydratase ES-NHT-118 from E. coli by macromolecular cross-linking agent[J]. 中国化学工程学报（英文版）, 2017,25(4):487-492. DOI: 10.1016/j.cjche.2016.08.027. DOI：

by macromolecular cross-linking agent[J]. , 2017, 25(4): 487-492. DOI： 10.1016/j.cjche.2016.08.027.

摘要

Abstract

Cross-linked enzyme aggregates (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 (

) 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.

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Preparation of cross-linked enzyme aggregates of nitrile hydratase ES-NHT-118 from E. coli by macromolecular cross-linking agent

Preparation of cross-linked enzyme aggregates of nitrile hydratase ES-NHT-118 from E. coli by macromolecular cross-linking agent

DOI：10.1016/j.cjche.2016.08.027

摘要

Abstract

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