The effects of macromolecular crowding and surface charge on the properties of an immobilized enzyme: activity, thermal stability, catalytic efficiency and reusability-Reference-Cited by-同舟云学术

The effects of macromolecular crowding and surface charge on the properties of an immobilized enzyme: activity, thermal stability, catalytic efficiency and reusability

Published:2017 Issue:60 Volume:7 Page:38028-38036
ISSN:2046-2069
Container-title:RSC Advances
language:en
Short-container-title:RSC Adv.

Author:

Yang Qiong¹²³⁴⁵,Wang Bochu¹²³⁴⁵^ORCID,Zhang Zhi¹²³⁴⁵,Lou Deshuai⁶⁷⁸⁹¹⁰,Tan Jun⁶⁷⁸⁹¹⁰,Zhu Liancai¹²³⁴⁵^ORCID

Affiliation:

1. Key Laboratory of Biorheological Science and Technology (Chongqing University)

2. Ministry of Education

3. College of Bioengineering

4. Chongqing University

5. Chongqing 400030

6. Chongqing Key Laboratory of Medicinal Resources in the Three Gorges Reservoir Region

7. School of Biological & Chemical Engineering

8. Chongqing University of Education

9. Chongqing 400067

10. PR China

Abstract

The microenvironment around an immobilized enzyme molecule significantly influences the properties of the immobilized enzyme.

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemical Engineering,General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2017/RA/C7RA06544B

Reference36 articles.

1. Dispelling the Myths--Biocatalysis in Industrial Synthesis

2. Immobilizing Enzymes: How to Create More Suitable Biocatalysts

3. Enhanced functionality and stabilization of a cold active laccase using nanotechnology based activation-immobilization

4. Selective oxidation of glycerol to 1,3-dihydroxyacetone by covalently immobilized glycerol dehydrogenases with higher stability and lower product inhibition

5. Immobilization of β-glucosidase from Aspergillus niger on κ-carrageenan hybrid matrix and its application on the production of reducing sugar from macroalgae cellulosic residue

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