Enhancement of thermal stability of proteinase K by biocompatible cholinium-based ionic liquids-Reference-Cited by-同舟云学术

Enhancement of thermal stability of proteinase K by biocompatible cholinium-based ionic liquids

Published:2022 Issue:21 Volume:24 Page:13057-13065
ISSN:1463-9076
Container-title:Physical Chemistry Chemical Physics
language:en
Short-container-title:Phys. Chem. Chem. Phys.

Author:

Li Rui¹²^ORCID,Liu Zhuo²³,Jiang Fan¹²^ORCID,Zhao Yang⁴,Yang Guangyu⁵,Hong Liang¹²³^ORCID

Affiliation:

1. School of Physics and Astronomy, Shanghai Jiao Tong University, Shanghai 200240, China

2. Institute of Natural Sciences, Shanghai Jiao Tong University, Shanghai 200240, China

3. Shanghai National Center for Applied Mathematics (SJTU center), MOE-LSC, Shanghai Jiao Tong University, Shanghai 200240, China

4. Institute of Biothermal Science and Technology, University of Shanghai for Science and Technology, Shanghai 200093, China

5. State Key Laboratory of Microbial Metabolism, School of Life Sciences and Biotechnology, Shanghai Jiao Tong University, Shanghai 200240, China

Abstract

The anions of cholinium-based IL molecules interact with the protein through hydrogen bonding and other interactions, causing great influence on the thermal stability and enzymatic activity of proteinase K.

Funder

National Natural Science Foundation of China

Publisher

Royal Society of Chemistry (RSC)

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

Link

http://pubs.rsc.org/en/content/articlepdf/2022/CP/D1CP04782E

Reference64 articles.

1. Insight Derived from Molecular Dynamics Simulation into Substrate-Induced Changes in Protein Motions of Proteinase K

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4. High-level expression of Proteinase K from Tritirachium album Limber in Pichia pastoris using multi-copy expression strains

5. Characterizing structural features of cuticle-degrading proteases from fungi by molecular modeling

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