Rational design of Pleurotus eryngii versatile ligninolytic peroxidase for enhanced pH and thermal stability through structure-based protein engineering-Reference-Cited by-同舟云学术

Rational design of Pleurotus eryngii versatile ligninolytic peroxidase for enhanced pH and thermal stability through structure-based protein engineering

Published:2017-11-01 Issue:11 Volume:30 Page:743-751
ISSN:1741-0126
Container-title:Protein Engineering, Design and Selection
language:en
Short-container-title:

Author:

Gao Yu¹,Li Jian-Jun²,Zheng Lanyan¹,Du Yuguang²

Affiliation:

1. Department of Microbiology and Parasitology, China Medical University, No. 77 Puhe Road, Shenyang 110122, Liaoning Province, China

2. National Key Laboratory of Biochemical Engineering, National Engineering Research Center for Biotechnology (Beijing), Key Laboratory of Biopharmaceutical Production & Formulation Engineering, PLA, Institute of Process Engineering, Chinese Academy of Sciences, No. 1 North 2nd Street, Beijing 100190, China

Funder

National Science Foundation of China

Beijing Natural Science Foundation

Publisher

Oxford University Press (OUP)

Subject

Molecular Biology,Biochemistry,Bioengineering,Biotechnology

Link

http://academic.oup.com/peds/article-pdf/30/11/743/22541662/gzx055.pdf

Reference43 articles.

1. Proton NMR investigation into the basis for the relatively high redox potential of lignin peroxidase.

2. NMR study of manganese(II) binding by a new versatile peroxidase from the white-rot fungus Pleurotus eryngii