Rational design for enhancing promiscuous activity of Candida antarctica lipase B: a clue for the molecular basis of dissimilar activities between lipase and serine-protease-Reference-Cited by-同舟云学术

Rational design for enhancing promiscuous activity of Candida antarctica lipase B: a clue for the molecular basis of dissimilar activities between lipase and serine-protease

Published:2013 Issue:8 Volume:3 Page:2590
ISSN:2046-2069
Container-title:RSC Advances
language:en
Short-container-title:RSC Adv.

Author:

Jung Suhyun,Kim Juhyun,Park Seongsoon

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemical Engineering,General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2013/RA/C2RA23333A

Reference28 articles.

1. Bacterial Biocatalysts: Molecular Biology, Three-Dimensional Structures, and Biotechnological Applications of Lipases

2. Serine Proteases: Structure and Mechanism of Catalysis

3. Use of nonproteases in peptide synthesis

4. Lipase catalysed synthesis of peptides: Preparation of a penicillin G precursor and other peptides

5. Peptide synthesis catalyzed by lipases in anhydrous organic solvents

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