Molecular cloning, over-expression and enzymatic characterization of an endo-acting beta-1,3-glucanase from marine bacterium Mesoflavibacter zeaxanthinifaciens S86 in Escherichia coli SCIE SCOPUS KCI

Cited 1 time in WEB OF SCIENCE Cited 2 time in Scopus
Title
Molecular cloning, over-expression and enzymatic characterization of an endo-acting beta-1,3-glucanase from marine bacterium Mesoflavibacter zeaxanthinifaciens S86 in Escherichia coli
Author(s)
Lee, Youngdeuk; Lee, Ji-Hyun; Shim, Won-Bo; Elvitigala, Don Anushka Sandaruwan; Zoysa, Mahanama De; Lee, Su-Jin; Heo, Soo-Jin; Lee, Jehee; Kang, Do-Hyung; Oh, Chulhong
KIOST Author(s)
Lee, Youngdeuk(이영득)Heo, Soo Jin(허수진)Kang, Do-Hyung(강도형)Oh, Chulhong(오철홍)
Publication Year
2014-12
Abstract
Glucanases are involved in degradation of glucans. Here, we report a new endo-beta-1,3-glucanase Mzl86 identified in Mesoflavibacter zeaxanthinifaciens S86. The deduced amino-acid sequence of Mzl86 showed highest similarity (45.1%) with Leeuwenhoekiella blandensi and thus placed in glycosyl hydrolase family 16. Purified recombinant protein (rMz186) showed an optimum enzyme activity against laminarin at 50a"integral and pH 8. The enzyme was stable at 50a"integral for 1 hour (maintaining 80% of its maximum activity) and was strongly activated (187%) in the presence of 2.5 mM manganese. Substrate-specific activities of rMzl86 against laminarin, barley beta-glucan and lichenan were 261, 128 and 115 unit/mg, respectively. rMzl86 degraded laminarioligosaccharides (lager than biose) and laminarin while producing mainly biose and glucose. Molecular and biochemical properties reveal that rMzl86 shares typical features of beta-1,3-glucanase (EC 3.2.1.39) and thus is a potential candidate for use in agriculture, drug, chemical and bioethanol industries.
ISSN
1738-5261
URI
https://sciwatch.kiost.ac.kr/handle/2020.kiost/2660
DOI
10.1007/s12601-014-0040-7
Bibliographic Citation
OCEAN SCIENCE JOURNAL, v.49, no.4, pp.425 - 432, 2014
Publisher
KOREA OCEAN RESEARCH DEVELOPMENT INST
Keywords
beta-1,3-glucanase; Mesoflavibacter zeaxanthinifaciens; recombinant enzyme; laminarinase activity; biochemical properties
Type
Article
Language
English
Document Type
Article
Publisher
KOREA OCEAN RESEARCH DEVELOPMENT INST
Related Researcher
Files in This Item:
There are no files associated with this item.

qrcode

Items in ScienceWatch@KIOST are protected by copyright, with all rights reserved, unless otherwise indicated.

Browse