NDLI: Molecular cloning, over-expression and enzymatic characterization of an endo-acting β-1,3-glucanase from marine bacterium Mesoflavibacter zeaxanthinifaciens S86 in Escherichia coli

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

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

Content Provider	Springer Nature Link
Author	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
Copyright Year	2014
Abstract	Glucanases are involved in degradation of glucans. Here, we report a new endo-β-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 50℃ and pH 8. The enzyme was stable at 50℃ 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 β-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 β-1,3-glucanase (EC 3.2.1.39) and thus is a potential candidate for use in agriculture, drug, chemical and bioethanol industries.
Starting Page	425
Ending Page	432
Page Count	8
File Format	PDF
ISSN	17385261
Journal	Ocean Science Journal
Volume Number	49
Issue Number	4
e-ISSN	20057172
Language	English
Publisher	Korea Ocean Research and Development Institute and The Korean Society of Oceanography
Publisher Date	2015-01-07
Publisher Place	Springer
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	β-1,3-glucanase Mesoflavibacter zeaxanthinifaciens recombinant enzyme laminarinase activity biochemical properties Oceanography Marine & Freshwater Sciences Waste Water Technology Water Pollution Control Water Management Aquatic Pollution
Content Type	Text
Resource Type	Article
Subject	Oceanography

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