Cloning and characterization of a beta-1,4-mannanase 5C possessing a family 27 carbohydrate-binding module from a marine bacterium, Vibrio sp. strain MA-138

Bioscience, Biotechnology, and Biochemistry
Megumi TanakaToshiyoshi Araki

Abstract

The beta-1,4-mannanase 5C gene (man5C) of Vibrio sp. strain MA-138 was cloned and expressed in Escherichia coli. The man5C gene consisted of 2,010 bp nucleotides encoding a protein of 669 amino acids with a predicted molecular weight of 76,309. beta-1,4-Mannanase (Man5C) is a modular enzyme composed of a catalytic module belonging to glycoside hydrolase family 5, a linker region, and a putative carbohydrate-binding module (CBM) belonging to family 27. Recombinant Man5C exhibited maximal activity at 50 degrees C at pH 7.0, and it had a K(m) of 0.6 mg ml(-1) and a V(max) of 556.2 micromol min(-1) mumol(-1) for glucomannan. Binding studies revealed that the C-terminal putative CBM27 had the ability to bind soluble beta-mannans and contributed to increasing the rate of depolymerization by binding to the polymeric substrate. Man5C of Vibrio sp. MA-138 is the first non-extremophile enzyme to be identified as a beta-mannanase possessing CBM27.

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Citations

May 4, 2012·Journal of Experimental Botany·María del Carmen Rodríguez-GacioAngel J Matilla
Feb 9, 2012·Applied Microbiology and Biotechnology·Prakram Singh ChauhanNaveen Gupta
Jul 19, 2014·Bioscience, Biotechnology, and Biochemistry·Yoshihiro HakamadaShinichi Ohashi
Dec 21, 2016·Biological Reviews of the Cambridge Philosophical Society·Simon LadevèzeGabrielle Potocki-Véronèse
Oct 10, 2020·Critical Reviews in Biotechnology·Gaurav Singh Kaira, Mukesh Kapoor

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