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Title 

Cloning and characterization of a modular GH5 beta-1,4-mannanase with high specific activity from the fibrolytic bacterium Cellulosimicrobium sp. strain HY-13

Authors 

Do Young KimS J HamHyun Ju LeeHan-Young ChoJi-Hoon KimY J KimD H ShinY H RheeKwang Hee SonHo Yong Park

Publisher 

Elsevier

Issue Date 

2011

Citation 

Bioresource Technology, vol. 102, no. 19, pp. 9185-9192

Keywords 

β-1,4-MannanaseCellulosimicrobium sp. strain HY-13Eisenia fetidaGut bacteriumHigh specific activity

Abstract 

The gene (1272-bp) encoding a β-1,4-mannanase from a gut bacterium of Eisenia fetida, Cellulosimicrobium sp. strain HY-13 was cloned and expressed in Escherichia coli. The recombinant β-1,4-mannanase (rManH) was approximately 44.0 kDa and has a catalytic GH5 domain that is 65% identical to that of the Micromonospora sp. β-1,4-mannosidase. The enzyme exhibited the highest catalytic activity toward mannans at 50 °C and pH 6.0. rManH displayed a high specific activity of 14,711 and 8498 IU mg-1 towards ivory nut mannan and locust bean gum, respectively; however it could not degrade the structurally unrelated polysaccharides, mannobiose, or p-nitrophenyl sugar derivatives. rManH was strongly bound to ivory nut mannan, Avicel, chitosan, and chitin but did not attach to curdlan, insoluble oat spelt xylan, lignin, or poly(3-hydroxybutyrate). The superior biocatalytic properties of rManH suggest that the enzyme can be exploited as an effective additive in the animal feed industry.

ISSN 

0960-8525

Link 

http://dx.doi.org/10.1016/j.biortech.2011.06.073

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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