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Title 

A highly active endo-beta-1,4-mannanase produced by Cellulosimicrobium sp. strain HY-13, a hemicellulolytic bacterium in the gut of Eisenia fetida

Authors 

Do Young KimS J HamHyun Ju LeeY J KimD H ShinY H RheeKwang Hee SonHo Yong Park

Publisher 

Elsevier

Issue Date 

2011

Citation 

Enzyme and Microbial Technology, vol. 48, no. 4, pp. 365-370

Keywords 

Cellulosimicrobium sp. strain HY-13Eisenia fetidaGut bacteriumHighly active endo-β-1,4-mannanaseMannan-degrading enzyme

Abstract 

A xylanolytic gut bacterium isolated from Eisenia fetida, Cellulosimicrobium sp. strain HY-13, produced an extracellular glycoside hydrolase capable of efficiently degrading mannose-based substrates such as locust bean gum, guar gum, mannotetraose, and mannopentaose. The purified mannan-degrading enzyme (ManK, 34,926 Da) from strain HY-13 was found to have an N-terminal amino acid sequence of DEATTDGLHVVDD, which has not yet been identified. Under the optimized reaction conditions of 50 °C and pH 7.0, ManK exhibited extraordinary high specific activities of 7109 IU/mg and 5158 IU/mg toward locust bean gum and guar gum, respectively, while the enzyme showed no effect on sugars substituted with p-nitrophenol and various non-mannose carbohydrates. Thin layer chromatography revealed that the enzyme degraded locust bean gum to mannobiose and mannotetraose. No detectable amount of mannose was produced from hydrolytic reactions with the substrates. ManK strongly attached to Avicel, β-cyclodextrin, lignin, and poly(3-hydroxybutyrate) granules, but not bound to chitin, chitosan, curdlan, or insoluble oat spelt xylan. The aforementioned characteristics of ManK suggest that it is a unique endo-β-1,4-mannanase without additional carbohydrolase activities, which differentiates it from other well-known carbohydrolases.

ISSN 

0141-0229

Link 

http://dx.doi.org/10.1016/j.enzmictec.2010.12.013

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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