상세 정보

underline
Metadata Downloads : dc(xml) or Excel
Cited 0 time in scopus ci

Title 

Biocatalytic characterization of an endo-β-1,4-mannanase produced by Paenibacillus sp. strain HY-8

Authors 

Do Young KimC W ChungHan Young ChoY H RheeD H ShinKwang- Hee SonHo Yong Park

Publisher 

Springer Verlag (Germany)

Issue Date 

2017

Citation 

Biotechnology Letters

Keywords 

Endo-β-1,4-mannanaseGut bacteriumLongicorn beetleMoechotypa diphysisPaenibacillus sp. strain HY-8

Abstract 

Objectives: To evaluate the biocatalytic characteristics of a new endo-β-1,4-d-mannan-degrading enzyme (ManP) from Paenibacillus sp. strain HY-8, a gut bacterium of the longicorn beetle Moechotypa diphysis. Results: Purified ManP (32?kDa) with an N-terminal amino acid sequence of APSFAVGADFSYVPG displayed the greatest degree of biocatalytic activity toward locust bean gum (LBG) at 55?°C and pH 7.0. The enzyme degraded LBG, guar gum, ivory nut mannan, and mannooligosaccharides (M2?M5), but did not exhibit any hydrolytic activity against structurally unrelated substrates. The biocatalytic activity of ManP against LBG and guar gum was 695 and 450?U?mg?1, respectively. Especially, enzymatic hydrolysis of mannobiose yielded a mixture of mannose (16.6?%) and mannobiose (83.4?%), although the degree of mannobiose degradation by ManP with was relatively limited. Conclusion: The present results suggest that ManP is an endo-β-1,4-mannanase and is distinct from various other characterized endo-β-1,4-mannanases.

ISSN 

0141-5492

Link 

http://dx.doi.org/10.1007/s10529-016-2228-7

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


There are no files associated with this item.
qrcode

FusionCharts.
DSpace Software Coptright(c) 2010 MIT and Hewleft-Packard  /  KRIBB-REPOSITORY ( Email:jakim@kribb.re.kr)