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枯草芽孢杆菌WD-23 β-甘露聚糖酶的纯化及其酶学性质(PDF)

《南京林业大学学报(自然科学版)》[ISSN:1000-2006/CN:32-1161/S]

Issue:
2014年03期
Page:
88-92
Column:
研究论文
publishdate:
2014-05-15

Article Info:/Info

Title:
Inrestigation on the purification methods of β-mannase from Bacillus subtilis WD-23 and studies on enzymatic properties
Article ID:
1000-2006(2014)03-0088-05
Author(s):
ZHANG Bing XIANG Bingbing CUI Daizong ZHAO Min*
College of Life Science, Northeast Forestry University, Harbin 150040, China
Keywords:
β-mannase purification enzymatic property Bacillus subtilis
Classification number :
Q936
DOI:
10.3969/j.issn.1000-2006.2014.03.017
Document Code:
A
Abstract:
The objective of this study was to purify β-mannase from Bacillus subtilis WD-23 and examine its enzymology properties. This study used the combining methods of ammonium sulfate, semi-permeable membrane dialysis, polyethylene glycol concentration, DEAE-Sepharose FF ion exchange chromatography, Sephadex G-75 gel filtration and SDS-PAGE gel electrophoresis to purify β-mannase. The result showed that the purified ratio of β-mannase of B. subtilis WD-23 was 14.1 by using the above methods, and the molecular mass was about 40 ku, the optimal pH and the stability range of pH were 5.6 and 5.0-7.0 respectively, and optimal temperature and the stability range of temperature were 55 ℃ and 40-70 ℃ separately, Ca2 + was the most obvious effect on the activation of the enzyme, on the contrary, the inhibitory effect of Li+ was the most obvious.

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Last Update: 2014-05-15