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dc.contributor.authorLiu, Bin
dc.contributor.authorWang, Yiqian
dc.contributor.author王义权
dc.contributor.authorZhang, Xiaobo
dc.date.accessioned2011-09-13T07:10:19Z
dc.date.available2011-09-13T07:10:19Z
dc.date.issued2006
dc.identifier.citationEnzyme and Microbial Technology,Volume 39, Issue 4, 2 August 2006, Pages 805-810zh_CN
dc.identifier.issn0141-0229
dc.identifier.urihttp://dx.doi.org/doi:10.1016/j.enzmictec.2006.01.003
dc.identifier.urihttps://dspace.xmu.edu.cn/handle/2288/10731
dc.description.abstractA maltogenic amylase-producing thermophilic strain WPD616, assigned to Bacillus sp. WPD616 based on 16S rRNA sequence, was isolated from a deep-sea hydrothermal field in west Pacific. Subsequently, a maltogenic amylase gene encoding 588 amino acids from this isolate was cloned and expressed in Escherichia coli as a fusion protein with glutathione S-transferase (GST). The results showed that the recombinant maltogenic amylase had an activity optimum at 50 degrees C and pH at 6.0. It was active up to 70 degrees C at pH 6.0 and stable at pHs ranging from 6.0 to 8.0. The recombinant enzyme was active when Chaps, DTT and Tween 20 (0.1 % or 1%) were used. However, it can be partially inhibited by 1 mM of EDTA, PMSF or SDS, as well as 0.1 % of Triton X-100 or 2-ME, and completely inhibited by 10 mM of PMSF and SDS (10 mM). Its catalytic function was stable in the presence of Li+ and K+ (1 mM or 10 mM), but its activity decreased when Ba2+, Ca2+, Mg2+, Mn2+ (1 mM or 10 mM) and Fe2+ (1 mM) were used. In the presence of Zn2+, Cu-2, Fe3+ (1 mM and 10 mM) and Fe2+ (10 mM), no activity was detected. (c) 2006 Elsevier Inc. All rights reserved.zh_CN
dc.language.isoenzh_CN
dc.publisherELSEVIER SCIENCE INCzh_CN
dc.subjectmaltogenic amylasezh_CN
dc.subjectrecombinant expressionzh_CN
dc.subjectcharacterizationzh_CN
dc.titleCharacterization of a recombinant maltogenic amylase from deep sea thermophilic Bacillus sp WPD616zh_CN
dc.typeArticlezh_CN


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