A beta-mannanase from Bacillus subtilis B36: Purification, properties, sequencing, gene cloning and expression in Escherichia coli

文献类型： 外文期刊

第一作者： Li, Ya Nan

作者： Li, Ya Nan;Meng, Kun;Wang, Ya Ru;Yao, Bin

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关键词： beta-mannanase;Bacillus subtilis;GLYCOSYL HYDROLASES;HYDROLYSIS

期刊名称：ZEITSCHRIFT FUR NATURFORSCHUNG SECTION C-A JOURNAL OF BIOSCIENCES （ 影响因子：1.649； 五年影响因子：1.66 ）

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收录情况： SCI

摘要： MANB36, a secrete endo-beta-1,4-D-mannanase produced by Bacillus subtilis B36, was purified to homogeneity from a culture supernatant and characterized. The optimum pH value for the mannanase activity of MANB36 is 6.4 and the optimum temperature is 50 degrees C. The enzyme activity of MANB36 is remarkably thermostable at 60 degrees C and the specific activity of MANB36 is 927.84 U/mg. Metal cations (except Hg2+ and Ag+), EDTA and 2-mercaptoethanol (2-ME) have no effects on enzyme activity. This enzyme exhibits high specificity with the substituted galactomannan locust bean gum (LBG). The gene encoding for MANB36, manB36, was cloned by PCR and sequenced. manB36 contains a single open reading frame (ORF) consisting of 1104 bp that encodes a protein of 367 amino acids. The predicted molecular weight of 38.13 kDa, calculated by the deduced protein of the gene manB36 without signal peptide, coincides with the apparent molecular weight of 38.0 kDa of the purified MANB36 estimated by SDS-PAGE. The mature protein of MANB36 has been expressed in Escherichia coli BL21 and the expressed mannanase has normal bioactivity.

分类号： Q

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