An Acidophilic and Acid-Stable beta-Mannanase from Phialophora sp P13 with High Mannan Hydrolysis Activity under Simulated Gastric Conditions

文献类型： 外文期刊

第一作者： Zhao, Junqi

作者： Zhao, Junqi;Shi, Pengjun;Luo, Huiying;Yang, Peilong;Zhao, Heng;Bai, Yingguo;Huang, Huoqing;Wang, Hui;Yao, Bin

作者机构：

关键词： Phialophora sp.;acidophilic and acid-stable enzyme;beta-mannanase;Pichia pastoris

期刊名称：JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY （ 影响因子：5.279； 五年影响因子：5.269 ）

ISSN： 0021-8561

年卷期： 2010 年 58 卷 5 期

页码：

收录情况： SCI

摘要： A beta-mannanase gene, man5AP13, was cloned from Phialophora sp. P13 and expressed in Pichia pastoris. The deduced amino acid sequence of the mature enzyme, MAN5AP13, had highest identity (53%) with the glycoside hydrolase family 5 beta-mannanase from Bispora sp. MEY-1. The purified recombinant beta-mannanase was acidophilic and acid stable, exhibiting maximal activity at pH 1.5 and retaining >60% of the initial activity over the pH range 1.5-7.0. The optimum temperature was 60 degrees C. The specific activity, K-m and V-max for locust bean gum substrate were 851 U/mg, 2.5 mg/mL, and 1667.7 U/min.mg, respectively. The enzyme had excellent activity and stability under simulated gastric conditions, and the released reducing sugar of locust bean gum was significantly enhanced by one-fold in simulated gastric fluid containing pepsin in contrast to that without pepsin. All these properties make MAN5AP13 a potential additive for use in the food and feed industries.

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