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  • Title: An acidophilic and acid-stable beta-mannanase from phialophora sp. p13 with high mannan hydrolysis activity under simulated gastric conditions.
    Author: Zhao J, Shi P, Luo H, Yang P, Zhao H, Bai Y, Huang H, Wang H, Yao B.
    Journal: J Agric Food Chem; 2010 Mar 10; 58(5):3184-90. PubMed ID: 20143777.
    Abstract:
    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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