Two acidic, thermophilic GH28 polygalacturonases from Talaromyces leycettanus JCM 12802 with application potentials for grape juice clarification

文献类型: 外文期刊

第一作者: Li, Yeqing

作者: Li, Yeqing;Xu, Bo;Li, Yeqing;Wang, Yuan;Tu, Tao;Zhang, Duoduo;Ma, Rui;You, Shuai;Wang, Xiaoyu;Yao, Bin;Luo, Huiying

作者机构:

关键词: Talaromyces leycettanus JCM12802;Polygalacturonase;Heterologous expression;Grape juice clarification

期刊名称:FOOD CHEMISTRY ( 影响因子:7.514; 五年影响因子:7.516 )

ISSN: 0308-8146

年卷期: 2017 年 237 卷

页码:

收录情况: SCI

摘要: Efficient hydrolysis of pectic materials to sugars requires the synergistic action of endo- and exo-polygalacturonases. Two novel polygalacturonases (exo-TePG28a and endo-TePG28b) were identified in Talaromyces leycettanus JCM12802, overexpressed in Pichia pastoris, and characterized in this report. The specific activities of TePG28a and TePG28b towards polygalacturonic acid were 280 +/- 9 and 25,900 +/- 502 U/mg, respectively. Both enzymes exhibited optimal activities at pH 3.5 and retained highly stable over a broad pH range of 2.0-7.0. Distinct from most fungal polygalacturonases that have low temperature optima, TePG28a and TePG28b were optimally active at 70 degrees C. When treated the grape juice with the enzyme combination (the unit ratio of TePG28a:TePG28b was 1:4), higher pectin-degrading efficiency (up to 140%) was achieved, and light transmittance was improved from 14% to 82%. These favorable enzymatic properties make TePG28a and TePG28b attractive for the applications in the juice industry. (C) 2017 Published by Elsevier Ltd.

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