Cloning, expression and characterization of an acidic endo-polygalacturonase from Bispora sp. MEY-1 and its potential application in juice clarification

文献类型： 外文期刊

第一作者： Yang, Jun

作者： Yang, Jun;Luo, Huiying;Wang, Kun;Cheng, HaiPing;Bai, Yingguo;Yuan, Tiezheng;Yao, Bin;Li, Jiang;Fan, Yunliu

作者机构：

关键词： Acidic endo-polygalacturonase;Bispora sp MEY-1;Pichia pastoris;Apple juice clarification

期刊名称：PROCESS BIOCHEMISTRY （ 影响因子：3.757； 五年影响因子：3.665 ）

ISSN： 1359-5113

年卷期： 2011 年 46 卷 1 期

页码：

收录情况： SCI

摘要： An endo-polygalacturonase gene, pga1, was cloned from the acidophilic fungus Bispora sp. MEY-1 and expressed in Pichia pastoris. The 1455-bp full-length complementary DNA of pga1 encoded a 485-amino acid polypeptide (endo-PGA1) including a putative 21-residue signal peptide and a catalytic domain belonging to glycoside hydrolase family 28. Purified recombinant endo-PGA1 exhibited activity towards polygalacturonic acid and pectin was optimally active at pH 3.5 and 50 degrees C, and showed good stability at pH 2.0-7.0. When tested against pectin, endo-PGA1 exhibited 40% of maximum activity at pH 2.0 and over 50% maximum activity at pH 2.5-4.5. The K-m.app and V-max.app values for polygalacturonic acid were 1.25 mg/ml and 2526 mu mol/min/mg, respectively. When treated apple juice at the concentration of 10 U/ml, endo-PGA1 reduced the intrinsic viscosity (7.7% vs. 8.0%) and increased the light transmittance (84% vs. 86%) almost on the same level as the commercial compound pectinase did. These properties make endo-PGA1 an interesting biocatalyst for acidic industrial processes, especially in the juice clarification. (C) 2010 Elsevier Ltd. All rights reserved.

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