A novel acidic and low-temperature-active endo-polygalacturonase from Penicillium sp CGMCC 1669 with potential for application in apple juice clarification

文献类型： 外文期刊

第一作者： Yuan, Peng

作者： Yuan, Peng;Meng, Kun;Huang, Huoqing;Shi, Pengjun;Luo, Huiying;Yang, Peilong;Yao, Bin

作者机构：

关键词： Penicillium sp CGMCC 1669;Acidic endo-polygalacturonase;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： 2011 年 129 卷 4 期

页码：

收录情况： SCI

摘要： An endo-polygalacturonase gene (pg I) was cloned from Penicillium sp. CGMCC 1669 and expressed in Pichia pastoris. The full-length cDNA consists of 1140 bp and encodes a glycoside hydrolase family 28 protein with a calculated molecular mass of 37.5 kDa. The optimal pH and temperature of purified recombinant endo-PG I were 3.5 and 40 degrees C, respectively. At 0 degrees C, endo-PG I still retained 7.3% of the maximal activity. The enzyme had a high affinity and specificity towards polygalacturonic acid. The Km(app) and Vmax(app) values were 19.5 mg/ml and 909.1 U/min/mg, respectively. Addition of endo-PG 1(3.4 U/ml) reduced the intrinsic viscosity of apple juice by 4.5%, and increased the light transmittance by 71.8%. Combination of a commercial pectin lyase and endo-PG I showed higher efficiency in juice clarification than the pectin lyase alone or the commercial pectinase widely used. These properties make endo-PG I an interesting biocatalyst for juice clarification. (C) 2011 Elsevier Ltd. All rights reserved.

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