High-yield production of a low-temperature-active polygalacturonase for papaya juice clarification

被引:75
作者
Tu, Tao [1 ]
Meng, Kun [1 ]
Bai, Yingguo [1 ]
Shi, Pengjun [1 ]
Luo, Huiying [1 ]
Wang, Yaru [1 ]
Yang, Peilong [1 ]
Zhang, Yuhong [2 ]
Zhang, Wei [2 ]
Yao, Bin [1 ]
机构
[1] Chinese Acad Agr Sci, Feed Res Inst, Key Lab Feed Biotechnol, Minist Agr, Beijing 100081, Peoples R China
[2] Chinese Acad Agr Sci, Biotechnol Res Inst, Beijing 100081, Peoples R China
基金
中国国家自然科学基金; 国家高技术研究发展计划(863计划);
关键词
Achaetomium sp Xz8; Endo-polygalacturonase; Low-temperature-active; High specific activity; Juice clarification; THERMOSTABLE POLYGALACTURONASE; ENDO-POLYGALACTURONASE; PURIFICATION; EXPRESSION; ENDOPOLYGALACTURONASE; OPTIMIZATION; PROTEINS; ENZYMES; PECTIN; TIME;
D O I
10.1016/j.foodchem.2013.05.132
中图分类号
O69 [应用化学];
学科分类号
070301 [无机化学];
摘要
A novel endo-polygalacturonase (endo-PG I) from Achaetomium sp. Xz8 was identified, overexpressed in Pichia pastoris, and characterized in this report. Recombinant endo-PG I is distinguished from other enzyme counterparts by its high activity towards polygalacturonic acid (49,934 U/ml) and high yield in the 15-1 fermentor (2.13 g/l). It exhibits optimal activity at 45 C and remained active over a broad temperature range of 0-80 degrees C. Distinct from most fungal polygalacturonases that have acidic pH optima, endo-PG I is optimally active at pH 6, similar to the pH of fresh papaya juice (5.7). Endo-PG I alone reduced the viscosity of papaya juice by 17.6%, and increased its transmittance by 59.1%. When combined with a commercial pectin methylesterase, it showed much higher efficiency with a synergy degree of more than 1.25. All these favourable enzymatic properties make endo-PG I attractive for potential applications in the juice industry. (C) 2013 Elsevier Ltd. All rights reserved.
引用
收藏
页码:2974 / 2981
页数:8
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