Hydrolysis of soybean isoflavone glycosides by a thermostable β-glucosidase from Paecilomyces thermophila

被引:94
作者
Yang, Shaoqing [1 ]
Wang, Lijun [1 ]
Yan, Qiaojuan [2 ]
Jiang, Zhengqiang [1 ]
Li, Lite [1 ]
机构
[1] China Agr Univ, Coll Food Sci & Nutr Engn, Dept Biotechnol, Beijing 100083, Peoples R China
[2] China Agr Univ, Coll Engn, Bioresource Utilizat Lab, Beijing 100083, Peoples R China
基金
中国国家自然科学基金;
关键词
Deglycosylation; beta-Glucosidase; Hydrolysis; Paecilomyces thermophila; Soybean isoflavone glycosides; Thermostable; BACILLUS-SUBTILIS NATTO; SOY ISOFLAVONES; PURIFICATION; AGLYCONES; CLONING; HUMANS; BIOAVAILABILITY; METABOLISM; ENRICHMENT; BACTERIUM;
D O I
10.1016/j.foodchem.2009.01.038
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
The beta-glucosidase from Paecilomyces thermophila J18 was found to be capable of hydrolysing daidzin and genistin in a previous study. This report further evaluated the thermostability and hydrolysis of soybean isoflavone glycosides. The enzyme was found to be very stable at 50 degrees C, and retained more than 95% of its initial activity after 8 h at 50 degrees C. It converted isoflavone glycosides, in soybean flour extract and soybean embryo extract, to their aglycones, resulting in more than 93% of hydrolysis of three isoflavone glycosides (namely, daidzin, genistin and glycitin) after 4 h of incubation. Also, addition of the beta-glucosidase greatly increased the contents of isoflavone aglycones in the suspended soybean flour and soymilk. The results indicate that the thermostable beta-glucosidase may be used to increase the isoflavone aglycones in soy products. This is the first report on the potential application of fungal beta-glucosidases for converting isoflavone glycosides to their aglycones in soy products. (C) 2009 Elsevier Ltd. All rights reserved.
引用
收藏
页码:1247 / 1252
页数:6
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