Abstract：
:The α-galactosidase gene, RmGal36, from Rhizomucor miehei was cloned and expressed in Escherichia coli. The gene has an open reading frame of 2256bp encoding 751 amino acid residues. RmGal36 was optimally active at pH 4.5 and 60°C, but is stable between pH 4.5 and 10.0 and at a temperature of up to 55°C for 30min retaining more than 80% of its relative activity. It displayed remarkable resistance to proteases and its activity was not inhibited by galactose concentrations of 100mM. The relative specificity of RmGal36 towards various substrates is in the order of p-nitrophenyl α-galactopyranoside>melibiose>stachyose>raffinose, with a K(m) of 0.36, 16.9, 27.6, and 47.9mM, respectively. The enzyme completely hydrolyzed raffinose and stachyose present in soybeans and kidney beans at 50°C within 60min. These features make RmGal36 useful in the food and feed industries and in processing of beet-sugar.
journal_name
Bioresour Technoljournal_title
Bioresource technologyauthors
Katrolia P,Jia H,Yan Q,Song S,Jiang Z,Xu Hdoi
10.1016/j.biortech.2012.01.144subject
Has Abstractpub_date
2012-04-01 00:00:00pages
578-86eissn
0960-8524issn
1873-2976pii
S0960-8524(12)00187-3journal_volume
110pub_type
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