Transglycosylation catalyzed by almond β-glucosidase and cloned Pichia etchellsii β-glucosidase II using glycosylasparagine mimetics as novel acceptors

被引:115
作者
Kannan, T
Loganathan, D [1 ]
Bhatia, Y
Mishra, S
Bisaria, VS
机构
[1] Indian Inst Technol, Dept Chem, Madras 600036, Tamil Nadu, India
[2] Indian Inst Technol, Dept Biochem Engn & Biotechnol, New Delhi 110016, India
关键词
beta-glucosidase; almond; Pichia etchellsii; transglycosylation; glycosylasparagine mimics; disaccharide synthesis;
D O I
10.1080/1024242032000156594
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The stability of almond beta-glucosidase in five different organic media was evaluated. After 1 hour of incubation at 30degreesC, the enzyme retained 95, 91, 81, 74 and 56% relative activity in aqueous solutions [30% (v/v)] of dioxane, DMSO, DMF, acetone and acetonitrile, respectively. Transglucosylation involving p -nitrophenyl beta-D-glucopyranoside as donor and beta-1- N -acetamido-D-glucopyranose, which is a glycosylasparagine mimic, as acceptor was explored under different reaction conditions using almond betaglucosidase and cloned Pichia etchellsii beta-glucosidase II. The yield of disaccharides obtained in both reactions turned out to be 3%. Both enzymes catalyzed the formation of (1-->3)- as well as (1-->6)- regioisomeric disaccharides, the former being the major product in cloned beta-glucosidase II reaction while the latter predominated in the almond enzyme catalyzed reaction. Use of beta-1- N -acetamido-D-mannopyranose and beta-1- N -acetamido-2-acetamido-2-deoxy-D-glucopyranose as acceptors in almond beta-glucosidase catalyzed reactions, however, did not afford any disaccharide products revealing the high acceptor specificity of this enzyme.
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页码:1 / 7
页数:7
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