β-Galactosidase transferase activity in ice and use of vinyl-β-d-galactoside as donor
摘要:
The ability of vinyl-beta-D-galactoside as a donor in transglycosylation reactions catalysed by the beta-glycosidase from Aspergillus oryzae using allylic alcohol and methyl-alpha-galactoside as accepters is tested. A kinetic study made in comparison with another donor, the 2-nitrophenyl-beta-D-galactoside, shows that the use of the latter leads at room temperature to better yields than those obtained from the former. A reverse situation is observed in ice at -7 degrees C, conditions in which the yield for transglycosylation can be enhanced from 59% to 82% with methyl-alpha-galactoside as an acceptor. (C) 1997 Elsevier Science Ltd.
beta-D-Galactosidase, isolated from cloned E. coli, was immobilised on cellulose beads via oxidation with sodium periodate, activation by cyanuric chloride, or diazotisation. beta-D-Galactosidase immobilised via azo bonds showed the highest relative activity and thermostability, and was used for synthesis of disaccharide methyl glycosides.
The ability of vinyl-beta-D-galactoside as a donor in transglycosylation reactions catalysed by the beta-glycosidase from Aspergillus oryzae using allylic alcohol and methyl-alpha-galactoside as accepters is tested. A kinetic study made in comparison with another donor, the 2-nitrophenyl-beta-D-galactoside, shows that the use of the latter leads at room temperature to better yields than those obtained from the former. A reverse situation is observed in ice at -7 degrees C, conditions in which the yield for transglycosylation can be enhanced from 59% to 82% with methyl-alpha-galactoside as an acceptor. (C) 1997 Elsevier Science Ltd.