Influence of water-miscible solvents on hydrolytic activity of crude almond β-glucosidase

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DOIResolve DOI: http://doi.org/10.1016/j.molcatb.2004.01.011
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TypeArticle
Journal titleJournal of Molecular Catalysis B: Enzymatic
Volume28
Issue1
Pages1518; # of pages: 4
AbstractThe influence of polar solvents on the hydrolysis of cellobiose (4-O-(β-Image -glucopyranosyl)-β-Image -glucopyranose) and p-NPG (p-nitrophenyl β-Image -glucopyranoside) by crude almond β-glucosidase has been measured. THF and acetonitrile diminish the initial reaction rate by a factor of 2 at a concentration of 10%, while DMF, DMSO and 2-methyl-2-butanol have little effect at this concentration, but induce a decrease at higher concentrations. The specificity constant Vmax/KM of the crude enzyme in aqueous solution was 200-fold higher for p-NPG than for cellobiose, indicating that between the two β-glucosidase activities present in almond, prunasin hydrolase may be more important than amygdalin hydrolase. However, the specificity constant for p-NPG was more affected by the presence of DMF, since it dropped six-fold for a 20% concentration of solvent while in the case of cellobiose, the drop was only 1.6-fold for the same solvent concentration.
Publication date
AffiliationNational Research Council Canada; NRC Biotechnology Research Institute
Peer reviewedNo
NPARC number12339312
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Record identifier49e0b0a7-9c58-4c49-ab74-d8347b011a5e
Record created2009-09-11
Record modified2016-05-09
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