Any suggestions?
In the literature there is a knowledge as ‘‘β-Glucosidases (EC 3.2.1.21; β-D-glucoside glucohydrolase) hydrolyze terminal, nonreducing 1,4-linked-β-glucose residues by releasing β-D-glucose from oligo- or polysaccharides (Webb, E.C. 1992)’’. Could it be explained as a reason for the enzyme not have an effect on sucrose by this information? Can you refer any journal or reference in this regards?
In sucrose, both hexoses are liked by their reducing carbon (C1 for glucose, and C2 for fructose). The glucosyl residue is alpha, not beta, hence beta-glucosidases won't work. The fructosyl moiety is beta, but that's irrelevant.
because sucrose is a disaccharide of glucose and fructose with a beta-1,2 linkage
this enzyme would better work on a beta 1,4 Glc-Glc
In sucrose, both hexoses are liked by their reducing carbon (C1 for glucose, and C2 for fructose). The glucosyl residue is alpha, not beta, hence beta-glucosidases won't work. The fructosyl moiety is beta, but that's irrelevant.
Enzymes are supposed to act under specific conditions in a specific substrate or in a group of similar molecules. It is guided by productive interactions between aa residues in catalytic cleft and the substrate molecule. Based on that statement it is quite impossible to an enzyme that acts on cellobiose (beta-1,4-linkage) to act in sucrose (beta-1,2-linkage) as well. Please check stereochemistry of both substrates (attached). In brief, sucrose structure dos not fit b-glucosidases catalytic cleft.
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