Abstract
The influence of the chemical modification of the functional groups of the β-1,3-glucanase L IV on its capacity for performing hydrolysis and transglycosylation reactions has been investigated. On the modification of the lysine, tryptophan, histidine, and dicarboxylic acid residues and on the oxidation of the carbohydrate component in the L IV molecule the ratio of the hydrolase and transglycosylating activities does not change. It is likely that the hydrolysis and transglycosylation reactions take place at the same active site with the participation of the same catalytic groups.
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