Studies on N-Acetyl-β-D-glucosaminidase of Aspergillus oryzae

Publisher Website
Google Scholar
Abstract
N-Acetyl-β-D-glucosaminidase [EC 3.2.1.30] isolated from Takadiastase (Sankyo) hydrolyzed partially O-methylated N-acetyl-chitooligosaccharides to produce N-acetyl glucosamine, 3-O-methyl-, 6-O-methyl- and 3, 6-di-O-methyl-N-acetylglucosamines. Phenyl 3-O-methyl- and 6-O-methyl-N-acetyl-β-D-glucosaminides were also hydrolyzed by the enzyme, whereas phenyl 3, 4-di-O-methyl-N-acetyl-β-D-glucosaminide was not hydrolyzed. N-Acetyl-β-D-glucosaminidase activity was inhibited by acetamido-compounds such as acetamide, acetanilide, and N-acetylglucosamine. N-Propionylglucosamine and N-formylglucosamine showed inhibitory action weaker than N-acetylglucosamine. These results indicated that the hydroxyl at carbon 4 and acetamido at carbon 2 of the substrate were significant in the formation of ES-complex. Fairly high specificity for the aglycon part of the substrates was recognized in a study of the hydrolysis rates of 1-L-β-aspartamido-2-acetamido-1, 2-dideoxy-β-D-glucose, N-acetylglucosaminyl-β(1–4)-N-acetylglucosaminyl-β(1–4)-N-acetylglucosaminitol and di-N-acetylchitobiose.

This publication has 0 references indexed in Scilit: