Abstract
The mode of degradation of glycol chitin by the liquefying chitinase of Aspergillus niger was invetsigated. Glycol chitin was rapidly cleaved to glycol chitodextrin and oligosaccharides, without formation of detectable amounts of monosaccharide. The enzyme attacked glycol chitodextrin as well as glycol chitin, but the rate of degradation was slower in the former than in the latter. Glycol chitosan, deacetylated compound, was not splitted. Activity of this enzyme preparation on N, N’-diacetylchitobiose and β-methyl-N -acetylglucosaminide was weak. Therefore, it is presumed that the liquefying chitinase degrade the glucosaminidic bonds at random in the interior of the polysaccharide chain.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
