Purification and some enzymatic properties of the chitosanase from Bacillus R-4 which lyses Rhizopus cell walls.

TitlePurification and some enzymatic properties of the chitosanase from Bacillus R-4 which lyses Rhizopus cell walls.
Publication TypeJournal Article
Year of Publication1975
AuthorsTominaga, Y, Tsujisaka, Y
JournalBiochim Biophys Acta
Volume410
Issue1
Pagination145-55
Date Published1975 Nov 20
ISSN0006-3002
KeywordsBacillus, Cations, Divalent, Cell Wall, Citrates, Drug Stability, Edetic Acid, Glycoside Hydrolases, Hydrogen-Ion Concentration, Kinetics, Molecular Weight, Polysaccharides, Rhizopus, Sulfhydryl Reagents, Temperature
Abstract

A strain of Bacillus sp (Bacillus R-4) produces a protease and a carbohydrolase both of which have the ability to lyse Rhizopus cell walls. Of the enzymes, the carbohydrolase has been purified to an ultracentrifugally and electrophoretically homogeneous state, and identified as a chitosanase. The enzyme was active on glycol chitosan as well as chitosan. Molecular weight of the purified enzyme was estimated as 31 000 and isoelectric point as pH 8.30. The enzyme was most active at pH 5.6 and at 40 degrees C with either Rhizopus cell wall or glycol chitosan as substrate, and was stable over a range of pH 4.5 to 7.5 at 40 degrees C for 3 h. The activity was lost by sulfhydryl reagents and restored by either reduced glutathione of L-cysteine. An abrupt decrease in viscosity of the reaction mixture suggested an endowise cleavage of chitosan by this enzyme.

DOI10.1016/0005-2744(75)90215-6
Alternate JournalBiochim Biophys Acta
PubMed ID69