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Purification and some enzymatic properties of the chitosanase from Bacillus R-4 which lyses Rhizopus cell walls.
Metadata
JournalBiochim. Biophys. ActaNot FoundDate
1975-Nov-20
Publication Type
Journal Article
Volume
1975-Nov-20 / 410 : 145-55
Author
Tominaga Y , Tsujisaka Y
DoiPMIDMESH
Bacillus
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.
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