PMID: 69Nov 20, 1975

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

Biochimica Et Biophysica Acta
Y Tominaga, Y Tsujisaka

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.

Citations

Oct 20, 2005·Journal of Bioscience and Bioengineering·K AkiyamaR Takata
Apr 23, 2011·Bioscience, Biotechnology, and Biochemistry·Tohru KobayashiKoki Horikoshi
Sep 29, 2011·Journal of Basic Microbiology·Naosekpam Ajit Singh, Veerubommu Shanmugam
Jul 3, 2002·Bioscience, Biotechnology, and Biochemistry·Ho-Geun YoonHong-Yon Cho
Dec 18, 2013·Journal of Bioscience and Bioengineering·Bon Geun Goo, Jae Kweon Park

Related Concepts

Cations, Divalent
Cell Wall
Citrates
Drug Stability
Edetic Acid, Calcium, Sodium Salt
Exoglycosidases
Hydrogen-Ion Concentration
Polysaccharides
Rhizopus
Sulfhydryl Reagents

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