Nov 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.

  • References1
  • Citations9

Mentioned in this Paper

Cations, Divalent
Enzymes, antithrombotic
Cytokinesis of the Fertilized Ovum
Bacillus species
Endopeptidases
Proteolytic Enzyme
Rhizopus
Cell Wall
Sulfhydryl Reagents
Enzymes for Treatment of Wounds and Ulcers

About this Paper

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