Re-examination of Zymolyase Purification

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概要

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• Zymolyase was purified from Zymolyase-60, 000 by ion-exchange chromatography with sugar and gel filtration. Zymolyase was separated into the two protein fractions A and B. Neither alone could lyse yeast cells, but together showed high lytic activity. Zymolyase A and B were β-1, 3-glucanase and alkaline protease, respectively. On stepwise treatment of yeast cells with the enzymes, yeast cells were lysed only by treatment with Zymolyase A after pretreatment with Zymolyase B. Zymolyase A lysed yeast cells in the presence of 2-mercaptoethanol, but B could not even at high concentration. Zymolyase B decreased the turbidity of a yeast cell suspension by about 13%.

• 社団法人 日本農芸化学会の論文

著者

• KITAMURA Kumpei

  The Research Laboratories of Kirin Brewery Co.

関連論文

• Lysis of Yeast Cells Showing Low Susceptibility to Zymolyase
• Isolation and identification of Crystalline Cellulose Hydrolyzing Bacterium and its Enzymatic Properties
• A High Yeast Cell Wall Lytic Enzyme-Producing Mutant of Arthrobacter luteus
• Effect of Culture Medium on Susceptibility of Yeast Cells to Zymolyase
• Re-examination of Zymolyase Purification
• A protease that participates in yeast cell wall lysis during zymolyase digestion.

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