Re-examination of Zymolyase Purification
- 1 April 1982
- journal article
- research article
- Published by Oxford University Press (OUP) in Agricultural and Biological Chemistry
- Vol. 46 (4) , 963-969
- https://doi.org/10.1080/00021369.1982.10865178
Abstract
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%.This publication has 7 references indexed in Scilit:
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