Effect of Drying Methods on Quality of Leaf Protein Concentrate |
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Authors: | Takao Mori Toshifumi Tsuji Motohiko Sugiura Masayuki Taniguchi Takeshi Kobayashi |
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Institution: | Department of Chemical Engineering,Faculty of Engineering, Nagoya University,Chikusa-ku, Nagoya 464, Japan |
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Abstract: | Glutathione thiol esterase activity in cell extracts of a yeast: Saccharomyces cerevisiae was separated into three peaks when filtered on a Sephadex G-150 gel column. One of the enzymes in these peaks was purified. The enzyme was a single polypeptide chain with a molecular weight of 28,000 and catalyzed the complete hydrolysis of S-acetylglutathione and S-lactoylglutathione. S- Methyl-, S-hexyl-, S-glyceryl-, S-succinylglutathiones, and acetyl CoA were not hydrolyzed. In addition to the hydrolytic activity, the purified enzyme showed a group transfer activity and catalyzed the formation of acetyl CoA from S-acetylglutathione and CoA. The purified enzyme was not identical with glyoxalase II in molecular weight, substrate specificity, or behaviors toward inhibitors. |
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Keywords: | α-linked galacto-oligosaccharide allergic peritonitis ovalbumin mice |
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