Enhancement of protease activity in transesterification of glycidol with vinyl n-butyrate by entrapment into alkyl-substituted silicates and pretreatment with a substrate

Koei Kawakami, Yoshiaki Matsui, Tsutomu Ono, Hiroyuki Ijima

研究成果: ジャーナルへの寄稿学術誌査読

7 被引用数 (Scopus)

抄録

Proteases originating from Aspergillus melleus (Protease P) and Bacillus subtillis (Prolether FG-F) were entrapped into organic-inorganic hybrid silicates on Celite 545 by the sol-gel method, and their activities measured at 35° C for transesterification of chiral glycidol with vinyl n-butyrate in isooctane. n-Butyl- and dimethyl-substituted silicates provided 12.6 times higher activities with Protease P and 5.5 times with Prolether FG-F, respectively, than those deposited on Celite 545. Although pretreatment of those immobilized proteases with the chiral glycidol affected transesterification activities of both enantiomers, the ratio of the initial transesterification rate of (S)-(-)-glycidol to that of (R)-(+)-glycidol, remained unchanged.

本文言語英語
ページ(範囲)49-52
ページ数4
ジャーナルBiocatalysis and Biotransformation
21
1
DOI
出版ステータス出版済み - 2月 2003

!!!All Science Journal Classification (ASJC) codes

  • バイオテクノロジー
  • 触媒
  • 生化学

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