𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Water activity does not influence the enantioselectivity of Lipase PS and lipoprotein lipase in organic solvents

✍ Scribed by Roberto Bovara; Giacomo Carrea; Gianluca Ottolina; Sergio Riva

Book ID
104634829
Publisher
Springer Netherlands
Year
1993
Tongue
English
Weight
306 KB
Volume
15
Category
Article
ISSN
0141-5492

No coin nor oath required. For personal study only.

✦ Synopsis

The activity and enantioselectivity of Lipase PS from Pseudomonas cepacia and lipoprotein lipase from Pseudomonas sp. were investigated in organic solvents preequilibrated to water activities ranging from 4.1 to 0.53, using as a model reaction the transesterification between (f)-sulcatol and vinyl acetate. Variations of water activity markedly influenced the transesterification rate but did not modify the enantioselectivity of the two enzymes.

πŸ“œ SIMILAR VOLUMES

Modern Biocatalysis || Importance of Enz
Modern Biocatalysis || Importance of Enzyme Formulation for the Activity and Enantioselectivity of Lipases in Organic Solvents
✍ Fessner, Wolf-Dieter; Anthonsen, Thorleif πŸ“‚ Article πŸ“… 2008 πŸ› Wiley-VCH Verlag GmbH & Co. KGaA 🌐 German βš– 156 KB πŸ‘ 2 views

5 5.1 a Relative to crude lipase BC taken as 1. b The transesterifi cation between 1 -octanol (0.19 M) and vinyl butyrate (0.79 M) to give 1 -octyl butyrate and acetaldehyde was used as a model reaction. An amount of enzyme form containing 10 Β΅ g of protein was used in a reaction volume of 1 ml. Th