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
Modern Biocatalysis || Activity and Stability of Proteases in Hydrophilic Solvents
β Scribed by Fessner, Wolf-Dieter; Anthonsen, Thorleif
- Publisher
- Wiley-VCH Verlag GmbH & Co. KGaA
- Year
- 2008
- Tongue
- German
- Weight
- 225 KB
- Edition
- 1
- Category
- Article
- ISBN
- 3527320717
No coin nor oath required. For personal study only.
β¦ Synopsis
This reference covers the wide and rapidly growing field of biocatalysis. It combines complementary expertise from such areas as microbiology, enzymology, molecular biology, structural biology and organic chemistry, this highlighting the interdisciplinary nature of the subject. With its special focus on progress and new developments towards environmentally beneficial reactions with high levels of selectivity for the production of key compound classes, this book will enlighten both chemists and biologists as to the advances and opportunities existing in enzyme catalysis.
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## Abstract Engineered extremely thermostable variants of the thermolysinβlike protease from __Bacillus stearothermophilus__ possessing an introduced disulfide bond G8C/N60C (double mutant, DM) and six additional amino acid substitutions in the exposed loop region 56β69 (Boilysin, BLN) have been pr
Lipases, when covalently modified with poly(ethylene glycol), catalyse the acylation of hydrophilic substrates in organic solvents with increase in the reaction rate even in the presence of 4% water. As a further result the modified Lipoprotein lipase from Pseudomonas species acylates only amino gro