Enhanced activities of lipase pretreated with organic solvents
β Scribed by Michiaki Matsumoto; Koji Kida; Kazuo Kondo
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 2001
- Tongue
- English
- Weight
- 89 KB
- Volume
- 76
- Category
- Article
- ISSN
- 0268-2575
- DOI
- 10.1002/jctb.491
No coin nor oath required. For personal study only.
β¦ Synopsis
Abstract
The catalytic activities of lipases derived from Pseudomonas sp and pretreated with various organic solvents were investigated. The activity of the solventβpretreated lipase was greater than that of native lipase in both the esterification reaction in an organic medium and the hydrolysis reaction in an aqueous medium. With esterification calalysed by pretreated lipase, the product, benzyl octanoate, was detected without timeβlag. Conversions at equilibrium state were correlated with the hydrophobicities of the solvents used. In the hydrolysis reaction, most pretreated lipases yielded increased acid production compared with native lipase. A linear correlation was observed between the solvent hydrophobicity and the relative initial reaction rate of the hydrolysis reaction when using pretreated lipases.
Β© 2001 Society of Chemical Industry
π SIMILAR VOLUMES
The activity of different formulations of Candida antarctica lipase B (CALB), such as crude CALB, purified CALB, purified CALB lyophilized with PEG (CALB + PEG) or oleic acid (CALB + OA), and the commercial formulation Novozym 435, was determined in toluene, carbon tetrachloride, and 1,4-dioxane at