Lipase catalyzed esterification in AOT reverse micelles: A structural study
β Scribed by V. Papadimitriou; C. Petit; G. Cassin; A. Xenakis; M.P. Pileni
- Publisher
- Elsevier Science
- Year
- 1995
- Tongue
- English
- Weight
- 686 KB
- Volume
- 54
- Category
- Article
- ISSN
- 0001-8686
No coin nor oath required. For personal study only.
β¦ Synopsis
AOT reverse micelles are used to cosolubilize hydrophilic and hydrophobic reactants of lipase catalysed esterification. Depending on the nature of the alcohol, a drastic change of the initial rate of the esterification is observed. A structural study of the micellar system with and without reactant is undertaken to explain the change in the activity with the various alcohols.
π SIMILAR VOLUMES
Polyphenol oxidase catalysing the oxidation of 4-methylcatechol in reverse micelles of AOT/cyclohexane had an optimum temperature 15 Β°C higher than in aqueous medium. However, the enzyme lost stability when it was preincubated in reverse micelles in the absence of substrate regardless of the tempera
## Abstract The addition of short chain polyethylene glycols (PEGs) activated __Chromobacterium viscosum__ lipase in AOT reverse micelles. In this study, it was assumed that when AOT reverse micelles contained PEG molecules, native and activated lipases contributed to the reaction according to thei
## Abstract Candida rugosa lipase has been used to investigate the hydrolysis of high concentration olive oil in the AOTβisooctane reversed micellar system at __W__~__o__~ = 10, pH 7.1, and 37Β°C. Results from this work show the hydrolytic reaction obeys MichaelisβMenten kinetics up to the initial s