Modern Biocatalysis || Importance of Enzyme Formulation for the Activity and Enantioselectivity of Lipases in Organic Solvents
โ Scribed by Fessner, Wolf-Dieter; Anthonsen, Thorleif
- Publisher
- Wiley-VCH Verlag GmbH & Co. KGaA
- Year
- 2008
- Tongue
- German
- Weight
- 156 KB
- Edition
- 1
- Category
- Article
- ISBN
- 3527320717
No coin nor oath required. For personal study only.
โฆ Synopsis
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 ยต g of protein was used in a reaction volume of 1 ml. The activity of crude lipase BC was 0.5 ยต mol/min ร 10 ยต g of protein. c PEG, methoxy poly(ethylene glycol) (molecular mass 5000 Da). d Lipase BC as commercialized by AMANO company (commercial name lipase PS). e CLEC, cross -linked enzyme crystals. Sample obtained as a kind gift of Altus. f Lipase BC entrapped in sol gel -AK. Sample purchased from Fluka.
๐ SIMILAR VOLUMES
The addition of simple inorganic salts to aqueous enzyme solutions prior to lyophilization results in a dramatic activation of the dried powder in organic media relative to enzyme with no added salt. Activation of both the serine protease subtilisin Carlsberg and lipase from Mucor javanicus resultin