The activity of different lipase (from Pseudomonas cepacia) forms, such as crude powder (crude PC), purified and lyophilized with PEG (PEG + PC), covalently linked to PEG (PEG-PC), cross-linked enzyme crystals (CLEC-PC), and immobilized in Sol-Gel-AK (Sol-Gel-AK-PC) was determined, at various water
Factors Governing the Activity of Lyophilised and Immobilised Lipase Preparations in Organic Solvents
β Scribed by Mattias Persson; Ernst Wehtje; Patrick Adlercreutz
- Publisher
- John Wiley and Sons
- Year
- 2002
- Tongue
- English
- Weight
- 101 KB
- Volume
- 3
- Category
- Article
- ISSN
- 1439-4227
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π SIMILAR VOLUMES
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
Surfactant-coated lipase (SCL) was prepared by coating the surface of Candida cylindracea lipase with the non-ionic surfactant, Span 85. SCL catalyzed the esteriΓΌcation of geraniol and acetic acid. The ester product, geranyl acetate, is an important component of Γ½avor and fragrance compounds. The SC
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