Chemoselectivity and enhanced activity of poly(ethylene glycol)-modified lipases acylating hydrophilic aminoacid derivatives in organic solvents
✍ Scribed by Cynthia Ebert; Lucia Gardossi; Paolo Linda; K'A. -M. Tambwe
- Publisher
- Springer-Verlag
- Year
- 1994
- Tongue
- English
- Weight
- 368 KB
- Volume
- 8
- Category
- Article
- ISSN
- 0951-208X
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✦ Synopsis
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 group in serine-I~-naphthylamide.
Lipases, when suspended in dry organic solvents, can catalyse the selective acylation of serine and lysine side-chains in different dipeptides (Klibanov and Gardossi, 1991). This has been explained by the steric requirements of lipases, which are sensitive to the presence of bulky groups on the rigid backbone of the peptides. This approach of selective acylation of