| Autor: |
Madry, Norbert, Zocher, Rainer, Grodzki, Karola, Kleinkauf, Horst |
| Zdroj: |
Applied Microbiology & Biotechnology; 1984, Vol. 20 Issue 2, p83-86, 4p |
| Abstrakt: |
The multifunctional enzyme enniatin synthetase was immobilized by adsorption to propyl agarose. The immobilized multienzyme retained 45% of the activity of the free enzyme; an operational half-life of about 15 h was estimated. Selective synthesis of several different enniatin homologues was achieved with propyl agarose-bound enniatin synthetase. In addition to enniatin A, B, and C formation, a selective synthesis of non-naturally occurring depsipeptides, containing norvaline, norleucine, or α-aminobutyric acid as sole amino acid moieties, was observed. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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