Covalent immobilization of the multienzyme enniatin synthetase

Autor:	Rainer Zocher, Karola Grodzki, Horst Kleinkauf, Klaus Mosbach, Nils Siegbahn, Norbert Madry
Rok vydání:	1985
Předmět:	chemistry.chemical_classification Depsipeptide Immobilized enzyme Chemistry Bioengineering General Medicine Applied Microbiology and Biotechnology chemistry.chemical_compound Enzyme Biosynthesis Biochemistry Covalent bond Molecule Bioorganic chemistry Agarose Biotechnology
Zdroj:	Biotechnology Letters. 7:297-302
ISSN:	1573-6776 0141-5492
DOI:	10.1007/bf01030274
Popis:	The multienzyme enniatin synthetase was covalently immobilized to N-hydroxysuccinimide activated agarose. The stability of the immobilized enzyme at 25°C was enhanced compared to the soluble enzyme. Immobilization experiments also indicated that the enniatins are synthesized by a single molecule and thus do not require interactions of several enzyme molecules.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::10e069a5eca25db74fc4be61bcea7263 https://doi.org/10.1007/bf01030274 Zobrazit plný text záznamu Full text from SpringerLink