Stability and catalytic properties of penicillin acylase in systems with low water content

Autor:	M I, Youshko, A V, Sinev, V K, Svedas
Rok vydání:	1999
Předmět:	Enzyme Stability Thermodynamics Water Penicillin Amidase Enzymes Immobilized Catalysis
Zdroj:	Biochemistry. Biokhimiia. 64(10)
ISSN:	0006-2979
Popis:	Stability and catalytic properties of native and immobilized penicillin acylase were studied in systems with low water content. Preparations of both native and immobilized penicillin acylase demonstrated the catalytic activity even in solid-phase systems which contained 3-5 wt. % of water. The stability and catalytic activity of penicillin acylase at low water content depended on the thermodynamic water activity (aw) in the system.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::edca7afbb2fc452efe7ebf35ea867253 https://pubmed.ncbi.nlm.nih.gov/10561568 Zobrazit plný text záznamu