Purification and some properties of Pseudomonas fluorescens lipase

Autor:	H, Sztajer, J, Borkowski, K, Sobiech
Rok vydání:	1991
Předmět:	Sepharose Temperature Chemical Precipitation Lipase Hydrogen-Ion Concentration Chromatography Agarose Electrophoresis Disc Pseudomonas fluorescens Chromatography DEAE-Cellulose
Zdroj:	Biotechnology and applied biochemistry. 13(1)
ISSN:	0885-4513
Popis:	Lipase (triacylglycerol lipase, EC 3.1.1.3) has been purified from Pseudomonas fluorescens wild strain by chromatography on DEAE-cellulose and octyl-Sepharose CL-4B. The yield was 21% and the specific activity of the purified enzyme 4780 U/mg protein. It showed a Mr of about 45 x 10(4) by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The enzyme is active over a wide pH range and at 50-55 degrees C.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::a5f3f5aa8ddf901c67f7d006089220c6 https://pubmed.ncbi.nlm.nih.gov/1905137 Zobrazit plný text záznamu Plný text