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Purification and properties of a lipase from Penicillium chrysogenum isolated from industrial wastes
Author(s) -
Ferrer Manuel,
Plou Francisco J,
Nuero Oscar M,
Reyes Fuensanta,
Ballesteros Antonio
Publication year - 2000
Publication title -
journal of chemical technology and biotechnology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.64
H-Index - 117
eISSN - 1097-4660
pISSN - 0268-2575
DOI - 10.1002/1097-4660(200007)75:7<569::aid-jctb258>3.0.co;2-s
Subject(s) - penicillium chrysogenum , lipase , hydrolysis , chemistry , chromatography , anion exchanger , molecular mass , pulmonary surfactant , aqueous solution , triacylglycerol lipase , ion exchange , enzyme , organic chemistry , biochemistry , ion
A fungal lipase was isolated from the wastes of industrial cultures of Penicillium chrysogenum employed in antibiotics production. Lipase activity was only detected in solid aggregates present in the protein concentrates. To extract the lipase, Triton X‐100 was the most suitable surfactant. The lipase was further purified by hydrophobic interaction and anion exchange chromatography. A molecular mass of approx 40 kDa and a pI of approx 3.8 were estimated. Optimum pH and temperature were 7.9–8.1 and 45 °C respectively. Although its activity in the hydrolysis of lipids and esters is not very high, the lipase from P chrysogenum proved to be notably efficient in several synthetic reactions in non‐aqueous media. © 2000 Society of Chemical Industry