Purification and properties of a lipase from Penicillium chrysogenum isolated from industrial wastes

• Published in: Journal of chemical technology and biotechnology (1986) Vol. 75; no. 7; pp. 569 - 576
• Main Authors: Ferrer, Manuel, Plou, Francisco J, Nuero, Oscar M, Reyes, Fuensanta, Ballesteros, Antonio
• Format: Journal Article
• Language: English
• Published: Chichester, UK John Wiley & Sons, Ltd 01.07.2000; Wiley
• Subjects: Biological and medical sciences; Biology of microorganisms of confirmed or potential industrial interest; Biotechnology; Cell culture; filamentous fungi; Fundamental and applied biological sciences. Psychology; Fungi; Hydrolysis; Hydrophobic chromatography; Industrial wastes; lipases; Miscellaneous; Mission oriented research; Molecular weight; Penicillium; Penicillium chrysogenum; Purification; Surface active agents; Temperature; Purification; Stability; Enzyme; Triacylglycerol lipase; Environmental factor; Esterases; Carboxylic ester hydrolases; Penicillium chrysogenum; Fungi; Industrial waste; Enzymatic activity; Substrate specificity; Hydrolases; Extraction; Fungi Imperfecti; Physicochemical properties; Thallophyta
• ISSN: 0268-2575; 1097-4660
• DOI: 10.1002/1097-4660(200007)75:7<569::AID-JCTB258>3.0.CO;2-S

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