Differential induction, purification and characterization of cold active lipase from Yarrowia lipolytica NCIM 3639

• Published in: Bioresource technology Vol. 102; no. 22; pp. 10663 - 10670
• Main Authors: Sathish Yadav, K.N., Adsul, M.G., Bastawde, K.B., Jadhav, D.D., Thulasiram, H.V., Gokhale, D.V.
• Format: Journal Article
• Language: English
• Published: Kidlington Elsevier Ltd 01.11.2011; Elsevier
• Subjects: Acetates; Acetates - metabolism; Amino Acid Sequence; Biological and medical sciences; Cell bound lipase; Chromatography, Liquid; Cold active lipase; Cold Temperature; Electrophoresis, Polyacrylamide Gel; Enzyme Induction - drug effects; Enzyme Stability - drug effects; Extracellular lipase; Extracellular Space - drug effects; Extracellular Space - enzymology; Fingers; Fundamental and applied biological sciences. Psychology; Hydrogen-Ion Concentration - drug effects; Hydrolysis - drug effects; Ions; Kinetics; Lavandulyl acetate; Lipase; Lipase - biosynthesis; Lipase - chemistry; Lipase - isolation & purification; Mass Spectrometry; Metals - pharmacology; Molecular Sequence Data; Molecular Weight; Monoterpenes - metabolism; Nitrophenols - metabolism; Olea; Oligomeric lipase; Olive Oil; Optimization; Organophosphorus Compounds - metabolism; Peptide Mapping; Peptides; Plant Oils - chemistry; Polysorbates - pharmacology; Purification; Substrate Specificity - drug effects; Temperature; Time Factors; Yarrowia - cytology; Yarrowia - drug effects; Yarrowia - enzymology; Yarrowia - growth & development; Yarrowia lipolytica; Cold active lipase; Cell bound lipase; Oligomeric lipase; Extracellular lipase; Lavandulyl acetate; Ascomycota; Purification; Cold; Enzyme; Acetate; Oligomer; Extracellular; Fungi; Lipolytic enzyme; Yarrowia lipolytica
• ISSN: 0960-8524; 1873-2976
• DOI: 10.1016/j.biortech.2011.09.013

► The lipase is multimeric in nature and such lipases are not reported so far. ► The induction of intra- and extracellular lipase depends on the substrate used for enzyme production. ► It is cold active enzyme. ► Extracellular and cell bound lipases showed the preference over the opposite antipodes of lavandulyl acetate. The production, purification and characterization of cold active lipases by Yarrowia lipolytica NCIM 3639 is described. The study presents a new finding of production of cell bound and extracellular lipase activities depending upon the substrate used for growth. The strain produced cell bound and extracellular lipase activity when grown on olive oil and Tween 80, respectively. The organism grew profusely at 20°C and at initial pH of 5.5, producing maximum extracellular lipase. The purified lipase has a molecular mass of 400kDa having 20 subunits forming a multimeric native protein. Further the enzyme displayed an optimum pH of 5.0 and optimum temperature of 25°C. Peptide mass finger printing reveled that some peptides showed homologues sequence (42%) to Yarrowia lipolytica LIP8p. The studies on hydrolysis of racemic lavandulyl acetate revealed that extracellular and cell bound lipases show preference over the opposite antipodes of irregular monoterpene, lavandulyl acetate.