Characterization of biotechnologically relevant extracellular lipase produced by Aspergillus terreus NCFT 4269.10

• Published in: Brazilian journal of microbiology Vol. 47; no. 1; pp. 143 - 149
• Main Authors: Sethi, Bijay Kumar, Nanda, Prativa Kumari, Sahoo, Santilata
• Format: Journal Article
• Language: English
• Published: Brazil Elsevier Editora Ltda 01.01.2016; Springer Nature B.V; Elsevier; Sociedade Brasileira de Microbiologia
• Subjects: Aspergillus - enzymology; Aspergillus terreus; Biosynthesis; Cations, Divalent - metabolism; Electrophoresis, Polyacrylamide Gel; Enzyme Activators - analysis; Enzyme Inhibitors - analysis; Enzyme Stability; Enzymes; Fermentation; Hydrogen-Ion Concentration; Industrial Microbiology; Lipase; Lipase - chemistry; Lipase - isolation & purification; Lipase - metabolism; Liquid static surface fermentation; Mercaptoethanol - metabolism; Metals - metabolism; MICROBIOLOGY; Molecular Weight; Solid-state fermentation; Temperature; Vegetable oils; Solid-state fermentation; Aspergillus terreus; Lipase; Liquid static surface fermentation
• ISSN: 1517-8382; 1678-4405; 1678-4405
• DOI: 10.1016/j.bjm.2015.11.026

Enzyme production by Aspergillus terreus NCFT 4269.10 was studied under liquid static surface and solid-state fermentation using mustard oil cake as a substrate. The maximum lipase biosynthesis was observed after incubation at 30°C for 96h. Among the domestic oils tested, the maximum lipase biosynthesis was achieved using palm oil. The crude lipase was purified 2.56-fold to electrophoretic homogeneity, with a yield of 8.44%, and the protein had a molecular weight of 46.3kDa as determined by SDS-PAGE. Enzyme characterization confirmed that the purified lipase was most active at pH 6.0, temperature of 50°C, and substrate concentration of 1.5%. The enzyme was thermostable at 60°C for 1h, and the optimum enzyme–substrate reaction time was 30min. Sodium dodecyl sulfate and commercial detergents did not significantly affect lipase activity during 30-min incubation at 30°C. Among the metal ions tested, the maximum lipase activity was attained in the presence of Zn2+, followed by Mg2+ and Fe2+. Lipase activity was not significantly affected in the presence of ethylenediaminetetraacetic acid, sodium lauryl sulfate and Triton X-100. Phenylmethylsulfonyl fluoride (1mM) and the reducing, β-mercaptoethanol significantly inhibited lipase activity. The remarkable stability in the presence of detergents, additives, inhibitors and metal ions makes this lipase unique and a potential candidate for significant biotechnological exploitation.