Characterization of biotechnologically relevant extracellular lipase produced by Aspergillus terreus NCFT 4269.10
Abstract 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 96 h. Among the domestic oils tested, the maximum lipa...
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Sociedade Brasileira de Microbiologia
2016-03-01
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doaj-de1c46d8633b4b43a712a15e79f7409e2020-11-24T23:22:25ZengSociedade Brasileira de MicrobiologiaBrazilian Journal of Microbiology1678-44052016-03-0147114314910.1016/j.bjm.2015.11.026S1517-83822016000100143Characterization of biotechnologically relevant extracellular lipase produced by Aspergillus terreus NCFT 4269.10Bijay Kumar SethiPrativa Kumari NandaSantilata SahooAbstract 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 96 h. 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 46.3 kDa 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 1 h, and the optimum enzyme–substrate reaction time was 30 min. 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 (1 mM) 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.http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822016000100143&lng=en&tlng=enAspergillus terreusLipaseLiquid static surface fermentationSolid-state fermentation |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Bijay Kumar Sethi Prativa Kumari Nanda Santilata Sahoo |
spellingShingle |
Bijay Kumar Sethi Prativa Kumari Nanda Santilata Sahoo Characterization of biotechnologically relevant extracellular lipase produced by Aspergillus terreus NCFT 4269.10 Brazilian Journal of Microbiology Aspergillus terreus Lipase Liquid static surface fermentation Solid-state fermentation |
author_facet |
Bijay Kumar Sethi Prativa Kumari Nanda Santilata Sahoo |
author_sort |
Bijay Kumar Sethi |
title |
Characterization of biotechnologically relevant extracellular lipase produced by Aspergillus terreus NCFT 4269.10 |
title_short |
Characterization of biotechnologically relevant extracellular lipase produced by Aspergillus terreus NCFT 4269.10 |
title_full |
Characterization of biotechnologically relevant extracellular lipase produced by Aspergillus terreus NCFT 4269.10 |
title_fullStr |
Characterization of biotechnologically relevant extracellular lipase produced by Aspergillus terreus NCFT 4269.10 |
title_full_unstemmed |
Characterization of biotechnologically relevant extracellular lipase produced by Aspergillus terreus NCFT 4269.10 |
title_sort |
characterization of biotechnologically relevant extracellular lipase produced by aspergillus terreus ncft 4269.10 |
publisher |
Sociedade Brasileira de Microbiologia |
series |
Brazilian Journal of Microbiology |
issn |
1678-4405 |
publishDate |
2016-03-01 |
description |
Abstract 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 96 h. 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 46.3 kDa 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 1 h, and the optimum enzyme–substrate reaction time was 30 min. 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 (1 mM) 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. |
topic |
Aspergillus terreus Lipase Liquid static surface fermentation Solid-state fermentation |
url |
http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822016000100143&lng=en&tlng=en |
work_keys_str_mv |
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