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Purification and characterization of a surfactant-compatible lipase from Aspergillus tamarii JGIF06 exhibiting energy-efficient removal of oil stains from polycotton fabric
An extracellular lipase with 23,666.66 U/ml/min activity was produced by Aspergillus tamarii JGIF06 under submerged fermentation in mineral salt medium containing coconut oil (2.5 % v/v), tryptone (2 % w/v) and ammonium chloride (2 % w/v), with initial pH of 5 ± 0.2, incubated at 25 °C for 7 days on...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer Berlin Heidelberg
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4909032/ https://www.ncbi.nlm.nih.gov/pubmed/28330188 http://dx.doi.org/10.1007/s13205-016-0449-z |
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author | Das, Arijit Shivakumar, Srividya Bhattacharya, Sourav Shakya, Sujina Swathi, S. S. |
author_facet | Das, Arijit Shivakumar, Srividya Bhattacharya, Sourav Shakya, Sujina Swathi, S. S. |
author_sort | Das, Arijit |
collection | PubMed |
description | An extracellular lipase with 23,666.66 U/ml/min activity was produced by Aspergillus tamarii JGIF06 under submerged fermentation in mineral salt medium containing coconut oil (2.5 % v/v), tryptone (2 % w/v) and ammonium chloride (2 % w/v), with initial pH of 5 ± 0.2, incubated at 25 °C for 7 days on a rotary shaker at 120 rpm. A 7.9-fold increase in lipase-specific activity was recorded after purification by DEAE Sepharose ion exchange and Sephadex G200 column chromatography. The apparent molecular mass of this enzyme was revealed as 50 kDa by sodium dodecyl sulphate polyacrylamide gel electrophoresis. The optimal lipase activity was recorded at pH 4 and 37 °C. The enzyme revealed broad specificity towards different vegetable oils. The K (m) and V (max) of the lipase on olive oil was found to be 330.4 mg and 53,690 U/ml/min, respectively. The lipase activity was stable in the presence of surfactants such as cetrimonium bromide, sodium dodecyl sulphate and Tween 80, and metal ions and reagents such as Ca(2+), Ba(2+) and 2-mercaptoethanol. However, the activity was greatly reduced in the presence of organic solvents such as chloroform. The stain removal potential of the crude lipase was determined on polycotton fabric pieces stained with peanut oil. Lipase added to cold water alone significantly enhanced the removal of stain by 152 %. The addition of lipase also improved the stain removal efficiency of a commercially available detergent in the presence of either cold (25 ± 2 °C) or hot (65 ± 2 °C) water. The current findings suggest the potentiality of this enzyme for energy-efficient biocatalytic application. |
format | Online Article Text |
id | pubmed-4909032 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Springer Berlin Heidelberg |
record_format | MEDLINE/PubMed |
spelling | pubmed-49090322016-06-15 Purification and characterization of a surfactant-compatible lipase from Aspergillus tamarii JGIF06 exhibiting energy-efficient removal of oil stains from polycotton fabric Das, Arijit Shivakumar, Srividya Bhattacharya, Sourav Shakya, Sujina Swathi, S. S. 3 Biotech Original Article An extracellular lipase with 23,666.66 U/ml/min activity was produced by Aspergillus tamarii JGIF06 under submerged fermentation in mineral salt medium containing coconut oil (2.5 % v/v), tryptone (2 % w/v) and ammonium chloride (2 % w/v), with initial pH of 5 ± 0.2, incubated at 25 °C for 7 days on a rotary shaker at 120 rpm. A 7.9-fold increase in lipase-specific activity was recorded after purification by DEAE Sepharose ion exchange and Sephadex G200 column chromatography. The apparent molecular mass of this enzyme was revealed as 50 kDa by sodium dodecyl sulphate polyacrylamide gel electrophoresis. The optimal lipase activity was recorded at pH 4 and 37 °C. The enzyme revealed broad specificity towards different vegetable oils. The K (m) and V (max) of the lipase on olive oil was found to be 330.4 mg and 53,690 U/ml/min, respectively. The lipase activity was stable in the presence of surfactants such as cetrimonium bromide, sodium dodecyl sulphate and Tween 80, and metal ions and reagents such as Ca(2+), Ba(2+) and 2-mercaptoethanol. However, the activity was greatly reduced in the presence of organic solvents such as chloroform. The stain removal potential of the crude lipase was determined on polycotton fabric pieces stained with peanut oil. Lipase added to cold water alone significantly enhanced the removal of stain by 152 %. The addition of lipase also improved the stain removal efficiency of a commercially available detergent in the presence of either cold (25 ± 2 °C) or hot (65 ± 2 °C) water. The current findings suggest the potentiality of this enzyme for energy-efficient biocatalytic application. Springer Berlin Heidelberg 2016-06-10 2016-12 /pmc/articles/PMC4909032/ /pubmed/28330188 http://dx.doi.org/10.1007/s13205-016-0449-z Text en © The Author(s) 2016 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. |
spellingShingle | Original Article Das, Arijit Shivakumar, Srividya Bhattacharya, Sourav Shakya, Sujina Swathi, S. S. Purification and characterization of a surfactant-compatible lipase from Aspergillus tamarii JGIF06 exhibiting energy-efficient removal of oil stains from polycotton fabric |
title | Purification and characterization of a surfactant-compatible lipase from Aspergillus tamarii JGIF06 exhibiting energy-efficient removal of oil stains from polycotton fabric |
title_full | Purification and characterization of a surfactant-compatible lipase from Aspergillus tamarii JGIF06 exhibiting energy-efficient removal of oil stains from polycotton fabric |
title_fullStr | Purification and characterization of a surfactant-compatible lipase from Aspergillus tamarii JGIF06 exhibiting energy-efficient removal of oil stains from polycotton fabric |
title_full_unstemmed | Purification and characterization of a surfactant-compatible lipase from Aspergillus tamarii JGIF06 exhibiting energy-efficient removal of oil stains from polycotton fabric |
title_short | Purification and characterization of a surfactant-compatible lipase from Aspergillus tamarii JGIF06 exhibiting energy-efficient removal of oil stains from polycotton fabric |
title_sort | purification and characterization of a surfactant-compatible lipase from aspergillus tamarii jgif06 exhibiting energy-efficient removal of oil stains from polycotton fabric |
topic | Original Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4909032/ https://www.ncbi.nlm.nih.gov/pubmed/28330188 http://dx.doi.org/10.1007/s13205-016-0449-z |
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