Production of a solvent, detergent and thermotolerant lipase by a newly isolated Acinetobacter sp. in submerged and solid-state fermentations

The lipase production ability of a newly isolated Acinetobacter sp. in submerged (SmF) and solid-state (SSF) fermentations was evaluated. The results demonstrated this strain as one of the rare bacterium, which is able to grow and produce lipase in SSF even more than SmF. Coconut oil cake as a cheap...

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Main Authors: Khoramnia, Anahita, Ebrahimpour, Afshin, Beh, Boon Kee, Lai, Oi Ming
Format: Article
Language:English
Published: Hindawi Publishing Corporation 2011
Online Access:http://psasir.upm.edu.my/id/eprint/22340/1/Production%20of%20a%20solvent.pdf
http://psasir.upm.edu.my/id/eprint/22340/
http://www.hindawi.com/journals/bmri/2011/702179/
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spelling my.upm.eprints.223402015-09-22T02:47:15Z http://psasir.upm.edu.my/id/eprint/22340/ Production of a solvent, detergent and thermotolerant lipase by a newly isolated Acinetobacter sp. in submerged and solid-state fermentations Khoramnia, Anahita Ebrahimpour, Afshin Beh, Boon Kee Lai, Oi Ming The lipase production ability of a newly isolated Acinetobacter sp. in submerged (SmF) and solid-state (SSF) fermentations was evaluated. The results demonstrated this strain as one of the rare bacterium, which is able to grow and produce lipase in SSF even more than SmF. Coconut oil cake as a cheap agroindustrial residue was employed as the solid substrate. The lipase production was optimized in both media using artificial neural network. Multilayer normal and full feed forward backpropagation networks were selected to build predictive models to optimize the culture parameters for lipase production in SmF and SSF systems, respectively. The produced models for both systems showed high predictive accuracy where the obtained conditions were close together. The produced enzyme was characterized as a thermotolerant lipase, although the organism was mesophile. The optimum temperature for the enzyme activity was 45°C where 63% of its activity remained at 70°C after 2 h. This lipase remained active after 24 h in a broad range of pH (6–11). The lipase demonstrated strong solvent and detergent tolerance potentials. Therefore, this inexpensive lipase production for such a potent and industrially valuable lipase is promising and of considerable commercial interest for biotechnological applications. Hindawi Publishing Corporation 2011 Article PeerReviewed application/pdf en http://psasir.upm.edu.my/id/eprint/22340/1/Production%20of%20a%20solvent.pdf Khoramnia, Anahita and Ebrahimpour, Afshin and Beh, Boon Kee and Lai, Oi Ming (2011) Production of a solvent, detergent and thermotolerant lipase by a newly isolated Acinetobacter sp. in submerged and solid-state fermentations. Journal of Biomedicine and Biotechnology, 2011. art. no. 702179. pp. 1-12. ISSN 1110-7243; ESSN: 1110-7251 http://www.hindawi.com/journals/bmri/2011/702179/ 10.1155/2011/702179
institution Universiti Putra Malaysia
building UPM Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Putra Malaysia
content_source UPM Institutional Repository
url_provider http://psasir.upm.edu.my/
language English
description The lipase production ability of a newly isolated Acinetobacter sp. in submerged (SmF) and solid-state (SSF) fermentations was evaluated. The results demonstrated this strain as one of the rare bacterium, which is able to grow and produce lipase in SSF even more than SmF. Coconut oil cake as a cheap agroindustrial residue was employed as the solid substrate. The lipase production was optimized in both media using artificial neural network. Multilayer normal and full feed forward backpropagation networks were selected to build predictive models to optimize the culture parameters for lipase production in SmF and SSF systems, respectively. The produced models for both systems showed high predictive accuracy where the obtained conditions were close together. The produced enzyme was characterized as a thermotolerant lipase, although the organism was mesophile. The optimum temperature for the enzyme activity was 45°C where 63% of its activity remained at 70°C after 2 h. This lipase remained active after 24 h in a broad range of pH (6–11). The lipase demonstrated strong solvent and detergent tolerance potentials. Therefore, this inexpensive lipase production for such a potent and industrially valuable lipase is promising and of considerable commercial interest for biotechnological applications.
format Article
author Khoramnia, Anahita
Ebrahimpour, Afshin
Beh, Boon Kee
Lai, Oi Ming
spellingShingle Khoramnia, Anahita
Ebrahimpour, Afshin
Beh, Boon Kee
Lai, Oi Ming
Production of a solvent, detergent and thermotolerant lipase by a newly isolated Acinetobacter sp. in submerged and solid-state fermentations
author_facet Khoramnia, Anahita
Ebrahimpour, Afshin
Beh, Boon Kee
Lai, Oi Ming
author_sort Khoramnia, Anahita
title Production of a solvent, detergent and thermotolerant lipase by a newly isolated Acinetobacter sp. in submerged and solid-state fermentations
title_short Production of a solvent, detergent and thermotolerant lipase by a newly isolated Acinetobacter sp. in submerged and solid-state fermentations
title_full Production of a solvent, detergent and thermotolerant lipase by a newly isolated Acinetobacter sp. in submerged and solid-state fermentations
title_fullStr Production of a solvent, detergent and thermotolerant lipase by a newly isolated Acinetobacter sp. in submerged and solid-state fermentations
title_full_unstemmed Production of a solvent, detergent and thermotolerant lipase by a newly isolated Acinetobacter sp. in submerged and solid-state fermentations
title_sort production of a solvent, detergent and thermotolerant lipase by a newly isolated acinetobacter sp. in submerged and solid-state fermentations
publisher Hindawi Publishing Corporation
publishDate 2011
url http://psasir.upm.edu.my/id/eprint/22340/1/Production%20of%20a%20solvent.pdf
http://psasir.upm.edu.my/id/eprint/22340/
http://www.hindawi.com/journals/bmri/2011/702179/
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score 13.211869