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A Novel Lipase as Aquafeed Additive for Warm-Water Aquaculture
A novel Acinetobacter lipase gene lipG1was cloned from DNA extracted from intestinal sample of common carp (Cyprinus carpio), and expressed in E. coli BL21. The encoded protein was 406 amino acids in length. Phylogenetic analysis indicated that LipG1 and its relatives comprised a novel group of true...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Public Library of Science
2015
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4492967/ https://www.ncbi.nlm.nih.gov/pubmed/26147311 http://dx.doi.org/10.1371/journal.pone.0132049 |
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author | Ran, Chao He, Suxu Yang, Yalin Huang, Lu Zhou, Zhigang |
author_facet | Ran, Chao He, Suxu Yang, Yalin Huang, Lu Zhou, Zhigang |
author_sort | Ran, Chao |
collection | PubMed |
description | A novel Acinetobacter lipase gene lipG1was cloned from DNA extracted from intestinal sample of common carp (Cyprinus carpio), and expressed in E. coli BL21. The encoded protein was 406 amino acids in length. Phylogenetic analysis indicated that LipG1 and its relatives comprised a novel group of true lipases produced by Gram-negative bacteria. LipG1 showed maximal activity at 40℃ and pH 8.0 when pNP decanoate (C10) was used as the substrate, and remained high activity between 20℃ and 35℃. Activity of the lipase was promoted by Ca(2+) and Mg(2+), and inhibited by Zn(2+) and Cu(2+). Moreover, LipG1 is stable with proteases, most commercial detergents and organic solvents. Substrate specificity test indicated that LipG1can hydrolyse pNP esters with acyl chain length from C2 to C16, with preference for medium-chain pNP esters (C8, C10). Lastly, LipG1was evaluated as an aquafeed additive for juvenile common carp (Cyprinus carpio). Results showed that supplementation of LipG1significantly improved the gut and heptaopancreas lipase activity of fish fed with palm oil diet. Consistently, improved feed conversion ratio and growth performance were recorded in the LipG1 feeding group, to levels comparable to the group of fish fed with soybean oil diet. Collectively, LipG1 exhibited good potential as an aquafeed additive enzyme, and deserves further characterization as the representative of a novel group of lipases. |
format | Online Article Text |
id | pubmed-4492967 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-44929672015-07-15 A Novel Lipase as Aquafeed Additive for Warm-Water Aquaculture Ran, Chao He, Suxu Yang, Yalin Huang, Lu Zhou, Zhigang PLoS One Research Article A novel Acinetobacter lipase gene lipG1was cloned from DNA extracted from intestinal sample of common carp (Cyprinus carpio), and expressed in E. coli BL21. The encoded protein was 406 amino acids in length. Phylogenetic analysis indicated that LipG1 and its relatives comprised a novel group of true lipases produced by Gram-negative bacteria. LipG1 showed maximal activity at 40℃ and pH 8.0 when pNP decanoate (C10) was used as the substrate, and remained high activity between 20℃ and 35℃. Activity of the lipase was promoted by Ca(2+) and Mg(2+), and inhibited by Zn(2+) and Cu(2+). Moreover, LipG1 is stable with proteases, most commercial detergents and organic solvents. Substrate specificity test indicated that LipG1can hydrolyse pNP esters with acyl chain length from C2 to C16, with preference for medium-chain pNP esters (C8, C10). Lastly, LipG1was evaluated as an aquafeed additive for juvenile common carp (Cyprinus carpio). Results showed that supplementation of LipG1significantly improved the gut and heptaopancreas lipase activity of fish fed with palm oil diet. Consistently, improved feed conversion ratio and growth performance were recorded in the LipG1 feeding group, to levels comparable to the group of fish fed with soybean oil diet. Collectively, LipG1 exhibited good potential as an aquafeed additive enzyme, and deserves further characterization as the representative of a novel group of lipases. Public Library of Science 2015-07-06 /pmc/articles/PMC4492967/ /pubmed/26147311 http://dx.doi.org/10.1371/journal.pone.0132049 Text en © 2015 Ran et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Ran, Chao He, Suxu Yang, Yalin Huang, Lu Zhou, Zhigang A Novel Lipase as Aquafeed Additive for Warm-Water Aquaculture |
title | A Novel Lipase as Aquafeed Additive for Warm-Water Aquaculture |
title_full | A Novel Lipase as Aquafeed Additive for Warm-Water Aquaculture |
title_fullStr | A Novel Lipase as Aquafeed Additive for Warm-Water Aquaculture |
title_full_unstemmed | A Novel Lipase as Aquafeed Additive for Warm-Water Aquaculture |
title_short | A Novel Lipase as Aquafeed Additive for Warm-Water Aquaculture |
title_sort | novel lipase as aquafeed additive for warm-water aquaculture |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4492967/ https://www.ncbi.nlm.nih.gov/pubmed/26147311 http://dx.doi.org/10.1371/journal.pone.0132049 |
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