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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...

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Autores principales: Ran, Chao, He, Suxu, Yang, Yalin, Huang, Lu, Zhou, Zhigang
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2015
Materias:
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.
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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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