Cloning and Expression of Aspergillus tamarii FS132 Lipase Gene in Pichia pastoris

A lipase gene (atl) was cloned from Aspergillus tamarii FS132 for the first time. The gene was found to have an open reading frame of 1024 base pairs (bp), and the coding region of the gene contained two introns (51 bp and 52 bp). Multi-alignment analysis of the deduced amino acid sequence indicated...

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Detalles Bibliográficos
Autores principales: Shi, Bihong, Zeng, Liqing, Song, Haolei, Shi, Qiaoqin, Wu, Songgang
Formato: Texto
Lenguaje:English
Publicado: Molecular Diversity Preservation International (MDPI) 2010
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2904922/
https://www.ncbi.nlm.nih.gov/pubmed/20640158
http://dx.doi.org/10.3390/ijms11062373
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author Shi, Bihong
Zeng, Liqing
Song, Haolei
Shi, Qiaoqin
Wu, Songgang
author_facet Shi, Bihong
Zeng, Liqing
Song, Haolei
Shi, Qiaoqin
Wu, Songgang
author_sort Shi, Bihong
collection PubMed
description A lipase gene (atl) was cloned from Aspergillus tamarii FS132 for the first time. The gene was found to have an open reading frame of 1024 base pairs (bp), and the coding region of the gene contained two introns (51 bp and 52 bp). Multi-alignment analysis of the deduced amino acid sequence indicated high homology between the enzyme and mono-and diacylglycerol lipases from fungi Aspergillus. The recombinant lipase was expressed in Pichia pastoris GS115 cells. The recombinant lipase was found to have a molecular mass of 36.7 kDa, and it exhibited lipase activity of 20 U/mL in culture supernatant when tributyrin was used as the substrate.
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spelling pubmed-29049222010-07-16 Cloning and Expression of Aspergillus tamarii FS132 Lipase Gene in Pichia pastoris Shi, Bihong Zeng, Liqing Song, Haolei Shi, Qiaoqin Wu, Songgang Int J Mol Sci Article A lipase gene (atl) was cloned from Aspergillus tamarii FS132 for the first time. The gene was found to have an open reading frame of 1024 base pairs (bp), and the coding region of the gene contained two introns (51 bp and 52 bp). Multi-alignment analysis of the deduced amino acid sequence indicated high homology between the enzyme and mono-and diacylglycerol lipases from fungi Aspergillus. The recombinant lipase was expressed in Pichia pastoris GS115 cells. The recombinant lipase was found to have a molecular mass of 36.7 kDa, and it exhibited lipase activity of 20 U/mL in culture supernatant when tributyrin was used as the substrate. Molecular Diversity Preservation International (MDPI) 2010-06-03 /pmc/articles/PMC2904922/ /pubmed/20640158 http://dx.doi.org/10.3390/ijms11062373 Text en © 2010 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland. http://creativecommons.org/licenses/by/3.0 This article is an open-access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).
spellingShingle Article
Shi, Bihong
Zeng, Liqing
Song, Haolei
Shi, Qiaoqin
Wu, Songgang
Cloning and Expression of Aspergillus tamarii FS132 Lipase Gene in Pichia pastoris
title Cloning and Expression of Aspergillus tamarii FS132 Lipase Gene in Pichia pastoris
title_full Cloning and Expression of Aspergillus tamarii FS132 Lipase Gene in Pichia pastoris
title_fullStr Cloning and Expression of Aspergillus tamarii FS132 Lipase Gene in Pichia pastoris
title_full_unstemmed Cloning and Expression of Aspergillus tamarii FS132 Lipase Gene in Pichia pastoris
title_short Cloning and Expression of Aspergillus tamarii FS132 Lipase Gene in Pichia pastoris
title_sort cloning and expression of aspergillus tamarii fs132 lipase gene in pichia pastoris
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2904922/
https://www.ncbi.nlm.nih.gov/pubmed/20640158
http://dx.doi.org/10.3390/ijms11062373
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AT songhaolei cloningandexpressionofaspergillustamariifs132lipasegeneinpichiapastoris
AT shiqiaoqin cloningandexpressionofaspergillustamariifs132lipasegeneinpichiapastoris
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