Molecular Cloning and Characterization of a Novel α-Amylase from Antarctic Sea Ice Bacterium Pseudoalteromonas sp. M175 and Its Primary Application in Detergent
A novel cold-adapted and salt-tolerant α-amylase gene (amy175) from Antarctic sea ice bacterium Pseudoalteromonas sp. M175 was successfully cloned and expressed. The open reading frame (ORF) of amy175 had 1722 bp encoding a protein of 573 amino acids residues. Multiple alignments indicated Amy175 ha...
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ftpubmed:oai:pubmedcentral.nih.gov:6040283 2023-05-15T13:40:36+02:00 Molecular Cloning and Characterization of a Novel α-Amylase from Antarctic Sea Ice Bacterium Pseudoalteromonas sp. M175 and Its Primary Application in Detergent Wang, Xiaofei Kan, Guangfeng Ren, Xiulian Yu, Geng Shi, Cuijuan Xie, Qiuju Wen, Hua Betenbaugh, Michael 2018-06-27 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6040283/ https://doi.org/10.1155/2018/3258383 en eng Hindawi http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6040283/ http://dx.doi.org/10.1155/2018/3258383 Copyright © 2018 Xiaofei Wang et al. https://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. CC-BY Research Article Text 2018 ftpubmed https://doi.org/10.1155/2018/3258383 2018-07-29T00:11:53Z A novel cold-adapted and salt-tolerant α-amylase gene (amy175) from Antarctic sea ice bacterium Pseudoalteromonas sp. M175 was successfully cloned and expressed. The open reading frame (ORF) of amy175 had 1722 bp encoding a protein of 573 amino acids residues. Multiple alignments indicated Amy175 had seven highly conserved sequences and the putative catalytic triad (Asp244, Glu286, and Asp372). It was the first identified member of GH13_36 subfamily which contained QPDLN in the CSR V. The recombinant enzyme (Amy175) was purified to homogeneity with a molecular mass of about 62 kDa on SDS-PAGE. It had a mixed enzyme specificity of α-amylase and α-glucosidase. Amy175 displayed highest activity at pH 8.0 and 25°C and exhibited extreme salt-resistance with the maximum activity at 1 M NaCl. Amy175 was strongly stimulated by Mg2+, Ni2+, K+, 1 mM Ca2+, 1 mM Ba2+, 1 mM Pb2+, 1 mM sodium dodecyl sulphate (SDS), and 10% dimethyl sulfoxide (DMSO) but was significantly inhibited by Cu2+, Mn2+, Hg2+, 10 mM β-mercaptoethanol (β-ME), and 10% Tween 80. Amy175 demonstrated excellent resistance towards all the tested commercial detergents, and wash performance analysis displayed that the addition of Amy175 improved the stain removal efficiency. This study demonstrated that Amy175 would be proposed as a novel α-amylase source for industrial application in the future. Text Antarc* Antarctic Sea ice PubMed Central (PMC) Antarctic BioMed Research International 2018 1 16 |
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Research Article |
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Research Article Wang, Xiaofei Kan, Guangfeng Ren, Xiulian Yu, Geng Shi, Cuijuan Xie, Qiuju Wen, Hua Betenbaugh, Michael Molecular Cloning and Characterization of a Novel α-Amylase from Antarctic Sea Ice Bacterium Pseudoalteromonas sp. M175 and Its Primary Application in Detergent |
topic_facet |
Research Article |
description |
A novel cold-adapted and salt-tolerant α-amylase gene (amy175) from Antarctic sea ice bacterium Pseudoalteromonas sp. M175 was successfully cloned and expressed. The open reading frame (ORF) of amy175 had 1722 bp encoding a protein of 573 amino acids residues. Multiple alignments indicated Amy175 had seven highly conserved sequences and the putative catalytic triad (Asp244, Glu286, and Asp372). It was the first identified member of GH13_36 subfamily which contained QPDLN in the CSR V. The recombinant enzyme (Amy175) was purified to homogeneity with a molecular mass of about 62 kDa on SDS-PAGE. It had a mixed enzyme specificity of α-amylase and α-glucosidase. Amy175 displayed highest activity at pH 8.0 and 25°C and exhibited extreme salt-resistance with the maximum activity at 1 M NaCl. Amy175 was strongly stimulated by Mg2+, Ni2+, K+, 1 mM Ca2+, 1 mM Ba2+, 1 mM Pb2+, 1 mM sodium dodecyl sulphate (SDS), and 10% dimethyl sulfoxide (DMSO) but was significantly inhibited by Cu2+, Mn2+, Hg2+, 10 mM β-mercaptoethanol (β-ME), and 10% Tween 80. Amy175 demonstrated excellent resistance towards all the tested commercial detergents, and wash performance analysis displayed that the addition of Amy175 improved the stain removal efficiency. This study demonstrated that Amy175 would be proposed as a novel α-amylase source for industrial application in the future. |
format |
Text |
author |
Wang, Xiaofei Kan, Guangfeng Ren, Xiulian Yu, Geng Shi, Cuijuan Xie, Qiuju Wen, Hua Betenbaugh, Michael |
author_facet |
Wang, Xiaofei Kan, Guangfeng Ren, Xiulian Yu, Geng Shi, Cuijuan Xie, Qiuju Wen, Hua Betenbaugh, Michael |
author_sort |
Wang, Xiaofei |
title |
Molecular Cloning and Characterization of a Novel α-Amylase from Antarctic Sea Ice Bacterium Pseudoalteromonas sp. M175 and Its Primary Application in Detergent |
title_short |
Molecular Cloning and Characterization of a Novel α-Amylase from Antarctic Sea Ice Bacterium Pseudoalteromonas sp. M175 and Its Primary Application in Detergent |
title_full |
Molecular Cloning and Characterization of a Novel α-Amylase from Antarctic Sea Ice Bacterium Pseudoalteromonas sp. M175 and Its Primary Application in Detergent |
title_fullStr |
Molecular Cloning and Characterization of a Novel α-Amylase from Antarctic Sea Ice Bacterium Pseudoalteromonas sp. M175 and Its Primary Application in Detergent |
title_full_unstemmed |
Molecular Cloning and Characterization of a Novel α-Amylase from Antarctic Sea Ice Bacterium Pseudoalteromonas sp. M175 and Its Primary Application in Detergent |
title_sort |
molecular cloning and characterization of a novel α-amylase from antarctic sea ice bacterium pseudoalteromonas sp. m175 and its primary application in detergent |
publisher |
Hindawi |
publishDate |
2018 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6040283/ https://doi.org/10.1155/2018/3258383 |
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Antarctic |
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Antarctic |
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Antarc* Antarctic Sea ice |
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Antarc* Antarctic Sea ice |
op_relation |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6040283/ http://dx.doi.org/10.1155/2018/3258383 |
op_rights |
Copyright © 2018 Xiaofei Wang et al. https://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
op_rightsnorm |
CC-BY |
op_doi |
https://doi.org/10.1155/2018/3258383 |
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BioMed Research International |
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2018 |
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16 |
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