Heterologous expression and biochemical characterization of a novel cold-active α-amylase from the Antarctic bacteria Pseudoalteromonas sp. 2-3
© 2018 Elsevier Inc.α-Amylase is an endo-acting enzyme which catalyzes random hydrolysis of starch. These enzymes are used in various biotechnological processes including the textile, paper, food, biofuels, detergents and pharmaceutical industries. The use of active enzymes at low temperatures has a...
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Online Access: | https://doi.org/10.1016/j.pep.2018.11.009 https://repositorio.uchile.cl/handle/2250/171386 |
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ftunivchile:oai:repositorio.uchile.cl:2250/171386 2023-05-15T13:34:35+02:00 Heterologous expression and biochemical characterization of a novel cold-active α-amylase from the Antarctic bacteria Pseudoalteromonas sp. 2-3 Sanchez, Anamaria C. Ravanal, María Cristina Andrews, Barbara A. Asenjo, Juan A. 2019 application/pdf https://doi.org/10.1016/j.pep.2018.11.009 https://repositorio.uchile.cl/handle/2250/171386 en eng Academic Press Inc. Protein Expression and Purification, Volumen 155, 10465928 doi:10.1016/j.pep.2018.11.009 https://repositorio.uchile.cl/handle/2250/171386 Attribution-NonCommercial-NoDerivs 3.0 Chile http://creativecommons.org/licenses/by-nc-nd/3.0/cl/ CC-BY-NC-ND Protein Expression and Purification Antarctic bacteria Heterologous expression Pseudoalteromonas sp. 2–3 Psychrophilic Starch α-Amylase Artículo de revista 2019 ftunivchile https://doi.org/10.1016/j.pep.2018.11.009 2023-01-22T00:53:26Z © 2018 Elsevier Inc.α-Amylase is an endo-acting enzyme which catalyzes random hydrolysis of starch. These enzymes are used in various biotechnological processes including the textile, paper, food, biofuels, detergents and pharmaceutical industries. The use of active enzymes at low temperatures has a high potential because these enzymes would avoid the demand for heating during the process thereby reducing costs. In this work, the gene of α-amylase from Pseudoalteromonas sp. 2–3 (Antarctic bacteria) has been sequenced and expressed in Escherichia coli BL21(DE3). The ORF of the α-amylase gene cloned into pET22b(+) is 1824 bp long and codes for a protein of 607 amino acid residues including a His6-tag. The mature protein has a calculated molecular mass of 68.8 kDa. Recombinant α-amylase was purified with Ni-NTA affinity chromatography. The purified enzyme is active on potato starch with a Km of 6.94 mg/ml and Vmax of 0.27 mg/ml*min. The pH optimum is 8.0 and the optimal temperature is 20 Article in Journal/Newspaper Antarc* Antarctic Universidad de Chile: Repositorio académico Antarctic The Antarctic Protein Expression and Purification 155 78 85 |
institution |
Open Polar |
collection |
Universidad de Chile: Repositorio académico |
op_collection_id |
ftunivchile |
language |
English |
topic |
Antarctic bacteria Heterologous expression Pseudoalteromonas sp. 2–3 Psychrophilic Starch α-Amylase |
spellingShingle |
Antarctic bacteria Heterologous expression Pseudoalteromonas sp. 2–3 Psychrophilic Starch α-Amylase Sanchez, Anamaria C. Ravanal, María Cristina Andrews, Barbara A. Asenjo, Juan A. Heterologous expression and biochemical characterization of a novel cold-active α-amylase from the Antarctic bacteria Pseudoalteromonas sp. 2-3 |
topic_facet |
Antarctic bacteria Heterologous expression Pseudoalteromonas sp. 2–3 Psychrophilic Starch α-Amylase |
description |
© 2018 Elsevier Inc.α-Amylase is an endo-acting enzyme which catalyzes random hydrolysis of starch. These enzymes are used in various biotechnological processes including the textile, paper, food, biofuels, detergents and pharmaceutical industries. The use of active enzymes at low temperatures has a high potential because these enzymes would avoid the demand for heating during the process thereby reducing costs. In this work, the gene of α-amylase from Pseudoalteromonas sp. 2–3 (Antarctic bacteria) has been sequenced and expressed in Escherichia coli BL21(DE3). The ORF of the α-amylase gene cloned into pET22b(+) is 1824 bp long and codes for a protein of 607 amino acid residues including a His6-tag. The mature protein has a calculated molecular mass of 68.8 kDa. Recombinant α-amylase was purified with Ni-NTA affinity chromatography. The purified enzyme is active on potato starch with a Km of 6.94 mg/ml and Vmax of 0.27 mg/ml*min. The pH optimum is 8.0 and the optimal temperature is 20 |
format |
Article in Journal/Newspaper |
author |
Sanchez, Anamaria C. Ravanal, María Cristina Andrews, Barbara A. Asenjo, Juan A. |
author_facet |
Sanchez, Anamaria C. Ravanal, María Cristina Andrews, Barbara A. Asenjo, Juan A. |
author_sort |
Sanchez, Anamaria C. |
title |
Heterologous expression and biochemical characterization of a novel cold-active α-amylase from the Antarctic bacteria Pseudoalteromonas sp. 2-3 |
title_short |
Heterologous expression and biochemical characterization of a novel cold-active α-amylase from the Antarctic bacteria Pseudoalteromonas sp. 2-3 |
title_full |
Heterologous expression and biochemical characterization of a novel cold-active α-amylase from the Antarctic bacteria Pseudoalteromonas sp. 2-3 |
title_fullStr |
Heterologous expression and biochemical characterization of a novel cold-active α-amylase from the Antarctic bacteria Pseudoalteromonas sp. 2-3 |
title_full_unstemmed |
Heterologous expression and biochemical characterization of a novel cold-active α-amylase from the Antarctic bacteria Pseudoalteromonas sp. 2-3 |
title_sort |
heterologous expression and biochemical characterization of a novel cold-active α-amylase from the antarctic bacteria pseudoalteromonas sp. 2-3 |
publisher |
Academic Press Inc. |
publishDate |
2019 |
url |
https://doi.org/10.1016/j.pep.2018.11.009 https://repositorio.uchile.cl/handle/2250/171386 |
geographic |
Antarctic The Antarctic |
geographic_facet |
Antarctic The Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_source |
Protein Expression and Purification |
op_relation |
Protein Expression and Purification, Volumen 155, 10465928 doi:10.1016/j.pep.2018.11.009 https://repositorio.uchile.cl/handle/2250/171386 |
op_rights |
Attribution-NonCommercial-NoDerivs 3.0 Chile http://creativecommons.org/licenses/by-nc-nd/3.0/cl/ |
op_rightsnorm |
CC-BY-NC-ND |
op_doi |
https://doi.org/10.1016/j.pep.2018.11.009 |
container_title |
Protein Expression and Purification |
container_volume |
155 |
container_start_page |
78 |
op_container_end_page |
85 |
_version_ |
1766054493027303424 |