Functional expression of a novel α-amylase from Antarctic psychrotolerant fungus for baking industry and its magnetic immobilization ...
Abstract Background α-Amylase plays a pivotal role in a broad range of industrial processes. To meet increasing demands of biocatalytic tasks, considerable efforts have been made to isolate enzymes produced by extremophiles. However, the relevant data of α-amylases from cold-adapted fungi are still...
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ftdatacite:10.6084/m9.figshare.c.3705637 2024-04-28T07:58:40+00:00 Functional expression of a novel α-amylase from Antarctic psychrotolerant fungus for baking industry and its magnetic immobilization ... He, Lei Mao, Youzhi Zhang, Lujia Wang, Hualei Alias, Siti Gao, Bei Wei, Dongzhi 2017 https://dx.doi.org/10.6084/m9.figshare.c.3705637 https://springernature.figshare.com/collections/Functional_expression_of_a_novel_-amylase_from_Antarctic_psychrotolerant_fungus_for_baking_industry_and_its_magnetic_immobilization/3705637 unknown figshare Creative Commons Attribution 4.0 International https://creativecommons.org/licenses/by/4.0/legalcode cc-by-4.0 Biochemistry Space Science Medicine Biotechnology Chemical Sciences not elsewhere classified Ecology FOS Biological sciences Biological Sciences not elsewhere classified Inorganic Chemistry FOS Chemical sciences Collection article 2017 ftdatacite https://doi.org/10.6084/m9.figshare.c.3705637 2024-04-02T11:53:14Z Abstract Background α-Amylase plays a pivotal role in a broad range of industrial processes. To meet increasing demands of biocatalytic tasks, considerable efforts have been made to isolate enzymes produced by extremophiles. However, the relevant data of α-amylases from cold-adapted fungi are still insufficient. In addition, bread quality presents a particular interest due to its high consummation. Thus developing amylases to improve textural properties could combine health benefits with good sensory properties. Furthermore, iron oxide nanoparticles provide an economical and convenient method for separation of biomacromolecules. In order to maximize the catalytic efficiency of α-amylase and support further applications, a comprehensive characterization of magnetic immobilization of α-amylase is crucial and needed. Results A novel α-amylase (AmyA1) containing an open reading frame of 1482 bp was cloned from Antarctic psychrotolerant fungus G. pannorum and then expressed in the newly constructed Aspergillus ... Article in Journal/Newspaper Antarc* Antarctic DataCite Metadata Store (German National Library of Science and Technology) |
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Open Polar |
collection |
DataCite Metadata Store (German National Library of Science and Technology) |
op_collection_id |
ftdatacite |
language |
unknown |
topic |
Biochemistry Space Science Medicine Biotechnology Chemical Sciences not elsewhere classified Ecology FOS Biological sciences Biological Sciences not elsewhere classified Inorganic Chemistry FOS Chemical sciences |
spellingShingle |
Biochemistry Space Science Medicine Biotechnology Chemical Sciences not elsewhere classified Ecology FOS Biological sciences Biological Sciences not elsewhere classified Inorganic Chemistry FOS Chemical sciences He, Lei Mao, Youzhi Zhang, Lujia Wang, Hualei Alias, Siti Gao, Bei Wei, Dongzhi Functional expression of a novel α-amylase from Antarctic psychrotolerant fungus for baking industry and its magnetic immobilization ... |
topic_facet |
Biochemistry Space Science Medicine Biotechnology Chemical Sciences not elsewhere classified Ecology FOS Biological sciences Biological Sciences not elsewhere classified Inorganic Chemistry FOS Chemical sciences |
description |
Abstract Background α-Amylase plays a pivotal role in a broad range of industrial processes. To meet increasing demands of biocatalytic tasks, considerable efforts have been made to isolate enzymes produced by extremophiles. However, the relevant data of α-amylases from cold-adapted fungi are still insufficient. In addition, bread quality presents a particular interest due to its high consummation. Thus developing amylases to improve textural properties could combine health benefits with good sensory properties. Furthermore, iron oxide nanoparticles provide an economical and convenient method for separation of biomacromolecules. In order to maximize the catalytic efficiency of α-amylase and support further applications, a comprehensive characterization of magnetic immobilization of α-amylase is crucial and needed. Results A novel α-amylase (AmyA1) containing an open reading frame of 1482 bp was cloned from Antarctic psychrotolerant fungus G. pannorum and then expressed in the newly constructed Aspergillus ... |
format |
Article in Journal/Newspaper |
author |
He, Lei Mao, Youzhi Zhang, Lujia Wang, Hualei Alias, Siti Gao, Bei Wei, Dongzhi |
author_facet |
He, Lei Mao, Youzhi Zhang, Lujia Wang, Hualei Alias, Siti Gao, Bei Wei, Dongzhi |
author_sort |
He, Lei |
title |
Functional expression of a novel α-amylase from Antarctic psychrotolerant fungus for baking industry and its magnetic immobilization ... |
title_short |
Functional expression of a novel α-amylase from Antarctic psychrotolerant fungus for baking industry and its magnetic immobilization ... |
title_full |
Functional expression of a novel α-amylase from Antarctic psychrotolerant fungus for baking industry and its magnetic immobilization ... |
title_fullStr |
Functional expression of a novel α-amylase from Antarctic psychrotolerant fungus for baking industry and its magnetic immobilization ... |
title_full_unstemmed |
Functional expression of a novel α-amylase from Antarctic psychrotolerant fungus for baking industry and its magnetic immobilization ... |
title_sort |
functional expression of a novel α-amylase from antarctic psychrotolerant fungus for baking industry and its magnetic immobilization ... |
publisher |
figshare |
publishDate |
2017 |
url |
https://dx.doi.org/10.6084/m9.figshare.c.3705637 https://springernature.figshare.com/collections/Functional_expression_of_a_novel_-amylase_from_Antarctic_psychrotolerant_fungus_for_baking_industry_and_its_magnetic_immobilization/3705637 |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_rights |
Creative Commons Attribution 4.0 International https://creativecommons.org/licenses/by/4.0/legalcode cc-by-4.0 |
op_doi |
https://doi.org/10.6084/m9.figshare.c.3705637 |
_version_ |
1797570906168492032 |