Molecular Cloning and Characterization of a Novel α-Amylase from Antarctic Sea Ice Bacterium Pseudoalteromonas sp. M175 and Its Primary Application in Detergent
Joint Authors
Wang, Xiaofei
Kan, Guangfeng
Ren, Xiulian
Yu, Geng
Shi, Cuijuan
Xie, Qiuju
Wen, Hua
Betenbaugh, Michael
Source
Issue
Vol. 2018, Issue 2018 (31 Dec. 2018), pp.1-16, 16 p.
Publisher
Hindawi Publishing Corporation
Publication Date
2018-06-27
Country of Publication
Egypt
No. of Pages
16
Main Subjects
Abstract EN
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.
American Psychological Association (APA)
Wang, Xiaofei& Kan, Guangfeng& Ren, Xiulian& Yu, Geng& Shi, Cuijuan& Xie, Qiuju…[et al.]. 2018. Molecular Cloning and Characterization of a Novel α-Amylase from Antarctic Sea Ice Bacterium Pseudoalteromonas sp. M175 and Its Primary Application in Detergent. BioMed Research International،Vol. 2018, no. 2018, pp.1-16.
https://search.emarefa.net/detail/BIM-1125743
Modern Language Association (MLA)
Wang, Xiaofei…[et al.]. Molecular Cloning and Characterization of a Novel α-Amylase from Antarctic Sea Ice Bacterium Pseudoalteromonas sp. M175 and Its Primary Application in Detergent. BioMed Research International No. 2018 (2018), pp.1-16.
https://search.emarefa.net/detail/BIM-1125743
American Medical Association (AMA)
Wang, Xiaofei& Kan, Guangfeng& Ren, Xiulian& Yu, Geng& Shi, Cuijuan& Xie, Qiuju…[et al.]. Molecular Cloning and Characterization of a Novel α-Amylase from Antarctic Sea Ice Bacterium Pseudoalteromonas sp. M175 and Its Primary Application in Detergent. BioMed Research International. 2018. Vol. 2018, no. 2018, pp.1-16.
https://search.emarefa.net/detail/BIM-1125743
Data Type
Journal Articles
Language
English
Notes
Includes bibliographical references
Record ID
BIM-1125743