ArticleThe protein journal2010
Cloning, expression, purification, and characterization of cold-adapted α-amylase from Pseudoalteromonas arctica GS230.
Article in The protein journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 54 citations in OpenAlex.
- Vertical Structure and Functional Diversity of Microbial Communities in the Ross Sea, Antarctica.Microbial ecology · 2025Article
- Multilocus sequence based identification and adaptational strategies of Pseudomonas sp. from the supraglacial site of Sikkim Himalaya.PloS one · 2022Article
- Secondary metabolite biosynthetic diversity in Arctic Ocean metagenomes.Microbial genomics · 2021Article
- A Novel Digestive α-Amylase from Blue Crab (International journal of molecular sciences · 2021Article
- Cloning, Expression and Characterization of a Novel α-Amylase from Salinispora arenicola CNP193.The protein journal · 2019Article
- AmyZ1: a novel α-amylase from marine bacteriumBiotechnology for biofuels · 2019Article
- Molecular cloning, expression, and biochemical characterization of a novel cold-active α-amylase from Bacillus sp. dsh19-1.Extremophiles : life under extreme conditions · 2018Article
- Molecular Cloning and Characterization of a NovelBioMed research international · 2018Article
- Functional expression of a novel α-amylase from Antarctic psychrotolerant fungus for baking industry and its magnetic immobilization.BMC biotechnology · 2017Article
- Review
- Expression and characterization of thermotolerant lipase with broad pH profiles isolated from an AntarcticPeerJ · 2016Article
- A novel cold-active and salt-tolerant α-amylase from marine bacterium Zunongwangia profunda: molecular cloning, heterologous expression and biochemical characterization.Extremophiles : life under extreme conditions · 2014Article
- Sequence and structural investigation of a novel psychrophilic α-amylase from Glaciozyma antarctica PI12 for cold-adaptation analysis.Journal of molecular modeling · 2013Article
- Cold-adapted RTX lipase from antarctic Pseudomonas sp. strain AMS8: isolation, molecular modeling and heterologous expression.The protein journal · 2013Article
- Molecular characterization of α-amylase from Staphylococcus aureus.Bioinformation · 2013Article
- Cold-adapted features of arginine kinase from the deep-sea clam Calyptogena kaikoi.Marine biotechnology (New York, N.Y.) · 2012Article
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6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A cold-adapted α-amylase (ParAmy) gene from Pseudoalteromonas arctica GS230 was cloned, sequenced, and expressed as an N-terminus His-tag fusion protein in E. coli. A recombinant protein was produced and purified with DEAE-sepherose ion exchange chromatography and Ni affinity chromatography. The molecular weight of ParAmy was estimated to be 55 KDa with sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). With an optimum temperature for activity 30 °C, ParAmy showed 34.5% of maximum activity at 0 °C and its activity decreased sharply at above 40 °C. ParAmy was stable in the range of pH 7-8.5 at 30 °C for 1 h. ParAmy was activated by Mn(2+), K(+) and Na(+), and inhibited by Hg(2+), Cu(2+), and Fe(3+). N-Bromosuccinimid showed a significant repressive effect on enzyme activity. The K (m) and V (max) values of the α-amylase for soluble starch were 7.28 mg/mL and 13.07 mg/mL min, respectively. This research suggests that Paramy has a good potential to be a cold-stable and alkalitolerant amylase in detergent industry.
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