ArticleMarine biotechnology (New York, N.Y.)
Purification and characterization of a cold-adapted alpha-amylase produced by Nocardiopsis sp. 7326 isolated from Prydz Bay, Antarctic.
Article in Marine biotechnology (New York, N.Y.). The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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20 citing papers in PubMed.
- A CALB-like Cold-Active Lipolytic Enzyme fromMarine drugs · 2025Article
- Kinetics of growth and co-production of amylase and protease in novel marine actinomycete, Streptomyces lopnurensis KaM5.Folia microbiologica · 2021Article
- Biochemical and synergistic properties of a novel alpha-amylase from Chinese nong-flavor Daqu.Microbial cell factories · 2021Article
- A Novel Digestive α-Amylase from Blue Crab (International journal of molecular sciences · 2021Article
- Characterization of earthworm α-amylases for dietary supplement development and biomass utilization.Environmental science and pollution research international · 2020Article
- 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
- Rational Engineering of a Cold-Adapted α-Amylase from the Antarctic Ciliate Euplotes focardii for Simultaneous Improvement of Thermostability and Catalytic Activity.Applied and environmental microbiology · 2017Article
- Review
- Degradation properties of various macromolecules of cultivable psychrophilic bacteria from the deep-sea water of the South Pacific Gyre.Extremophiles : life under extreme conditions · 2016Article
- Integrated (Meta) Genomic and Synthetic Biology Approaches to Develop New Biocatalysts.Marine drugs · 2016Review
- 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
- Partial Purification and Characterization of a Heat Stable α-Amylase from a Thermophilic Actinobacteria, Streptomyces sp. MSC702.Enzyme research · 2014Article
- Sequence and structural investigation of a novel psychrophilic α-amylase from Glaciozyma antarctica PI12 for cold-adaptation analysis.Journal of molecular modeling · 2013Article
- Identification and phylogenetic characterization of a new subfamily of α-amylase enzymes from marine microorganisms.Marine biotechnology (New York, N.Y.) · 2012Article
- Production of cold-adapted amylase by marine bacterium Wangia sp. C52: optimization, modeling, and partial characterization.Marine biotechnology (New York, N.Y.) · 2011Article
- Cloning, expression, purification, and characterization of cold-adapted α-amylase from Pseudoalteromonas arctica GS230.The protein journal · 2010Article
- Genomics of deep-sea and sub-seafloor microbes.Microbial biotechnology · 2009Article
- Marine metagenomics: strategies for the discovery of novel enzymes with biotechnological applications from marine environments.Microbial cell factories · 2008Article
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Abstract
An actinomycete strain 7326 producing cold-adapted alpha-amylase was isolated from the deep sea sediment of Prydz Bay, Antarctic. It was identified as Nocardiopsis based on morphology, 16S rRNA gene sequence analysis, and physiological and biochemical characteristics. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis and zymogram activity staining of purified amylase showed a single band equal to a molecular mass of about 55 kDa. The optimal activity temperature of Nocardiopsis sp. 7326 amylase was 35 degrees C, and the activity decreased dramatically at temperatures above 45 degrees C. The enzyme was stable between pH 5 and 10, and exhibited a maximal activity at pH 8.0. Ca(2+), Mn(2+), Mg(2+), Cu(2+), and Co(2+) stimulated the activity of the enzyme significantly, and Rb(2+), Hg(2+), and EDTA inhibited the activity. The hydrolysates of soluble starch by the enzyme were mainly glucose, maltose, and maltotriose. This is the first report on the isolation and characterization of cold-adapted amylase from Nocardiopsis sp.
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