ArticleExtremophiles : life under extreme conditions2007
Intrinsic halotolerance of the psychrophilic alpha-amylase from Pseudoalteromonas haloplanktis.
Article in Extremophiles : life under extreme conditions, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 50 citations in OpenAlex.
- Enzyme Technology in the Food Industry: Molecular Mechanisms, Applications, and Sustainable Innovations.Food science & nutrition · 2025Review
- Extremophilic Microorganisms as a Source of Emerging Enzymes for the Food Industry: A Review.Food science & nutrition · 2025Review
- Genomic signatures of cold adaptation in the family Colwelliaceae.Extremophiles : life under extreme conditions · 2024Article
- Article
- ThermoSlope: A Software for Determining Thermodynamic Parameters from Single Steady-State Experiments.Molecules (Basel, Switzerland) · 2021Article
- Biotechnological potential of psychrophilic microorganisms as the source of cold-active enzymes in food processing applications.3 Biotech · 2021Review
- Carbohydrate-Binding Module and Linker Allow Cold Adaptation and Salt Tolerance of Maltopentaose-Forming Amylase From Marine BacteriumFrontiers in microbiology · 2021Article
- Novel Psychrophiles and Exopolymers from Permafrost Thaw Lake Sediments.Microorganisms · 2020Article
- Harnessing Marine Biocatalytic Reservoirs for Green Chemistry Applications through Metagenomic Technologies.Marine drugs · 2018Review
- Expression and characterization of a new heat-stable endo-type alginate lyase from deep-sea bacterium Flammeovirga sp. NJ-04.Extremophiles : life under extreme conditions · 2017Article
- Microbial Diversity in Extreme Marine Habitats and Their Biomolecules.Microorganisms · 2017Review
- Molecular cloning and characterization of a halotolerant α-amylase from marine metagenomic library derived from Arabian Sea sediments.3 Biotech · 2017Article
- Review
- 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
- Amino acid substitutions in cold-adapted proteins from Halorubrum lacusprofundi, an extremely halophilic microbe from antarctica.PloS one · 2013Article
- Properties of the endogenous components of the thioredoxin system in the psychrophilic eubacterium Pseudoalteromonas haloplanktis TAC 125.Extremophiles : life under extreme conditions · 2012Article
- Function and biotechnology of extremophilic enzymes in low water activity.Aquatic biosystems · 2012Article
- Biotechnological uses of enzymes from psychrophiles.Microbial biotechnology · 2011Review
- Cytoplasmic and periplasmic proteomic signatures of exponentially growing cells of the psychrophilic bacterium Pseudoalteromonas haloplanktis TAC125.Applied and environmental microbiology · 2011Article
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Authors and funding
5 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The halotolerance of a cold adapted alpha-amylase from the psychrophilic bacterium Pseudoalteromonas haloplanktis (AHA) was investigated. AHA exhibited hydrolytic activity over a broad range of NaCl concentrations (0.01-4.5 M). AHA showed 28% increased activity in 0.5-2.0 M NaCl compared to that in 0.01 M NaCl. In contrast, the corresponding mesophilic (Bacillus amyloliquefaciens) and thermostable (B. licheniformis) alpha-amylases showed a 39 and 46% decrease in activity respectively. Even at 4.5 M NaCl, 80% of the initial activity was detected for AHA, whereas the mesophilic and thermostable enzymes were inactive. Besides an unaltered fluorescence emission and secondary structure, a 10 degrees C positive shift in the temperature optimum, a stabilization factor of >5 for thermal inactivation and a Delta T(m) of 8.3 degrees C for the secondary structure melting were estimated in 2.7 M NaCl. The higher activation energy, half-life time and T(m) indicated reduced conformational dynamics and increased rigidity in the presence of higher NaCl concentrations. A comparison with the sequences of other halophilic alpha-amylases revealed that AHA also contains higher proportion of small hydrophobic residues and acidic residues resulting in a higher negative surface potential. Thus, with some compromise in cold activity, psychrophilic adaptation has also manifested halotolerance to AHA that is comparable to the halophilic enzymes.
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