Stability and structural analysis of α‐amylase from the antarctic psychrophile Alteromonas haloplanctis A23

• Published in: European Journal of Biochemistry Vol. 222; no. 2; pp. 441 - 447
• Main Authors: FELLER, Georges, PAYAN, Françoise, THEYS, Fabienne, QIAN, Minxie, HASER, Richard, GERDAY, Charles
• Format: Journal Article Web Resource
• Language: English
• Published: Oxford, UK Blackwell Publishing Ltd 01.06.1994; Wiley; Blackwell
• Subjects: alpha-Amylases - chemistry; alpha-Amylases - isolation & purification; alpha-Amylases - metabolism; Alteromonas haloplanctis; Amino Acid Sequence; Animals; Antarctic Regions; Biochemistry, biophysics & molecular biology; Biochemistry, Molecular Biology; Biochimie, biophysique & biologie moléculaire; Enzyme Stability; Gram-Negative Aerobic Bacteria - enzymology; Guanidine; Guanidines; Kinetics; Life Sciences; Molecular Sequence Data; Pancreas - enzymology; Protein Conformation; Protein Denaturation; Protein Folding; Protein Structure, Secondary; Sciences du vivant; Sequence Homology, Amino Acid; Swine; Thermodynamics; Urea; Antarctic Regions

The α‐amylase secreted by the antarctic bacterium Alteromonas haloplanctis displays 66% amino acid sequence similarity with porcine pancreatic α‐amylase. The psychrophilic α‐amylase is however characterized by a sevenfold higher kcat and kcat/Km values at 4°C and a lower conformational stability est...