Abstract

 

Intrinsic halotolerance of the psychrophilic a -amylase from Pseudoalteromonas haloplanktis.

Srimathi, S.; Jayaraman, G.; Feller, G.; Danielsson, B.; Narayanan, P.R.

Extremophiles; 2007; 11; 505-515.

Abstract: The halotolerance of a cold adapted a -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 ) a -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 o C positive shift in the temperature optimum, a stabilization factor of >5 for thermal inactivation and a D T m of 8.3 o 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 a -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.

Keywords: Acidic protein - Pseudoalteromonas haloplanktis a - amylase Halophilic Halotolerance Psychrophilic Stability

 

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