Reference : Intrinsic halotolerance of the psychrophilic alpha-amylase from Pseudoalteromonas halopl...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/14549
Intrinsic halotolerance of the psychrophilic alpha-amylase from Pseudoalteromonas haloplanktis
English
Srimathi, S. [> > > >]
Jayaraman, G. [> > > >]
Feller, Georges mailto [Université de Liège - ULg > Département des sciences de la vie > Labo de biochimie >]
Danielsson, B. [> > > >]
Narayanan, P. R. [> > > >]
May-2007
Extremophiles : Life Under Extreme Conditions
11
3
505-515
Yes (verified by ORBi)
International
1431-0651
[en] acidic protein ; Pseudoalteromonas haloplanktis alpha-amylase ; halophilic ; halotolerance ; psychrophilic ; stability
[en] 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.
http://hdl.handle.net/2268/14549

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