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Intrinsic halotolerance of the psychrophilic alpha-amylase from Pseudoalteromonas haloplanktis
Srimathi, S.; Jayaraman, G.; Feller, G.; Danielsson, B.; Narayanan, P.R. (2007). Intrinsic halotolerance of the psychrophilic alpha-amylase from Pseudoalteromonas haloplanktis. Extremophiles 11(3): 505-515. https://dx.doi.org/10.1007/s00792-007-0062-5
In: Extremophiles. Springer: Tokyo. ISSN 1431-0651; e-ISSN 1433-4909, meer
Peer reviewed article  
Beschikbaar in  Auteurs 
Trefwoorden
    Pseudoalteromonas haloplanktis (ZoBell & Upham, 1944) Gauthier, Gauthier & Christen, 1995 [WoRMS]
    Marien/Kust
Author keywords
    acidic protein; Pseudoalteromonas haloplanktis alpha-amylase;halophilic; halotolerance; psychrophilic; stability
Auteurs  Top 
  • Srimathi, S.
  • Jayaraman, G.
  • Feller, G., meer
  • Danielsson, B.
  • Narayanan, P.R.
Abstract
    The halotolerance of a cold adapted α-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) α-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°C positive shift in the temperature optimum, a stabilization factor of >5 for thermal inactivation and a ΔTm of 8.3°C for the secondary structure melting were estimated in 2.7 M NaCl. The higher activation energy, half-life time and Tm indicated reduced conformational dynamics and increased rigidity in the presence of higher NaCl concentrations. A comparison with the sequences of other halophilic α-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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