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High pressure, thermal, and combined pressure–temperature stabilities of α-amylases from Bacillus species

✍ Scribed by C. Weemaes; S. de Cordt; K. Goossens; L. Ludikhuyze; M. Hendrickx; K. Heremans; P. Tobback

Publisher
John Wiley and Sons
Year
1996
Tongue
English
Weight
782 KB
Volume
50
Category
Article
ISSN
0006-3592

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✦ Synopsis

Three different a-amylases from Bacillus subtilis, B. amyloliquefaciens, and B. licheniformis, were mutually compared with respect to thermal stability, pressure stability, and combined pressure-temperature stability. Measurements of residual enzyme activity and residual denaturation enthalpy showed that the a-amylase from B. licheniformis has by far the highest thermostability and that the two other a-amylases have thermostabilities of the same order of magnitude. FTlR spectroscopy showed that changes in the conformation of the a-amylases from B. amyloliquefaciens, B. subtilis, and B. licheniformis due to pressure occurred at about 6.5,7.5, and 11 kbar, respectively. It seemed that, for the enzymes studied, thermal stability was correlated with pressure stability. As to the resistance under combined heat and high pressure, the a-amylase from B. licheniformis was much more stable than the a-amylases from B. amyloliquefaciens and B. subtilis, the latter two being about equally stable. It appears that under high pressure and/or temperature, B. licheniformis a-amylase is the most resistant among the three enzymes studied. 0 1996

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