ISSN:
0006-3592
Keywords:
Bacillus amyloliquefaciens α-amylase
;
Bacillus licheniformis α-amylase
;
Bacillus subtilis α-amylase
;
thermostability and pressure stability
;
Chemistry
;
Biochemistry and Biotechnology
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Biology
,
Process Engineering, Biotechnology, Nutrition Technology
Notes:
Three different α-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 α-amylase from B. licheniformis has by far the highest thermostability and that the two other α-amylases have thermostabilities of the same order of magnitude. FTIR spectroscopy showed that changes in the conformation of the α-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 α-amylase from B. licheniformis was much more stable than the α-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 α-amylase is the most resistant among the three enzymes studied. © 1996 John Wiley & Sons, Inc.
Additional Material:
5 Ill.
Type of Medium:
Electronic Resource
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