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High pressure, thermal, and combined pressure–temperature stabilities of α‐amylases from Bacillus species
Author(s) -
Weemaes C.,
de Cordt S.,
Goossens K.,
Ludikhuyze L.,
Hendrickx M.,
Heremans K.,
Tobback P.
Publication year - 1996
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/(sici)1097-0290(19960405)50:1<49::aid-bit6>3.0.co;2-1
Subject(s) - thermostability , bacillus amyloliquefaciens , bacillus licheniformis , amylase , thermal stability , chemistry , enzyme , bacillus subtilis , biochemistry , biology , organic chemistry , fermentation , bacteria , genetics
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.