Studies on the thermostability of the α-amylase of Bacillus caldovelox

Springer Science and Business Media LLC - 1991
Francis Bealin-Kelly1, Catherine T. Kelly1, William M. Fogarty1
1Department of Industrial Microbiology, University College Dublin, Dublin 4, Ireland

Tóm tắt

Molecular mechanisms of thermoinactivation of the thermostable α-amylase of Bacillus caldovelox were examined. Monomolecular conformational processes were found to be the major causes of thermoinactivation at both pH 4.5 and 8.0. The enzyme possessed considerable additional thermostability at pH 8.0, with half-lives of 0.75 and 7.0 min at 90° C and pH 4.5 and 8.0, respectively. The amino acid composition was examined with respect to the underlying thermostability exhibited by this enzyme. The inherent thermostability exhibited may be due to the high proline content (4.47 mol%), but more likely due to the high content of residues forming hydrophobic bonds (60.89 mol%) allied to a low content of residues responsible for ionic interactions (28.34 mol%).

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