THERMAL STABILITY OF A NEUTRAL PROTEASE OF ASPERGILLUS ORYZAE
The thermal stability of the neutral protease of Aspergillus oryzae was measured by differential scanning calorimetry. The activation energy, preexponential factor and the reaction rate constant calculated by means of the dynamic method are similar to those obtained for denaturation of other protein...
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| Autores principales: | , , |
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| Formato: | JOUR |
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| Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_01458884_v18_n1_p31_BOMBARA |
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| Sumario: | The thermal stability of the neutral protease of Aspergillus oryzae was measured by differential scanning calorimetry. The activation energy, preexponential factor and the reaction rate constant calculated by means of the dynamic method are similar to those obtained for denaturation of other proteins. Half life (t1/2) calculated by using the above‐mentioned parameters permitted estimation of the amount of native enzyme remaining after different thermal treatments. Complete denaturation occurred above 60C. The presence of substrate stabilizes the enzyme. The behavior of flour samples treated with the neutral protease was studied as well. A tendency to shift towards higher temperatures when flour was treated with the enzyme was observed for both the Tp (DSC peak maximum temperature) corresponding to gelatinization of starch and the dissociation of the amylose‐lipid complex. Copyright © 1994, Wiley Blackwell. All rights reserved |
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