Thermal stability of a neutral protease of Aspergillus oryzae

BOMBARARA N; A. PILOSOF; AÑÓN MC

JOURNAL OF FOOD BIOCHEMISTRY

WILEY-BLACKWELL PUBLISHING, INC

Lugar: Londres; Año: 1994 vol. 18 p. 31 - 41

0145-8884

The thermal stability of the neutral protease of Aspergillus oryzae was measuredby diflerential scanning calorimetry. me activation energy, preexponential factorand the reaction rate constant calculated by means of the dynamic methodare similar to those obtained for denaturation of other proteins. Hay life (tm)calcuiated by using the above-mentioned parameters permitted estimation of theamount of native enzyme remaining afrer different thermal treatments. Completedenaturation occurred above 6OC. The presence of substrate stabilizes the enzyme.The behavior offlour samples treated with the neutral protease was studiedas well. A tendency to shifr towards higher temperatures whenflour was treatedwith the enzyme was observed for both the Tp (DSCpeak maximum temperature)corresponding to gelatinization of starch and the dissociation of the amylose-lipidcomplex.