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: BOMBARA, N., PILOSOF, A.M.R., AÑÓN, M.C.
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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spelling todo:paper_01458884_v18_n1_p31_BOMBARA2023-10-03T15:00:10Z THERMAL STABILITY OF A NEUTRAL PROTEASE OF ASPERGILLUS ORYZAE BOMBARA, N. PILOSOF, A.M.R. AÑÓN, M.C. 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 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 Fil:PILOSOF, A.M.R. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_01458884_v18_n1_p31_BOMBARA
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic Aspergillus oryzae
spellingShingle Aspergillus oryzae
BOMBARA, N.
PILOSOF, A.M.R.
AÑÓN, M.C.
THERMAL STABILITY OF A NEUTRAL PROTEASE OF ASPERGILLUS ORYZAE
topic_facet Aspergillus oryzae
description 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
format JOUR
author BOMBARA, N.
PILOSOF, A.M.R.
AÑÓN, M.C.
author_facet BOMBARA, N.
PILOSOF, A.M.R.
AÑÓN, M.C.
author_sort BOMBARA, N.
title THERMAL STABILITY OF A NEUTRAL PROTEASE OF ASPERGILLUS ORYZAE
title_short THERMAL STABILITY OF A NEUTRAL PROTEASE OF ASPERGILLUS ORYZAE
title_full THERMAL STABILITY OF A NEUTRAL PROTEASE OF ASPERGILLUS ORYZAE
title_fullStr THERMAL STABILITY OF A NEUTRAL PROTEASE OF ASPERGILLUS ORYZAE
title_full_unstemmed THERMAL STABILITY OF A NEUTRAL PROTEASE OF ASPERGILLUS ORYZAE
title_sort thermal stability of a neutral protease of aspergillus oryzae
url http://hdl.handle.net/20.500.12110/paper_01458884_v18_n1_p31_BOMBARA
work_keys_str_mv AT bombaran thermalstabilityofaneutralproteaseofaspergillusoryzae
AT pilosofamr thermalstabilityofaneutralproteaseofaspergillusoryzae
AT anonmc thermalstabilityofaneutralproteaseofaspergillusoryzae
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