Kinetics of wheat proteins solubilization with a fungal protease
The kinetics of wheat protein solubilization with a fungal protease as a function of hydrolysis parameters was studied. High correlations were obtained when a modified Foster-Nieman equation, which accounts for product inhibition, was applied to the experimental kinetic data. A good correlation was...
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todo:paper_00236438_v25_n6_p527_Bombara2023-10-03T14:33:56Z Kinetics of wheat proteins solubilization with a fungal protease Bombara, N. Pilosof, A.M.R. Añón, M.C. The kinetics of wheat protein solubilization with a fungal protease as a function of hydrolysis parameters was studied. High correlations were obtained when a modified Foster-Nieman equation, which accounts for product inhibition, was applied to the experimental kinetic data. A good correlation was also achieved between the first order rate constant (k1) and the lumped (h) constant from the Foster-Nieman model. Both constants can be used to describe the effect of enzyme concentration and temperature. The activation energies calculated from h and k1 by applying the Arrhenius equation law were 58.8-71.4 kJ/mol. Protein solubilization was proportional to the degree of hydrolysis. Maximum protein solubilization under the conditions of this work was around 80% and molecular weight of soluble peptides was 13,000 or less. © 1992. 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_00236438_v25_n6_p527_Bombara |
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Universidad de Buenos Aires |
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I-28 |
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R-134 |
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Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| description |
The kinetics of wheat protein solubilization with a fungal protease as a function of hydrolysis parameters was studied. High correlations were obtained when a modified Foster-Nieman equation, which accounts for product inhibition, was applied to the experimental kinetic data. A good correlation was also achieved between the first order rate constant (k1) and the lumped (h) constant from the Foster-Nieman model. Both constants can be used to describe the effect of enzyme concentration and temperature. The activation energies calculated from h and k1 by applying the Arrhenius equation law were 58.8-71.4 kJ/mol. Protein solubilization was proportional to the degree of hydrolysis. Maximum protein solubilization under the conditions of this work was around 80% and molecular weight of soluble peptides was 13,000 or less. © 1992. |
| format |
JOUR |
| author |
Bombara, N. Pilosof, A.M.R. Añón, M.C. |
| spellingShingle |
Bombara, N. Pilosof, A.M.R. Añón, M.C. Kinetics of wheat proteins solubilization with a fungal protease |
| author_facet |
Bombara, N. Pilosof, A.M.R. Añón, M.C. |
| author_sort |
Bombara, N. |
| title |
Kinetics of wheat proteins solubilization with a fungal protease |
| title_short |
Kinetics of wheat proteins solubilization with a fungal protease |
| title_full |
Kinetics of wheat proteins solubilization with a fungal protease |
| title_fullStr |
Kinetics of wheat proteins solubilization with a fungal protease |
| title_full_unstemmed |
Kinetics of wheat proteins solubilization with a fungal protease |
| title_sort |
kinetics of wheat proteins solubilization with a fungal protease |
| url |
http://hdl.handle.net/20.500.12110/paper_00236438_v25_n6_p527_Bombara |
| work_keys_str_mv |
AT bombaran kineticsofwheatproteinssolubilizationwithafungalprotease AT pilosofamr kineticsofwheatproteinssolubilizationwithafungalprotease AT anonmc kineticsofwheatproteinssolubilizationwithafungalprotease |
| _version_ |
1807314466562375680 |