Modeling Tool for Studying the Influence of Operating Conditions on the Enzymatic Hydrolysis of Milk Proteins
Systematic modeling of the enzymatic hydrolysis of milk proteins is needed to assist the study and production of partially hydrolyzed milk. The enzymatic hydrolysis of milk proteins was characterized and evaluated as a function of the temperature and protease concentration using Alcalase, Neutrase a...
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| Format: | Article |
| Language: | English |
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MDPI AG
2022-12-01
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| Series: | Foods |
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| Online Access: | https://www.mdpi.com/2304-8158/11/24/4080 |
| _version_ | 1797458631532216320 |
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| author | Pedro Valencia Karen Espinoza Carolina Astudillo-Castro Fernando Salazar |
| author_facet | Pedro Valencia Karen Espinoza Carolina Astudillo-Castro Fernando Salazar |
| author_sort | Pedro Valencia |
| collection | DOAJ |
| description | Systematic modeling of the enzymatic hydrolysis of milk proteins is needed to assist the study and production of partially hydrolyzed milk. The enzymatic hydrolysis of milk proteins was characterized and evaluated as a function of the temperature and protease concentration using Alcalase, Neutrase and Protamex. Modeling was based on the combination of two empirical models formed by a logarithmic and a polynomial equation to correlate the kinetic constants and the operating conditions. The logarithmic equation fitted with high accuracy to the experimental hydrolysis curves with the three proteases (<i>R</i><sup>2</sup> > 0.99). The kinetic constants were correlated with the operating conditions (<i>R</i><sup>2</sup> > 0.97) using polynomial equations. The temperature and protease concentration significantly affected the initial rate of hydrolysis, i.e., the kinetic constant <i>a</i>, while the kinetic constant <i>b</i> was not significantly affected. The values for the kinetic constant <i>a</i> were predicted according to the operating conditions and they were strongly correlated with the experimental data (<i>R</i><sup>2</sup> = 0.95). The model allowed for a high-quality prediction of the hydrolysis curves of milk proteins. This modeling tool can be used in future research to test the correlation between the degree of hydrolysis and the functional properties of milk hydrolysates. |
| first_indexed | 2024-03-09T16:40:55Z |
| format | Article |
| id | doaj.art-3887c940a13f4fc684782f415ed65652 |
| institution | Directory Open Access Journal |
| issn | 2304-8158 |
| language | English |
| last_indexed | 2024-03-09T16:40:55Z |
| publishDate | 2022-12-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Foods |
| spelling | doaj.art-3887c940a13f4fc684782f415ed656522023-11-24T14:52:06ZengMDPI AGFoods2304-81582022-12-011124408010.3390/foods11244080Modeling Tool for Studying the Influence of Operating Conditions on the Enzymatic Hydrolysis of Milk ProteinsPedro Valencia0Karen Espinoza1Carolina Astudillo-Castro2Fernando Salazar3Department of Chemical and Environmental Engineering, Universidad Técnica Federico Santa María, Avenida España 1680, Valparaíso 2390123, ChileDepartment of Chemical and Environmental Engineering, Universidad Técnica Federico Santa María, Avenida España 1680, Valparaíso 2390123, ChileSchool of Food Engineering, Pontificia Universidad Católica de Valparaíso, Waddington 716, Valparaíso 2360100, ChileSchool of Food Engineering, Pontificia Universidad Católica de Valparaíso, Waddington 716, Valparaíso 2360100, ChileSystematic modeling of the enzymatic hydrolysis of milk proteins is needed to assist the study and production of partially hydrolyzed milk. The enzymatic hydrolysis of milk proteins was characterized and evaluated as a function of the temperature and protease concentration using Alcalase, Neutrase and Protamex. Modeling was based on the combination of two empirical models formed by a logarithmic and a polynomial equation to correlate the kinetic constants and the operating conditions. The logarithmic equation fitted with high accuracy to the experimental hydrolysis curves with the three proteases (<i>R</i><sup>2</sup> > 0.99). The kinetic constants were correlated with the operating conditions (<i>R</i><sup>2</sup> > 0.97) using polynomial equations. The temperature and protease concentration significantly affected the initial rate of hydrolysis, i.e., the kinetic constant <i>a</i>, while the kinetic constant <i>b</i> was not significantly affected. The values for the kinetic constant <i>a</i> were predicted according to the operating conditions and they were strongly correlated with the experimental data (<i>R</i><sup>2</sup> = 0.95). The model allowed for a high-quality prediction of the hydrolysis curves of milk proteins. This modeling tool can be used in future research to test the correlation between the degree of hydrolysis and the functional properties of milk hydrolysates.https://www.mdpi.com/2304-8158/11/24/4080milk proteinprotein hydrolysisenzymatic hydrolysismathematical modeling |
| spellingShingle | Pedro Valencia Karen Espinoza Carolina Astudillo-Castro Fernando Salazar Modeling Tool for Studying the Influence of Operating Conditions on the Enzymatic Hydrolysis of Milk Proteins Foods milk protein protein hydrolysis enzymatic hydrolysis mathematical modeling |
| title | Modeling Tool for Studying the Influence of Operating Conditions on the Enzymatic Hydrolysis of Milk Proteins |
| title_full | Modeling Tool for Studying the Influence of Operating Conditions on the Enzymatic Hydrolysis of Milk Proteins |
| title_fullStr | Modeling Tool for Studying the Influence of Operating Conditions on the Enzymatic Hydrolysis of Milk Proteins |
| title_full_unstemmed | Modeling Tool for Studying the Influence of Operating Conditions on the Enzymatic Hydrolysis of Milk Proteins |
| title_short | Modeling Tool for Studying the Influence of Operating Conditions on the Enzymatic Hydrolysis of Milk Proteins |
| title_sort | modeling tool for studying the influence of operating conditions on the enzymatic hydrolysis of milk proteins |
| topic | milk protein protein hydrolysis enzymatic hydrolysis mathematical modeling |
| url | https://www.mdpi.com/2304-8158/11/24/4080 |
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