Stability kinetic study for amylase and protease enzymes under food stain removal conditions
•Amylase and protease stability model is developed under food stain removal conditions.•The kinetic deactivation mechanisms are indentified based on a response surface methodology.•A kinetic dissolution model was added for spherical enzyme particles.•Validation of each stability model is done by exp...
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Published in | Chemical engineering science Vol. 287; p. 119767 |
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Main Authors | , , , , , |
Format | Journal Article |
Language | English |
Published |
Elsevier Ltd
05.04.2024
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Subjects | |
Online Access | Get full text |
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Summary: | •Amylase and protease stability model is developed under food stain removal conditions.•The kinetic deactivation mechanisms are indentified based on a response surface methodology.•A kinetic dissolution model was added for spherical enzyme particles.•Validation of each stability model is done by experimental data.
A mechanistic model to evaluate the stability of amylase and protease under food stain removal conditions has been developed. The mechanism was determined identifying the significant factors for each enzyme based on response surface methodology. The amylase stability was jeopardized by the deprotonated peracid-based bleach, the interaction pH–temperature, and the protonated peroxide-based bleach promoted by manganese-based bleaching catalyst. The stability of the protease decreased in presence of protonated peracid-based bleach, acid-base equilibria species from peroxide-based bleach as well as temperature and pH. This work integrates the main mechanisms based on non-linear differential equations for each enzyme. In addition, a kinetic dissolution model was included for the enzymatic spherical particles. The models were validated, obtaining a determination coefficient of 0.84 and 0.90 for amylase and protease respectively for the training data set. For the validation set, a determination coefficient of 0.91 and 0.90 were obtained for amylase and protease, respectively. |
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ISSN: | 0009-2509 1873-4405 |
DOI: | 10.1016/j.ces.2024.119767 |