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Título
Stability kinetic study for amylase and protease enzymes under food stain removal conditions
Autor(es)
Palabras clave
Amylase
Protease
Stability
Response surface methodology
Mechanistic model
Food stain removal
Clasificación UNESCO
3303 Ingeniería y Tecnología Químicas
Fecha de publicación
2024
Editor
Elsevier
Citación
José E. Roldán-San Antonio, Carlos Amador, Mariano Martín, Kevin Blyth, Vania Cristina Croce Mago, Joe Bowman, Stability kinetic study for amylase and protease enzymes under food stain removal conditions, Chemical Engineering Science, Volume 287, 2024, 119767, ISSN 0009-2509, https://doi.org/10.1016/j.ces.2024.119767. (https://www.sciencedirect.com/science/article/pii/S0009250924000678)
Resumen
[EN] 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.
URI
ISSN
0009-2509
DOI
10.1016/j.ces.2024.119767
Versión del editor
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- PSEM3. Artículos [54]












