Physical-mathematical model to predict the kinetic coagulation process by clotting activity of bacterial endopeptidases

dc.creatorMancilla Canales, Manuel Arturo
dc.creatorFolmer Côrrea, Ana Paula
dc.creatorRiquelme, Bibiana Doris
dc.creatorBrandelli, Adriano
dc.creatorRisso, Patricia Hilda
dc.date2022-12-01T16:30:01Z
dc.date2022-12-01T16:30:01Z
dc.date2022-08
dc.date2022-12-01T16:30:01Z
dc.date2022-12-01T16:30:01Z
dc.date2022-08
dc.date.accessioned2023-08-30T21:17:19Z
dc.date.available2023-08-30T21:17:19Z
dc.identifier2379-6367
dc.identifierhttp://hdl.handle.net/2133/24936
dc.identifierhttp://hdl.handle.net/2133/24936
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/8541861
dc.descriptionA physical-mathematical model was used to evaluate the capability of an enzymatic pool of Bacillus sp. P7 (isolated from Piaractus mesopotamicus) to promote the bovine casein micelles coagulation. Experiments were designed to assess the effects of temperature, pH, and enzyme activity/mass of substrate ratio on the kinetic parameters of the coagulation process and the microstructure of the obtained clots. Descriptive and predictive equations indicate that the temperature and the pH modified these parameters significantly. In optimal conditions, the clot’s mean pore size was 3.6 times smaller using chymosin. On the other hand, rheological measurements evidence a moderate elasticity of clot, which indicates the usefulness of P7 protease preparation as a clotting agent in spreadable or soft cheese manufacture. Also, the hydrolysis products, which are in the whey after casein micelles coagulation, demonstrated antioxidant activities. Equations to model and predict the process kinetics were combined with rheological and microstructure analyses of the obtained clots, and whey bioactivities were evaluated. Nevertheless, the use of P7PP requires further investigation concerning the stability of the enzyme preparation during storage, its performance, and how these variables could be related to the proposed models.
dc.descriptionFil: Mancilla Canales, Manuel Arturo. Grupo de Física Biomédica. Instituto de Física Rosario (CONICET-UNR); Argentina.
dc.descriptionFil: Riquelme, Bibiana Doris. Grupo de Física Biomédica. Instituto de Física Rosario (CONICET-UNR); Argentina.
dc.descriptionFil: Mancilla Canales, Manuel Arturo. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas; Argentina.
dc.descriptionFil: Riquelme, Bibiana Doris. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas; Argentina.
dc.descriptionFil: Risso, Patricia Hilda. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas; Argentina.
dc.descriptionFil: Folmer Côrrea, Ana Paula. Universidade Federal de Rio Grande do Sul. Instituto de Ciência e Tecnologia de Alimentos; Brasil.
dc.descriptionFil: Brandelli, Adriano. Universidade Federal de Rio Grande do Sul. Instituto de Ciência e Tecnologia de Alimentos; Brasil.
dc.descriptionFil: Risso, Patricia Hilda. Universidad Nacional de Rosario. Facultad de Ciencias Veterinarias; Argentina.
dc.formatapplication/pdf
dc.languageeng
dc.publisherMedCrave
dc.relationhttps://medcraveonline.com/PPIJ/PPIJ-10-00375.pdf
dc.relationhttps://doi.org/10.15406/ppij.2022.10.00375
dc.rightshttps://creativecommons.org/licenses/by-nc/4.0/
dc.rightsMancilla Canales, Manuel Arturo
dc.rightsFolmer Côrrea, Ana Paula
dc.rightsRiquelme, Bibiana Doris
dc.rightsBrandelli, Adriano
dc.rightsRisso, Patricia Hilda
dc.rightsAtribución-NoComercial 4.0 Internacional (CC BY-NC 4.0)
dc.rightsopenAccess
dc.subjectBacillus sp. P7
dc.subjectBovine casein micelle
dc.subjectEnzymatic coagulation
dc.subjectExperimental design
dc.subjectAntioxidant activity
dc.titlePhysical-mathematical model to predict the kinetic coagulation process by clotting activity of bacterial endopeptidases
dc.typearticle
dc.typeartículo
dc.typepublishedVersion


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