Efficiency of Microencapsulation of Proteolytic Enzymes
Currently, special attention is paid to the study of the effectiveness of the immobilization method—microencapsulation. The aim of the research is to obtain a complex enzyme preparation from pepsin and papain by sequential microencapsulation of enzymes in a pseudo-boiling layer and to evaluate its t...
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| Autores principales: | , , , , , |
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| Formato: | article |
| Lenguaje: | EN |
| Publicado: |
MDPI AG
2021
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| Materias: | |
| Acceso en línea: | https://doaj.org/article/25e98154c446486985a22468b5892796 |
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| Sumario: | Currently, special attention is paid to the study of the effectiveness of the immobilization method—microencapsulation. The aim of the research is to obtain a complex enzyme preparation from pepsin and papain by sequential microencapsulation of enzymes in a pseudo-boiling layer and to evaluate its tenderizing effect on pork. The objects of research were enzymes: pepsin and papain, which were microencapsulated in a protective coating of maltodextrin. It was found that the biocatalytic activity of the complex enzyme preparation is higher than that of pure enzymes. Microencapsulation allows maintaining the high proteolytic activity of enzymes for a long storage period. It has been shown that the thickness of the protective layer during microencapsulation of pepsin and papain in the pseudo-boiling layer of maltodextrin should be in the range of 4–6 microns. During the research, the physicochemical properties of pork were studied depending on the duration of fermentation. It was found that the maximum activity of immobilized enzymes is shifted to the alkaline side. Pork salting with the use of a microencapsulated enzyme preparation in the brine increases the water-binding capacity of proteins to a greater extent in comparison with brine with pure enzymes. The presented data show the high efficiency of sequential microencapsulation of the enzyme pepsin and then papain into a protective layer of maltodextrin in order to preserve their activity during storage. |
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