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Comparative oil extraction from mutt (Myliobatis goodei) liver by enzymatic hydrolysis: free versus immobilized biocatalyst.
Morales, Andrés H; Pisa, José H; Gómez, María I; Romero, Cintia M; Vittone, Marina; Massa, Agueda E; Lamas, Daniela L.
Afiliación
  • Morales AH; Laboratorio de Biocatálisis y Biomateriales, Planta Piloto de Procesos Industriales Microbiológicos, PROIMI-CONICET, San Miguel de Tucumán, 4000, Argentina.
  • Pisa JH; Laboratorio de Biocatálisis y Biomateriales, Planta Piloto de Procesos Industriales Microbiológicos, PROIMI-CONICET, San Miguel de Tucumán, 4000, Argentina.
  • Gómez MI; Instituto de Química Inorgánica, Facultad de Bioquímica, Química y Farmacia, UNT, San Miguel de Tucumán, 4000, Argentina.
  • Romero CM; Laboratorio de Biocatálisis y Biomateriales, Planta Piloto de Procesos Industriales Microbiológicos, PROIMI-CONICET, San Miguel de Tucumán, 4000, Argentina.
  • Vittone M; Instituto de Química Inorgánica, Facultad de Bioquímica, Química y Farmacia, UNT, San Miguel de Tucumán, 4000, Argentina.
  • Massa AE; Instituto Nacional de Investigación y Desarrollo Pesquero, INIDEP, Mar del Plata, Argentina.
  • Lamas DL; Instituto Nacional de Investigación y Desarrollo Pesquero, INIDEP, Mar del Plata, Argentina.
J Sci Food Agric ; 104(4): 2493-2501, 2024 Mar 15.
Article en En | MEDLINE | ID: mdl-37986264
ABSTRACT

BACKGROUND:

The development and fine-tuning of biotechnological processes for fish oil extraction constitute a very important focus to contribute to the development of a food industry based on fish consumption. This work lies in a comparative analysis of the oil extraction yield of Myliobatis goodei livers using free and immobilized enzymes.

RESULTS:

An immobilized biocatalyst was designed from the cell-free extract of a Bacillus sp. Mcn4. A complete factorial design was used to study the components of the bacterial culture medium and select the condition with the highest titers of extracellular enzymatic activities. Wheat bran had a significant effect on the culture medium composition for enzymatic production. The immobilized biocatalyst was designed by covalent binding of the proteins present in the cocktail retaining a percentage of different types of enzymatic activities (Mult.Enz@MgFe2 O4 ). Among the biocatalyst used, Alcalase® 2.4 L and Purazyme® AS 60 L (free commercial proteases) showed extraction yields of 87.39% and 84.25%, respectively, while Mult.Enz@MgFe2 O4 achieved a better one of 89.97%. The oils obtained did not show significant differences in their physical-chemical properties while regarding the fatty acid content, the oil extracted with Purazyme® AS 60 L showed a comparatively lower proportion of polyunsaturated fatty acids.

CONCLUSIONS:

Our results suggest that the use of by-products of M. goodei is a valid alternative and encourages the use of immobilized multienzyme biocatalysts for the treatment of complex substrates in the fishing industry. © 2023 Society of Chemical Industry.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Enzimas Inmovilizadas / Lipasa Idioma: En Revista: J Sci Food Agric Año: 2024 Tipo del documento: Article País de afiliación: Argentina

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Enzimas Inmovilizadas / Lipasa Idioma: En Revista: J Sci Food Agric Año: 2024 Tipo del documento: Article País de afiliación: Argentina
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