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Application of Goat and Lamb Lipases on the Development of New Immobilized Biocatalysts Aiming at Fish Oil Hydrolysis.
- Source :
-
Applied biochemistry and biotechnology [Appl Biochem Biotechnol] 2024 Nov; Vol. 196 (11), pp. 8070-8081. Date of Electronic Publication: 2024 Apr 29. - Publication Year :
- 2024
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Abstract
- The use of lipases from animal sources for the synthesis of new biocatalysts is barely studied in the literature. The present work focused on the immobilization of lipases from kid goat's and lamb's epiglottis in different ionic supports. For this, anionic supports (monoaminoethyl-N-aminoethyl-agarose (MANAE) and diethylaminoethyl-agarose (DEAE)) and cationic supports (carboxymethyl-agarose and sulfopropyl-agarose) were used. The immobilization parameters were evaluated, as well as the thermal stability of the immobilized enzymes and their stability at different values of pH. Then, the performance of the biocatalysts was evaluated in hydrolysis reactions for obtaining omega-3 fatty acids from fish oil (eicosapentaenoic acid (EPA) and docosahexaenoic acid (DHA)). Values of 100% of recovered activity were obtained for lipase from goats, indicating that it was possible to maintain all the enzymatic activities of the immobilized enzymes on the supports. The immobilized enzymes were more stable in different pH conditions and at a temperature of 50 °C, reaching values of stabilization factor of 12.17 and t <subscript>1/2</subscript> of 9.86 h <superscript>-1</superscript> , for lamb lipase immobilized in sulfopropyl agarose. In general, the anionic supports led to lower Km values and the cationic ones to a higher Vmax. Lamb lipase showed the highest selectivity values for EPA/DHA, reaching values of 6.43 using MANAE. Thus, the high potential for using such biocatalysts from animal sources in the food or pharmaceutical industries is observed.<br />Competing Interests: Declarations. Consent to Participate: All authors provided their consent to participate. Consent for Publication: All authors provided their consent to publish their work. Competing Interests: The authors declare no competing interests.<br /> (© 2024. The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature.)
Details
- Language :
- English
- ISSN :
- 1559-0291
- Volume :
- 196
- Issue :
- 11
- Database :
- MEDLINE
- Journal :
- Applied biochemistry and biotechnology
- Publication Type :
- Academic Journal
- Accession number :
- 38683451
- Full Text :
- https://doi.org/10.1007/s12010-024-04942-2