Published 2022-10-20
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Enzymatic hydrolysis of Californian red worm (Eisenia fetida) proteins with different proteases

DOI: https://doi.org/10.22490/25394088.6502
Leidy Johanna Gómez Sampedro Universidad Nacional Abierta y a Distancia
Angela Maria Noreña Mora Universidad Nacional Abierta y a Distancia
Yhoan Sebastian Gaviria Gaviria Universidad de Antioquia
Jose Edgar Zapata Montoya Universidad de Antioquia

The enzymatic hydrolysis of proteins is a biotechnological technique that has gained great importance, since it constitutes an effective strategy for obtaining hydrolysates and peptides with techno-functional and biological properties. These properties depend on many factors, one of the most important it is enzyme type used to the reaction. The purpose of this work was to evaluate the effectiveness of different proteases in the hydrolysis process of Californian red worm (LRC) proteins. For this, the catalytic activity of three proteases with different characteristics was evaluated: Alcalase 2.4L, Flovourzyme and Neutrase, and the LRC hydrolysis process was carried out with each enzyme, under the same enzyme/substrate ratio and the optimal reaction conditions for each enzyme. Each reaction was carried out for 60 minutes after which the degree of hydrolysis (DH) was evaluated to identify the catalytic efficiency of the enzymes on this substrate. The results showed that the enzyme with the highest efficiency in the LRC hydrolysis process was Alcalase 2.4L with which a DH of 13.02% was achieved, twice higher than DH achieved with the other two enzymes. In conclusion, LRC proteins can be efficiently hydrolyzed with an endoprotease such as Alcalase 2.4L, obtaining hydrolysates that could be used in the food industry.

keywords: Alcalase 2.4L, Catalytic activity, Proteolysis
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How to Cite

Gómez Sampedro, L. J., Noreña Mora, A. M., Gaviria Gaviria, Y. S., & Zapata Montoya, J. E. (2022). Enzymatic hydrolysis of Californian red worm (Eisenia fetida) proteins with different proteases. Publicaciones E Investigación, 16(4). https://doi.org/10.22490/25394088.6502
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