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Angiotensin-Converting Enzyme Inhibition In Vitro by Protein Hydrolysates and Peptide Fractions from Mojarra of Nile Tilapia (Oreochromis niloticus) Skeleton

Journal of Medicinal Food 2019년 22권 3호 p.286 ~ 293
Borges-Contreras Berenise, Martinez-Sanchez Cecilia Eugenia, Herman-Lara Erasmo, Rodriguez-Miranda Jesus, Hernandez-Santos Betsabe, Juarez-Barrientos Jose Manuel, Guerra-Almonacid Carlos Martin, Betancur-Ancona David Abram, Torruco-Uco Juan Gabriel,
소속 상세정보
 ( Borges-Contreras Berenise ) - National Technology of Mexico Technological Institute of Tuxtepec
 ( Martinez-Sanchez Cecilia Eugenia ) - National Technology of Mexico Technological Institute of Tuxtepec
 ( Herman-Lara Erasmo ) - National Technology of Mexico Technological Institute of Tuxtepec
 ( Rodriguez-Miranda Jesus ) - National Technology of Mexico Technological Institute of Tuxtepec
 ( Hernandez-Santos Betsabe ) - National Technology of Mexico Technological Institute of Tuxtepec
 ( Juarez-Barrientos Jose Manuel ) - National Technology of Mexico Higher Technological Institute of Tierra Blanca
 ( Guerra-Almonacid Carlos Martin ) - University of Tolima Faculty of Sciences Department of Chemistry
 ( Betancur-Ancona David Abram ) - Autonomous University of Yucatan Faculty of Chemical Engineering Department of Food Science
 ( Torruco-Uco Juan Gabriel ) - National Technology of Mexico Technological Institute of Tuxtepec

Abstract


Mojarra of Nile tilapia (Oreochromis niloticus) skeleton was used as protein source for the preparation of protein hydrolysates and peptide fractions with angiotensin-converting enzyme (ACE) inhibitory activity. The flour presented a content of 34.92% protein and a brightness (luminosity, L*) of 82.29. Protein hydrolysates were obtained from the protein-rich flour with the enzymes Flavourzyme® and Alcalase® reaching degree of hydrolysis (%DH) of 52% and 67% at 100?min of reaction, respectively. Both hydrolysates showed low-molecular-weight (MW) peptides estimated by sodium dodecyl sulfate?polyacrylamide gel electrophoresis. The hydrolysates obtained with Flavourzyme at 60?min and at 80?min with Alcalase showed greater ACE inhibitory activity with IC50 values of 0.238 and 0.344?mg/mL, respectively. The peptide fraction A (MW >10?kDa) with Flavourzyme and fraction B (MW?=?10?5?kDa) with Alcalase obtained by ultrafiltration of hydrolysates with higher DH presented IC50 of 0.728 and 0.354?mg/mL, respectively, whereas peptide fraction C (MW?=?5?3?kDa) with both enzymes hydrolysates with greater ACE inhibitory activity showed IC50 values of 0.470 and 0.634?mg/mL. The components obtained in this study could be used as functional ingredients in the design and development of functional foods.

키워드

angiotensin-converting enzyme; Oreochromis niloticus; peptide fractions; protein hydrolysates; ultrafiltration

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