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Author: search.filters.author.Pereira, Nair de los Angeles

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    Antioxidant and functional properties of bioactive peptide fractions derived from shrimp (Pleoticus muelleri) waste hydrolysates.
    (Elsevier, 2025-06-16) Liebana, Clara; Pereira, Nair de los Angeles; Fernandez-Gimenez, Analía Veronica; Granone, Luis Ignacio; Fangio, María Florencia
    Protein hydrolysates were prepared from shrimp (Pleoticus muelleri) waste through autolysis (Aut) and using 1 % and 2 % (v/v) Alcalase (Alc 1 and Alc 2, respectively). The degree of hydrolysis (DH) and antioxidant activities were assessed via 2,2-diphenyl-1-picrylhydrazyl (DPPH) and 2,2′-azino-bis (3-ethylbenzothiazoline-6-sulfonic acid) (ABTS•+) scavenging assays at various hydrolysis times. After 90 min, Aut and Alc 1 were selected for fractionation by ultrafiltration, yielding peptide fractions: F1 (>10 kDa), F2 (3–10 kDa), and F3 (<3 kDa). Functional properties, antioxidant capacities, and lipid peroxidation inhibition in raw fish emulsions were assessed for both whole hydrolysates (WH) and their peptide fractions. Alc 1 achieved a significantly higher DH (42.02 ± 5.50 %) than Aut (28.75 ± 2.34 %). Both hydrolysates and their fractions displayed high solubility (>65.49 ± 2.07 %) across a wide pH range. The F1 fraction exhibited the strongest DPPH scavenging activity for both hydrolysates, with Aut's F1 reaching 445.90 ± 19.52 mg AEAC/100 g dry weight and Alc 1's F1 achieving 461.10 ± 15.81 mg AEAC/100 g dry weight. Aut's F3 fraction had the highest ABTS•+ scavenging capacity (723.66 ± 36.58 mg AEAC/100 g dry weight), while Alc 1's WH exhibited superior activity (776.20 ± 52.55 mg AEAC/100 g dry weight). Overall, Aut's F1 fraction demonstrated the most favorable antioxidant and functional properties, while Alc 1's F3 fraction showed superior solubility and lipid peroxidation inhibition. These findings underscore the potential of shrimp (P. muelleri) waste for producing functional hydrolysates and bioactive peptides with diverse applications.
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    Digestive proteinases from the marine fish processing wastes of the South‐West Atlantic ocean: their partial characterization and comparison.
    (2022-01-01) Friedman, Ivana S.; Behrens, Leonel A.; Pereira, Nair de los Angeles; Contreras, Edgardo M.; Fernández-Gimenez, Analia V.
    Fish processing generates plenty of waste that is directly discarded in open-air dumps and water sources, or treated in the same way as urban solid waste, causing serious pollution problems. The waste represents a significant source of high-value bioproducts with potential applications in different industrial processes such as the production of feed, fertilizers, biodiesel and biogas, detergent additives and cosmetics. The objective of this study was to characterize and compare specific activities under different pH values and temperature conditions of acid and alkaline proteinases and viscera yield from the following fish species: Argentine hake Merluccius hubbsi, Brazilian flathead Percophis brasiliensis, Brazilian codling Urophycis brasiliensis and Stripped weakfish Cynoscion guatucupa. Individuals were fished off the coast of Mar del Plata (Argentina) by a commercial fleet and the viscera were immediately extracted and kept on ice until use. Stomach proteinases from four species had the highest activity at pH 2, with stability in the range of pH 2–4. The optimum pH was 11.5 from intestinal enzymes of C. guatucupa, M. hubbsi and P. brasiliensis and 9.5 from intestinal enzymes of U. brasiliensis. Alkaline proteinases from all species were highly stable in the range of 7–11.5. The optimum temperature of stomach proteinases from the four species studied were 30 and 50_C, with stability at 10 and 30_C during 150 min. The optimum temperature of intestinal enzymes from the tested species were 50_C with high stability at 10 and 30_C during 150 min. Alkaline proteinase from all species and acid proteinases from C. guatucupa were inactive at 70_C after 150 min, while there was a residual activity lower than 5% at 80_C on preincubated stomach enzymes of M.hubbsi, P. brasiliensis and U. brasiliensis after 5, 10 and 20 min, respectively. Digestive proteinases recovered in this study could be appropriate for technological usage, reducing manufacturing costs, obtaining revenue from fishery wastes, and contributing to the reduction of environmental pollution.