2026-04-18T14:18:07Zhttps://riubu.ubu.es/oai/request

oai:riubu.ubu.es:10259/104432025-05-14T10:59:47Zcom_10259_4244com_10259_5086com_10259_2604col_10259_4245

2025-05-08T10:50:13Z urn:hdl:10259/10443 Membrane fractionation of hydrolysates of the water-soluble protein from tuna fish meal obtained by subcritical water and enzymatic treatments. Comparison of physical and chemical properties Barea Gómez, Pedro Illera Gigante, Alba Ester Candela Gil, Helena Melgosa Gómez, Rodrigo Benito Moreno, José Manuel Beltrán Calvo, Sagrario Sanz Díez, Mª Teresa Protein hydrolysis Dead-end fltration (UF and NF) Protein and Free amino acids profle Reducing and chelating capacities Molecular weight distribution Two different hydrolysates of the water-soluble protein (WSP) fraction from tuna fish meal were obtained by subcritical water-CO2 (subW-CO2) and Alcalase® treatments. Hydrolysates showed different chemical composition regarding their free amino acid (FAA) profile and molecular weight distribution of the peptides generated. Consequently, different strategies were proposed by using a stirred dead-end filtration system equipped with flat sheet membranes. Two nanofiltration (NF) consecutive steps were proposed for fractionation of subW-CO2 hydrolysates with polyamide membranes (800–600 Da and 300–150 Da) yielding a first retentate where 79% of the protein fraction was retained, while 92% of FAA were retained in the second step with a purity index of 29%. Alcalase® hydrolysates were fractionated by ultrafiltration (UF, 10 kDa) followed by NF (1–1.1 kDa) with polyethersulfone membranes obtaining a first retentate with more than 65% of protein fraction retention with a purity index of 50%. A relatively wide molecular weight distribution was observed in all streams, with high antioxidant and iron-chelating capacities in the retentate fractions. 2025-05-08T10:50:13Z 2025-05-08T10:50:13Z 2025-03 info:eu-repo/semantics/article 2197-4365 http://hdl.handle.net/10259/10443 10.1186/s40643-025-00850-3 2197-4365 eng Bioresources and Bioprocessing. 2025, V. 12, n. 16 https://doi.org/10.1186/s40643-025-00850-3 http://creativecommons.org/licenses/by/4.0/ info:eu-repo/semantics/openAccess Atribución 4.0 Internacional Springer