FN Archimer Export Format PT J TI Impact of ultrafiltration and nanofiltration of an industrial fish protein hydrolysate on its bioactive properties BT AF PICOT, Laurent RAVALLEC, Rozenn FOUCHEREAU-PERON, Martine VANDANJON, Laurent JAOUEN, Pascal CHAPLAIN-DEROUINIOT, Maryse GUERARD, Fabienne CHABEAUD, Aurelie LEGAL, Yves MARTINEZ ALVAREZ, Oscar BERGE, Jean-Pascal PIOT, Jean-Marie BATISTA, Irineu PIRES, Carla THORKELSSON, Gudjon DELANNOY, Charles JAKOBSEN, Greta JOHANSSON, Inger BOURSEAU, Patrick AS 1:1;2:2;3:3;4:4,5;5:4;6:4;7:6;8:6;9:3;10:3,7;11:8;12:1;13:11;14:11;15:9,10;16:;17:;18:;19:4,5; FF 1:;2:;3:;4:;5:;6:;7:;8:;9:;10:;11:PDG-DOP-DCN-BRM-STBM;12:;13:;14:;15:;16:;17:;18:PDG-DOP-DCN-BE-LBCO;19:; C1 Univ Rochelle, CNRS, UMR 6250, LIENSs, La Rochelle, France. IUT A Polytech Lille, UPRES EA 1026, ProBioGEM, Lille, France. UPMC, UMR BOREA, MNHN 7208, CNRS,Stn Biol Marine,IRD 207, Concarneau, France. Univ Nantes, CNRS, UMR 6144, GEPEA, St Nazaire, France. Univ Bretagne Sud, LIMATB, Lorient, France. Univ Bretagne Occidentale, ANTiOX, Quimper, France. CSIC, Inst Frio, E-28040 Madrid, Spain. STAM, IFREMER, Nantes, France. Maris Ohf, Reykjavik, Iceland. Univ Iceland, Reykjavik, Iceland. Ipimar, Lisbon, Portugal. C2 UNIV LA ROCHELLE, FRANCE UNIV LILLE, FRANCE UNIV PARIS 06, FRANCE UNIV NANTES, FRANCE UBS, FRANCE UBO, FRANCE CSIC, SPAIN IFREMER, FRANCE MARIS OHF, ICELAND UNIV ICELAND, ICELAND IPIMAR, PORTUGAL SI NANTES SE PDG-DOP-DCN-BRM-STBM PDG-DOP-DCN-BE-LBCO IN WOS Ifremer jusqu'en 2018 copubli-france copubli-europe copubli-univ-france copubli-int-hors-europe IF 1.36 TC 91 UR https://archimer.ifremer.fr/doc/00011/12217/9259.pdf LA English DT Article DE ;fish protein hydrolysate;ultrafiltration;nanofiltration;membrane separation;fractionation process;bioactive peptide AB BACKGROUND: Numerous studies have demonstrated that in vitro controlled enzymatic hydrolysis of fish and shellfish proteins leads to bioactive peptides. Ultrafiltration (UF) and/or nanofiltration (NF) can be used to refine hydrolysates and also to fractionate them in order to obtain a peptide population enriched in selected sizes. This study was designed to highlight the impact of controlled UF and NF on the stability of biological activities of an industrial fish protein hydrolysate (FPH) and to understand whether fractionation could improve its content in bioactive peptides. RESULTS: The starting fish protein hydrolysate exhibited a balanced amino acid composition, a reproducible molecular weight (MW) profile, and a low sodium chloride content, allowing the study of its biological activity. Successive fractionation on UF and NF membranes allowed concentration of peptides of selected sizes, without, however, carrying out sharp separations, some MW classes being found in several fractions. Peptides containing Pro, Hyp, Asp and Glu were concentrated in the UF and NF retentates compared to the unfractionated hydrolysate and UF permeate, respectively. Gastrin/cholecystokinin-like peptides were present in the starting FPH, UF and NF fractions, but fractionation did not increase their concentration. In contrast, quantification of calcitonin gene-related peptide (CGRP)-like peptides demonstrated an increase in CGRP-like activities in the UF permeate, relative to the starting FPH. The starting hydrolysate also showed a potent antioxidant and radical scavenging activity, and a moderate angiotensin-converting enzyme (ACE)-1 inhibitory activity, which were not increased by UF and NF fractionation. CONCLUSION: Fractionation of an FPH using membrane separation, with a molecular weight cut-off adapted to the peptide composition, may provide an effective means to concentrate CGRP-like peptides and peptides enriched in selected amino acids. The peptide size distribution observed after UF and NF fractionation demonstrates that it is misleading to characterize the fractions obtained by membrane filtration according to the MW cut-off of the membrane only, as is currently done in the literature. (C) 2010 Society of Chemical Industry PY 2010 PD AUG SO Journal Of The Science Of Food And Agriculture SN 0022-5142 PU John Wiley & Sons Ltd VL 90 IS 11 UT 000280482900008 BP 1819 EP 1826 DI 10.1002/jsfa.4020 ID 12217 ER EF