Impact of ultrafiltration and nanofiltration of an industrial fish protein hydrolysate on its bioactive properties
|Author(s)||Picot Laurent1, Ravallec Rozenn2, Fouchereau-Peron Martine3, Vandanjon Laurent4, 5, Jaouen Pascal4, Chaplain-Derouiniot Maryse4, Guerard Fabienne6, Chabeaud Aurelie6, Legal Yves3, Martinez Alvarez Oscar3, 7, Berge Jean-Pascal8, Piot Jean-Marie1, Batista Irineu11, Pires Carla11, Thorkelsson Gudjon9, 10, Delannoy Charles, Jakobsen Greta, Johansson Inger, Bourseau Patrick4, 5|
|Affiliation(s)||1 : Univ Rochelle, CNRS, UMR 6250, LIENSs, La Rochelle, France.
2 : IUT A Polytech Lille, UPRES EA 1026, ProBioGEM, Lille, France.
3 : UPMC, UMR BOREA, MNHN 7208, CNRS,Stn Biol Marine,IRD 207, Concarneau, France.
4 : Univ Nantes, CNRS, UMR 6144, GEPEA, St Nazaire, France.
5 : Univ Bretagne Sud, LIMATB, Lorient, France.
6 : Univ Bretagne Occidentale, ANTiOX, Quimper, France.
7 : CSIC, Inst Frio, E-28040 Madrid, Spain.
8 : STAM, IFREMER, Nantes, France.
9 : Maris Ohf, Reykjavik, Iceland.
10 : Univ Iceland, Reykjavik, Iceland.
11 : Ipimar, Lisbon, Portugal.
|Source||Journal Of The Science Of Food And Agriculture (0022-5142) (John Wiley & Sons Ltd), 2010-08 , Vol. 90 , N. 11 , P. 1819-1826|
|WOS© Times Cited||91|
|Keyword(s)||fish protein hydrolysate, ultrafiltration, nanofiltration, membrane separation, fractionation process, bioactive peptide|
|Abstract||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|