Performances of ultrafiltration membranes for fractionating a fish protein hydrolysate: Application to the refining of bioactive peptidic fractions

Chabeaud, A.; Vandanjon, Laurent; Bourseau, Patrick; Jaouen, Pascal; Chaplain-Derouiniot, M.; Guérard, Fabienne

doi:10.1016/j.seppur.2009.02.012

Cited by 76 publications

(35 citation statements)

References 18 publications

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“…2) made it possible to produce four fractions, 1 which should theoretically 2 have the following compositions: The selected values for the tangential velocity (v) and the transmembrane pressure (DP) were the highest allowed by the pilot or the membrane, in order to minimize the filtration time. These pressures were chosen on the basis of some earlier tests which showed that pressure had a significant effect on peptide retention (Chabeaud et al, 2009b). However, the durations of filtrations were rather long because high volume reduction factors (VRF) were reached.…”

Section: Fractionating and Concentration Operating Modesmentioning

confidence: 99%

Fractionating white fish fillet hydrolysates by ultrafiltration and nanofiltration

Vandanjon

Grignon

Courois

et al. 2009

Journal of Food Engineering

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Section: Fractionating and Concentration Operating Modesmentioning

confidence: 99%

Fractionating white fish fillet hydrolysates by ultrafiltration and nanofiltration

Vandanjon

Grignon

Courois

et al. 2009

Journal of Food Engineering

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“…It is recognized, however, that short peptides, below 3 or 4 kDa, usually harbour bioactive properties and the peptide size is a physicochemical parameter—although not a unique one—controlling peptide activities. Some studies, however, discuss the impact of ultrafiltration on peptidic populations on the basis of size exclusion chromatograms 51–54. The present study was designed to discover whether UF and nanofiltration (NF) of a bioactive FPH, performed under controlled conditions, represent innovative industrial processes for obtaining fractions defined by a strict range of peptide size and enriched in bioactive peptides.…”

Section: Introductionmentioning

confidence: 99%

Impact of ultrafiltration and nanofiltration of an industrial fish protein hydrolysate on its bioactive properties

Picot

Ravallec

Fouchereau-Péron

et al. 2010

J. Sci. Food Agric.

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International audienceBACKGROUND: 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. Copyright © 2010 Society of Chemical Industr

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“…The transmission of the b-casein peptides was approximately 10 to 20% lower than that of micellar casein, probably being a result of the lower protein concentration of the hydrolysate (Bargeman et al 2002;Chabeaud et al 2009). The transmission of the b-casein peptides was approximately 10 to 20% lower than that of micellar casein, probably being a result of the lower protein concentration of the hydrolysate (Bargeman et al 2002;Chabeaud et al 2009).…”

Section: Two-stage Ultrafiltration Of Micellar Casein and B-casein Trmentioning

confidence: 94%

A comparison of micellar casein and β‐casein as sources of basic peptides through tryptic hydrolysis and their enrichment using two‐stage ultrafiltration

Post

Sampels

Holder

et al. 2012

Int J of Dairy Tech

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For the application of functional peptides in innovative products, these peptides have to be individually available. This may be accomplished by a well‐considered combination of a pure protein precursor, a selective cleaving enzyme, and an advanced separation technology. In this proof‐of‐principle approach, micellar casein and β‐casein were subjected to tryptic hydrolysis and the generated casein peptides were identified and characterised. The basic target peptides, β‐casein f(177‐183) and β‐casein f(170‐176), were then enriched. A permeate containing 35% of the target peptides was produced after two‐stage ultrafiltration of micellar casein tryptic hydrolysate. In comparison, enrichment up to 58% was achieved starting from β‐casein tryptic hydrolysate.

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Performances of ultrafiltration membranes for fractionating a fish protein hydrolysate: Application to the refining of bioactive peptidic fractions

Cited by 76 publications

References 18 publications

Fractionating white fish fillet hydrolysates by ultrafiltration and nanofiltration

Fractionating white fish fillet hydrolysates by ultrafiltration and nanofiltration

Impact of ultrafiltration and nanofiltration of an industrial fish protein hydrolysate on its bioactive properties

A comparison of micellar casein and β‐casein as sources of basic peptides through tryptic hydrolysis and their enrichment using two‐stage ultrafiltration

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