2015
DOI: 10.1016/j.foodres.2015.09.012
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Identification of short peptide sequences in the nanofiltration permeate of a bioactive whey protein hydrolysate

Abstract: Short peptides in food protein hydrolysates are of significant interest as they may be highly bioactive whilst also being bioavailable. A dipeptidyl peptidase IV (DPP-IV) inhibitory whey protein hydrolysate (WPH) was fractionated using nanofiltration (

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Cited by 50 publications
(22 citation statements)
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References 36 publications
(57 reference statements)
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“…The systematic analysis of peptides possessing a specific length (e.g., di‐ or decapeptides) (Lacroix & Li‐Chan, ; Lan et al, ) or features (e.g., tripeptides with a Trp‐Arg N‐terminal sequence) (Lan et al, ) has been carried out using peptide library/array approaches. Another most commonly used approach consists in the identification of DPP‐IV inhibitory peptides following bioassay‐driven fractionation (Lacroix & Li‐Chan, ; Le Maux, Nongonierma, Murray, Kelly, & FitzGerald, ; Silveira, Martínez‐Maqueda, Recio, & Hernández‐Ledesma, ; Y. Zhang, Chen, Ma, & Chen, ). All three approaches (in silico methods, peptide library/array, and bioassay‐driven fractionation) have yielded the identification of relatively potent DPP‐IV inhibitory peptides.…”
Section: Identification Of Dpp‐iv Inhibitory Peptidesmentioning
confidence: 99%
See 1 more Smart Citation
“…The systematic analysis of peptides possessing a specific length (e.g., di‐ or decapeptides) (Lacroix & Li‐Chan, ; Lan et al, ) or features (e.g., tripeptides with a Trp‐Arg N‐terminal sequence) (Lan et al, ) has been carried out using peptide library/array approaches. Another most commonly used approach consists in the identification of DPP‐IV inhibitory peptides following bioassay‐driven fractionation (Lacroix & Li‐Chan, ; Le Maux, Nongonierma, Murray, Kelly, & FitzGerald, ; Silveira, Martínez‐Maqueda, Recio, & Hernández‐Ledesma, ; Y. Zhang, Chen, Ma, & Chen, ). All three approaches (in silico methods, peptide library/array, and bioassay‐driven fractionation) have yielded the identification of relatively potent DPP‐IV inhibitory peptides.…”
Section: Identification Of Dpp‐iv Inhibitory Peptidesmentioning
confidence: 99%
“…Ile‐Pro‐Ile is found in a range of dietary proteins such as bovine κ‐CN, chicken egg ovotransferrin, and the phycoerythrin β subunit from the macroalga P. palmata (Nongonierma & FitzGerald, ). For example, Ile‐Pro‐Ile (κ‐CN (f26–28)) was identified by LC‐MS/MS in the nanofiltration permeate of a bovine whey protein hydrolysate displaying a DPP‐IV IC 50 value of 0.66 ± 0.08 mg/mL (Le Maux, Nongonierma, Murray, et al, ).…”
Section: Identification Of Dpp‐iv Inhibitory Peptidesmentioning
confidence: 99%
“…The method of Le Maux, Nongonierma, Murray, Kelly, and FitzGerald (2015) was employed to measure the protein content of permeates and hydrolyzates. To find the appropriate range of hydrolysis optimization conditions, the pretreatments were performed at 40, 45, 50, 55°C, 60, 90, 150, 180, and 210 min and 30, 60, and 90 Anson unit/kg protein.…”
Section: Protein Hydrolysismentioning
confidence: 99%
“…Le Maux et al [17] separated the hydrolysates from whey protein hydrolysis using spiral wound NF membrane (200 Da retention coefficient). They used the membrane as a purifying method of reaction mixture and to separate the products (peptides) from unhydrolysed whey protein.…”
Section: Introductionmentioning
confidence: 99%
“…They used the membrane as a purifying method of reaction mixture and to separate the products (peptides) from unhydrolysed whey protein. [Le Maux et al, 2015]. Uluko et al [18] used three types of membranes with retention coefficient: 8.0, 3.5 and 0.2 kDa in order to separate angiotensin converting enzyme (ACE) from its inhibitors present in whey protein hydrolysates mixture.…”
Section: Introductionmentioning
confidence: 99%