Enzymatic generation of whey protein hydrolysates under pH-controlled and non pH-controlled conditions: Impact on physicochemical and bioactive properties

Maux, Solène Le; Nongonierma, Alice B.; Barre, Chloé; Fitzgerald, Richard J.

doi:10.1016/j.foodchem.2015.12.021

Cited by 80 publications

(63 citation statements)

References 26 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Another drawback of this method is the high salt content of the final hydrolysate as a consequence of the alkali or acid addition, which is required to maintain the pH constant and monitor the DH (Whitehurst and van Oort, 2009). As suggested by a recent study on whey protein, an interesting alternative could be to carry out the hydrolysis reaction without controlling pH (Le Maux et al, 2016). This work indicated that the bioactive properties of the hydrolysates (e.g., antioxidant and antidiabetic) might or might not be influenced by the control of the pH, depending on the enzyme employed (e.g., papain or a microbial-derived alternative).…”

Section: Enzymatic Protein Hydrolysismentioning

confidence: 84%

Peptides: Production, bioactivity, functionality, and applications

Hajfathalian

Ghelichi

Moreno

et al. 2017

Critical Reviews in Food Science and Nutrition

120

View full text Add to dashboard Cite

Production of peptides with various effects from proteins of different sources continues to receive academic attention. Researchers of different disciplines are putting increasing efforts to produce bioactive and functional peptides from different sources such as plants, animals, and food industry by-products. The aim of this review is to introduce production methods of hydrolysates and peptides and provide a comprehensive overview of their bioactivity in terms of their effects on immune, cardiovascular, nervous, and gastrointestinal systems. Moreover, functional and antioxidant properties of hydrolysates and isolated peptides are reviewed. Finally, industrial and commercial applications of bioactive peptides including their use in nutrition and production of pharmaceuticals and nutraceuticals are discussed.

show abstract

Section: Enzymatic Protein Hydrolysismentioning

confidence: 84%

Peptides: Production, bioactivity, functionality, and applications

Hajfathalian

Ghelichi

Moreno

et al. 2017

Critical Reviews in Food Science and Nutrition

120

View full text Add to dashboard Cite

show abstract

“…These products may include, e.g., carbonyl species known to be products of the α-carbon H abstraction pathway [28]. To exclude an influence of acidic or basic hydrolysis on the observed formation of glycine [41], control experiments were conducted, in which (Gly) 3 was incubated under acidic (pH 2) and basic (pH 12) conditions for 24 h, respectively. No glycine formation was observed in these experiments.…”

Section: Resultsmentioning

confidence: 99%

Release of free amino acids upon oxidation of peptides and proteins by hydroxyl radicals

et al. 2017

View full text Add to dashboard Cite

Hydroxyl radical-induced oxidation of proteins and peptides can lead to the cleavage of the peptide, leading to a release of fragments. Here, we used high-performance liquid chromatography tandem mass spectrometry (HPLC-MS/MS) and pre-column online ortho-phthalaldehyde (OPA) derivatization-based amino acid analysis by HPLC with diode array detection and fluorescence detection to identify and quantify free amino acids released upon oxidation of proteins and peptides by hydroxyl radicals. Bovine serum albumin (BSA), ovalbumin (OVA) as model proteins, and synthetic tripeptides (comprised of varying compositions of the amino acids Gly, Ala, Ser, and Met) were used for reactions with hydroxyl radicals, which were generated by the Fenton reaction of iron ions and hydrogen peroxide. The molar yields of free glycine, aspartic acid, asparagine, and alanine per peptide or protein varied between 4 and 55%. For protein oxidation reactions, the molar yields of Gly (∼32–55% for BSA, ∼10–21% for OVA) were substantially higher than those for the other identified amino acids (∼5–12% for BSA, ∼4–6% for OVA). Upon oxidation of tripeptides with Gly in C-terminal, mid-chain, or N-terminal positions, Gly was preferentially released when it was located at the C-terminal site. Overall, we observe evidence for a site-selective formation of free amino acids in the OH radical-induced oxidation of peptides and proteins, which may be due to a reaction pathway involving nitrogen-centered radicals.Electronic supplementary materialThe online version of this article (doi:10.1007/s00216-017-0188-y) contains supplementary material, which is available to authorized users.

show abstract

“…The DH of the hydrolysates (H1-H9) was determined in triplicate (n=3) using the TNBS method as already outlined. 26 Absorbance values at 350 nm were measured with a microplate reader (Biotek Synergy HT, Winoosky, VT, USA). The free amino group concentration (AN) was calculated using a Leu standard curve and the absorbance values.…”

Section: Degree Of Hydrolysis (Dh)mentioning

confidence: 99%

Generation of wheat gluten hydrolysates with dipeptidyl peptidase IV (DPP-IV) inhibitory properties

et al. 2017

View full text Add to dashboard Cite

Wheat gluten, a Pro-rich dietary protein, was investigated for its potential to produce dipeptidyl peptidase IV (DPP-IV) inhibitory peptides during enzymatic hydrolysis with Debitrase HYW20. Nine gluten hydrolysates (H1-H9) were generated using a 2 factor × 3 level design of experiments (DOE) including the incubation temperature (40, 50 and 60 °C) and the enzyme: substrate ratio (E : S, 0.5, 1.0 and 1.5% (w/w)). Their DPP-IV half maximal inhibitory concentration (IC) ranged from 0.24 ± 0.02 (H9) to 0.66 ± 0.06 mg mL (H2A and H7) and their degree of hydrolysis (DH) from 31.7 ± 0.9 (H7) to 62.2 ± 3.0% (H6). Gluten and H9, the most potent DPP-IV inhibitory hydrolysate, were subjected to simulated gastrointestinal digestion (SGID), yielding Gluten_CorPP and H9_CorPP, respectively. H9_CorPP had a higher DPP-IV inhibitory potency than Gluten_CorPP (i.e., DPP-IV IC values of 0.33 ± 0.03 vs. 1.45 ± 0.26 mg mL, respectively). H9 and H9_CorPP both contained relatively potent DPP-IV inhibitory peptides such as Val-Pro-Leu, Trp-Leu and Trp-Pro which were identified by liquid chromatography tandem mass spectrometry (LC-MS/MS). In addition, several sequences possessing features of DPP-IV inhibitory peptides, mostly consisting of a penultimate or C-terminal Pro, were identified within H9. The presence of Pro-containing peptides within H9 may contribute to its stability to digestive enzymes. Gluten hydrolysates may have antidiabetic potential for humans.

show abstract

Enzymatic generation of whey protein hydrolysates under pH-controlled and non pH-controlled conditions: Impact on physicochemical and bioactive properties

Cited by 80 publications

References 26 publications

Peptides: Production, bioactivity, functionality, and applications

Peptides: Production, bioactivity, functionality, and applications

Release of free amino acids upon oxidation of peptides and proteins by hydroxyl radicals

Generation of wheat gluten hydrolysates with dipeptidyl peptidase IV (DPP-IV) inhibitory properties

Contact Info

Product

Resources

About