Milk Protein Hydrolysates and Bioactive Peptides

Nongonierma, Alice B.; O’Keeffe, Martina B.; Fitzgerald, Richard J.

doi:10.1007/978-1-4939-2800-2_15

Cited by 47 publications

(32 citation statements)

References 430 publications

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“…They either involved a Zn 2+ ‐dependent or independent manner that triggered significant conformational changes of Zn 2+ ‐ligands and the binding channel, leading to a significant ACE inhibition (Masuyer, Schwager, Sturrock, Isaac, & Acharya, ). These findings imply that three C‐terminal residues are crucial in binding to ACE active site and subsites, which also explains that the low ACE affinity of ALPMHIR is possibly due to the low binding of HIR to ACE, in addition to the size limit (Nongonierma, O’keeffe, & FitzGerald, ).…”

Section: Molecular Structure–activity Relationship Of Acei Peptidesmentioning

confidence: 96%

Molecular interactions, bioavailability, and cellular mechanisms of angiotensin-converting enzyme inhibitory peptides

2018

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Food-derived angiotensin-converting enzyme inhibitory (ACEi) peptides have gained substantial interest as potential alternatives to synthetic drugs in the management of hypertension. Peptide size and sequence are two critical factors that determine their potency, bioavailability, and cellular mechanisms. Molecular interaction studies between ACE and ACEi peptides support that potent ACEi peptides are generally composed of hydrophobic, positively charged, and aromatic or cyclic amino acid residues at the third, second, and first position from the C-terminus, respectively. Small peptides containing N-terminal Tyr and/or C-terminal Pro could improve their stability against enterocyte peptidases and, thus, their bioavailability. Different ACEi peptides can reduce aberrant cellular proliferation, excessive inflammation, and oxidative stress but through different mechanisms. Further understanding the structure-activity-bioavailability relationships will help design novel potent ACEi peptides with improved bioavailability and in vivo efficacy. Practical applicationsAngiotensin-converting enzyme inhibitory peptides have the potential for uses as functional food ingredients against hypertension. K E Y W O R D S angiotensin-converting enzyme, angiotensin-converting enzyme inhibitory peptides, bioavailability, cellular mechanisms, molecular docking, vascular endothelial cells, vascular smooth muscle cells J Food Biochem. 2019;43:e12572.

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Section: Molecular Structure–activity Relationship Of Acei Peptidesmentioning

confidence: 96%

Molecular interactions, bioavailability, and cellular mechanisms of angiotensin-converting enzyme inhibitory peptides

2018

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“…Enzymatic hydrolysis is well accepted as a food-grade approach for the large-scale production of BAPs in a relatively cost-efficient manner. 1,17 In order to release specic BAP sequences from food proteins, knowledge of both the amino acid sequence of the protein as well as the enzyme specicity and kinetics is required.…”

Section: Limitations Of Qsar For the Study Of Bapsmentioning

confidence: 99%

Learnings from quantitative structure–activity relationship (QSAR) studies with respect to food protein-derived bioactive peptides: a review

Nongonierma

Fitzgerald

2016

RSC Adv.

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“…Enzymatic hydrolysis of food proteins releases peptides that are reported to have various bioactivities (Mine et al, 2010). In particular, milk protein-derived peptides have been studied for their potential to act as agents having anti-cancer, opioid, anti-hypertensive, ACE inhibitory and antioxidant activities (Nongonierma et al, 2016). Furthermore, there is growing evidence to support the fact that some hydrolysates/ peptides have multifunctional activity.…”

Section: Introductionmentioning

confidence: 99%

Identification of angiotensin converting enzyme inhibitory and antioxidant peptides in a whey protein concentrate hydrolysate produced at semi‐pilot scale

O’Keeffe

Conesa

Fitzgerald

2017

Int J of Food Sci Tech

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Summary Antioxidant and angiotensin converting enzyme (ACE) inhibitory peptides were identified in a 5 kDa ultrafiltration permeate of a whey protein hydrolysate generated at semi‐pilot scale. Further laboratory scale ultrafiltration of this 5 kDa permeate resulted in a 0.65 kDa permeate with antioxidant, (1.11 ± 0.074 μmol TE per mg dry weight, oxygen radical absorbance capacity, ORAC) and ACE inhibitory (ACE IC50 0.215 ± 0.043 mg mL−1) activities. Semi‐preparative (SP) reverse phase high‐performance liquid chromatography (RP‐HPLC) of the 0.65 kDa permeate resulted in a fraction (SP_F3) with a 4.4‐fold increase in ORAC activity (4.83 ± 0.45 μmol TE mg dry weight) and a 1.3‐fold increase in ACE inhibitory activity (84.35 ± 1.36% inhibition when assayed at 0.28 mg mL−1). Peptides within SP_F3 were identified using UPLC‐ESI‐MS/MS. Met‐Pro‐Ile had the highest ORAC activity (205.75 ± 12.08 μmol TE per mmol peptide) while Met‐Ala‐Ala and Val‐Ala‐Gly‐Thr had the highest ACE inhibitory activities (IC50:515.50 ± 1.11 and 610.30 ± 2.41 μm, respectively).

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Milk Protein Hydrolysates and Bioactive Peptides

Cited by 47 publications

References 430 publications

Molecular interactions, bioavailability, and cellular mechanisms of angiotensin-converting enzyme inhibitory peptides

Molecular interactions, bioavailability, and cellular mechanisms of angiotensin-converting enzyme inhibitory peptides

Learnings from quantitative structure–activity relationship (QSAR) studies with respect to food protein-derived bioactive peptides: a review

Identification of angiotensin converting enzyme inhibitory and antioxidant peptides in a whey protein concentrate hydrolysate produced at semi‐pilot scale

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