Physicochemical characterization and in vitro digestibility of β-lactoglobulin/β-Lg f142-148 complexes

Roufik, Samira; Gauthier, Sylvie F.; Turgeon, Sylvie L.

doi:10.1016/j.idairyj.2006.07.002

Cited by 13 publications

(10 citation statements)

References 57 publications

(63 reference statements)

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“…The peptide ALPMHIR presents the highest affinity energy and IC 50 values (IC 50 ¼ 42 mM) (Vermeirssen et al, 2002;Roufik et al, 2007) when compared with IPP and VPP (5 and 9 mM, respectively) (FitzGerald et al, 2004). As ALPMHIR is a larger ligand than IPP and VPP, there are more flexible bonds and therefore it could have been necessary to perform more docking runs for a better comparison of affinity energies (Thomsen and Christensen, 2006;Molegro, 2007).…”

Section: Resultsmentioning

confidence: 99%

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Studies on the molecular recognition between bioactive peptides and angiotensin‐converting enzyme

Pina

Roque

2008

J of Molecular Recognition

117

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High blood pressure or hypertension is a condition affecting many individuals and represents a controllable risk factor for cardiovascular diseases such as coronary heart disease and stroke. A non-pharmacological approach to manage these includes the application of food components with antihypertensive activity. Milk protein-derived peptides have been exploited as natural hypotensive agents, namely the peptides Val-Pro-Pro (VPP) and Ile-Pro-Pro (IPP), already commercialized in functional foods as a potential alternative to synthetic drugs. These bioactive peptides inhibit in vitro and in vivo the Angiotensin I-converting enzyme (ACE), a protein with an important role in blood pressure regulation. In this work, we attempted to elucidate the possible mode of interaction between the peptides and ACE, including mechanisms of binding to the cofactor Zn2+, and further contrast this with the known mode of inhibition exerted by synthetic drugs (Captopril, Enalaprilat and Lisinopril). The bioactive peptide Ala-Leu-Pro-Met-His-Ile-Arg (ALPMHIR), also known to inhibit the enzyme ACE but with a lower efficiency than VPP and IPP, was utilized in the docking studies for comparison. It was observed that the best docking poses obtained for VPP and IPP were located at the ACE catalytic site with very high resemblance to the drugs mode of interaction, including the coordination with Zn2+. As for ALPMHIR, the best docking poses were located in the narrow ACE channel outside the catalytic site, representing higher affinity energies and fewer resemblances with the interaction established by drugs.

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Section: Resultsmentioning

confidence: 99%

“…In order to increase the potential of b-Lg (142-148) for ACE inhibition, this peptide was complexed with b-Lg A. A delay in the peptide hydrolyses was observed (Roufik et al, 2007). Thus, these results suggest that ALPMHIR could enable greater inhibition of ACE if it is protected against enzymatic degradation.…”

Section: Introductionmentioning

confidence: 90%

Studies on the molecular recognition between bioactive peptides and angiotensin‐converting enzyme

Pina

Roque

2008

J of Molecular Recognition

117

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“…Table 4 shows their compositions in amino acid. Βlactoglobulin (β-LG) is the most abundant of whey proteins; it represents approximately 2 to 4g / L, which corresponds to 50% of total whey proteins [25]. Β-Lactoglobulin, absent in human milk, has all natural amino acids and contains 58% of essential amino acids.…”

Section: Whey Protein Compositionmentioning

confidence: 99%

Nutritional quality and use of whey in human food for its valorization

Bleoussi¹,

Konfo²,

Tchekessi³

et al. 2020

World J. Adv. Res. Rev.

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Whey is generated during cheese making and can be up to nine times the weight of cheese. The objective of this work is to highlight the nutritional quality and the importance of whey in order to explore other ways of valuing it in human food with a view to improving the nutritional quality of locally processed foods in Benin. To achieve this goal, a literature review was carried out between January and September 2020. The results revealed that whey contains more than 90% water. It also has a high content of lactose (75% of the dry matter), a low content of fat, soluble milk proteins (approximately 20% of total milk proteins) and various minerals. It also contains other components, such as citric acid and lactic acid, non-protein nitrogenous materials such as urea and uric acid and group B vitamins, mainly vitamin B1 (thiamine), vitamin B2 (riboflavin) and vitamin B6 (pyridoxine). Whey is exploited indirectly through its constituents in the food and pharmaceutical industry and also directly through the production of some variants of cheese.

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“…In this paper, important change in NF selectivity as affected by hydrodynamic conditions and recirculation time via possible peptide-peptide interactions occurring in the so-called weakly attached layer were reported. Roufik et al, (2007) showed that the hypotensive peptide -lactoglobulin ( -Lg) f142-148, known as lactokinin, bind to bovine -lactoglobulin variant A ( -Lg A) and this complex could delay the hydrolysis of this peptide by digestive enzymes.…”

Section: Bioactive Peptidesmentioning

confidence: 99%

Continuous Membrane Bioreactor (CMBR) to Produce Nanoparticles from Milk Components

Nieto-Nieto¹,

Amaya-Llano²,

Ozimek³

2012

Trends in Vital Food and Control Engineering

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Physicochemical characterization and in vitro digestibility of β-lactoglobulin/β-Lg f142-148 complexes

Cited by 13 publications

References 57 publications

Studies on the molecular recognition between bioactive peptides and angiotensin‐converting enzyme

Studies on the molecular recognition between bioactive peptides and angiotensin‐converting enzyme

Nutritional quality and use of whey in human food for its valorization

Continuous Membrane Bioreactor (CMBR) to Produce Nanoparticles from Milk Components

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