Inhibition of dipeptidyl peptidase IV by enzymatic hydrolysates derived from primary and secondary whey of fresh and Oaxaca cheeses

Mares-Mares, Everardo; Barboza‐Corona, José E.; Sosa‐Morales, María Elena; Gutiérrez-Chávez, Abner Josué; Gutiérrez-Vargas, Santiago; León-Galván, Ma. Fabiola

doi:10.1111/1471-0307.12623

Cited by 3 publications

(1 citation statement)

References 31 publications

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“…Adjonu et al (2013) treated whey protein with preheating treatments and protease hydrolysis to obtain doubly active peptides with antioxidant and ACE inhibitory abilities. Researchers (Mares‐Mares et al, 2019; Nongonierma et al, 2017) obtained peptides displaying ACE inhibitory and DPP‐IV inhibitory activities through the preparation of zymolytic whey protein. At present, the research regarding the preparation of peptides with double activities from whey proteins have generally focused on the combination of ACE inhibitory and DPP‐IV inhibitory activities, as well as the combination of ACE inhibitory and antioxidant activities.…”

Section: Introductionmentioning

confidence: 99%

The purification and identification of antioxidants and dipeptidyl peptidase IV inhibitory peptides from whey protein hydrolysates

Yuanrong

Jiakun

Liu

2022

Food Bioengineering

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In the present study, whey protein was enzymatically hydrolyzed using an ultrahigh‐pressure synergistic enzymolysis method. The antioxidant activities and DPP‐IV inhibitory activities of the enzymatic hydrolysates were measured. Three‐layer isolation and purification were conducted on the enzymatic hydrolysates with antioxidant activity and DPP‐IV inhibitory activity by gel filtration chromatography and RP‐HPLC. The amino acid sequences were determined by LC‐MS/MS. The identified amino acid sequences were then synthesized, and their antioxidants and DPP‐IV inhibitory activities were determined. The results showed that 3 of the 14 polypeptides of N3‐8 exhibited high antioxidant activity. Among them, peptide DDQNPHSSN had both high antioxidant activity and DPP‐IV inhibitory activity. When the concentration was 1 mg/mL, then the ABTS radical scavenging rate, DPPH radical scavenging rate and reducing power were prominent, reaching 91.42%, 88.76%, and 0.637%, respectively, and DPP‐IV inhibitory activity reached 66.28%. Whey protease hydrolysates are expected to be commercially developed as functional peptides.

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Section: Introductionmentioning

confidence: 99%

The purification and identification of antioxidants and dipeptidyl peptidase IV inhibitory peptides from whey protein hydrolysates

Yuanrong

Jiakun

Liu

2022

Food Bioengineering

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Diabetes and seeds: New horizon to promote human nutrition and anti-diabetics compounds in grains by germination

Maleki

Razavi

Yadav

2022

Critical Reviews in Food Science and Nutrition

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Anti-Diabetic Activity of Whey Proteins

Agarkova

Ryazantseva

Кручинин

2020

Food Processing: Techniques and Technology

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Absract. Introduction. With the advent of membrane filtration technologies, milk whey stopped being a “by-product” of cheese, cottage cheese, and casein production. The combination of various whey-processing technologies, e.g. enzymatic hydrolysis and membrane fractionation, made it possible to obtain concentrates, isolates, and hydrolysates of whey proteins with various biologically active effects. Study objects and methods. The article features research results of Russian and foreign scientific teams in the development of functional antidiabetic ingredients from hydrolyzed proteins of milk and whey. Results and discussion. According to foreign studies, Ile-Pro-Ile (diprotin A) with an IC50 value of 4.7 μM is one of the most effective low molecular mass peptides with an inhibitory potential against DPP-IV. Various studies of trypsin hydrolysis of β-lactoglobulin described the production of IPAVF peptide fragment with the most potent inhibitory activity of DPP-IV (IC50 = 44.7 μM). Other studies featured pepsin-treated lactoglobulin production of fragments LKPTPEGDL and LKPTPEGDLEIL with inhibitory activity DPP-IV IC50 = 45 and 57 μM, respectively. A number of studies described similar fragments obtained by the sequential action of the enzyme preparation Neutrase 0.8 LTM on β-lactoglobulin, followed by pepsin hydrolysis. As for the hydrolysis of α-lactalbumin with pepsin, scientists identified peptides WLAHKALCSEKLDQ, LAHKALCSEKL, and TKCEVFRE. They revealed a high inhibitory potential against DPP-IV (IC50 = 141, 165, and 166 μM, respectively). Tryptic hydrolysates of bovine β-lactoglobulin proved to be able to inhibit DPP-IV in vitro (IC50 of 210 μM). Peptide VAGTWY was the major compound responsible for this effect, displaying an IC50 of 174 μM. In other research, tryptic hydrolysate inhibited DPP-IV with an IC50 value of 1.6 mg/mL, also demonstrating antioxidant and ACE-inhibitory activities. This hydrolysate became source of VAGTWY, the most potent DPP-IV inhibitor (IC50 of 74.9 μM). Conclusion. An analysis of Russian and foreign studies proved that milk protein hydrolysis has a great potential for antidiabetic additives used in the treatment of type II diabetes. This are requires further research in order to define the safety of biologically active peptides.

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Inhibition of dipeptidyl peptidase IV by enzymatic hydrolysates derived from primary and secondary whey of fresh and Oaxaca cheeses

Cited by 3 publications

References 31 publications

The purification and identification of antioxidants and dipeptidyl peptidase IV inhibitory peptides from whey protein hydrolysates

The purification and identification of antioxidants and dipeptidyl peptidase IV inhibitory peptides from whey protein hydrolysates

Diabetes and seeds: New horizon to promote human nutrition and anti-diabetics compounds in grains by germination

Anti-Diabetic Activity of Whey Proteins

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