Rational design of enzyme compositions for the production of functional hydrolysates of cow milk whey proteins

Týčová, Anna; Ryazantseva, К.А.; Agarkova, E.Yu.; Кручинин, А.Г.; Tsentalovich, Mikhail; Федорова, Т. В.

doi:10.1134/s0003683817060138

Cited by 28 publications

(17 citation statements)

References 28 publications

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“…The in vitro antioxidant activity in WSEs was determined by the oxygen radical absorbance capacity fluorescence method (ORAC) using a Synergy 2 microplate photometer–fluorometer as described in Ref. [ 13 ]. The peroxyl radical was generated directly in the reaction medium during the thermal decomposition of the azo compound 2,2′-azobis (2-methylpropionamidine) dihydrochloride (AAPH, Sigma-Aldrich, St. Louis, MO, USA), initiated by incubation at 37 °C for 10 min.…”

Section: Methodsmentioning

confidence: 99%

Development of Antioxidant and Antihypertensive Properties during Growth of Lactobacillus helveticus, Lactobacillus rhamnosus and Lactobacillus reuteri on Cow’s Milk: Fermentation and Peptidomics Study

Begunova

Savinova

Glazunova

et al. 2020

Foods

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Bioactive peptides derived from milk proteins are an active research area. Exhibiting numerous positive physiological effects on digestive, cardiovascular, immune and nervous systems, these peptides thought to be one of the most promising ingredients for functional food. Generally, these peptides are inactive within the parent proteins and can be liberated during milk fermentation by the specific proteolytic systems of various Lactobacillus spp. Here we present the study of milk fermentation by Lactobacillus helveticus NK1, Lactobacillus rhamnosus F and Lactobacillus reuteri LR1 strains. It was demonstrated that the antioxidant activity of the milk fermented by these strains concomitantly increased with the strains’ proteolytic activity. For the angiotensin I-converting enzyme (ACE) inhibitory activity, the same tendency was not observed. Although the proteolytic activity of L. helveticus NK1 was two times higher than that of L. rhamnosus F, the milk fermented by these strains showed comparable ACE inhibition. The analysis of the peptide profiles of the fermented milk samples allowed us to hypothesize that some previously unreported peptides can be produced by L. rhamnosus F. In addition, it was demonstrated that these potential ACE-inhibiting peptides originated from the C-terminus of αS2-casein.

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Section: Methodsmentioning

confidence: 99%

Development of Antioxidant and Antihypertensive Properties during Growth of Lactobacillus helveticus, Lactobacillus rhamnosus and Lactobacillus reuteri on Cow’s Milk: Fermentation and Peptidomics Study

Begunova

Savinova

Glazunova

et al. 2020

Foods

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“…Previous study revealed that hydrolysis with alcalase, flavourzyme, and/or trypsin facilitated the release of more ACE‐inhibitory peptides from original proteins. For alcalase and trypsin (endopeptidases), it tends to cleave peptide bonds binding to aromatic amino acids (Phe, Tyr, and Trp) or uncharged branched amino acid residues (Ile, Val, and Leu); while flavourzyme (endo‐ and exopeptidase) prefers to hydrolyze bonds linked hydrophobic amino acid residues (Rao et al., 2012; Torkova et al., 2017). Consequently, the exposed hydrophobic amino acids especially the aromatic acid and branched amino acid residues at the C ‐terminal tripeptide can significantly improve the ACE‐inhibitory activity of the produced peptides (Lee & Hur, 2017).…”

Section: Resultsmentioning

confidence: 99%

Isolation of novel ACE‐inhibitory peptide from naked oat globulin hydrolysates in silico approach: Molecular docking, in vivo antihypertension and effects on renin and intracellular endothelin‐1

Zheng

Wang

Zhuang

et al. 2020

Journal of Food Science

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Naked oat globulin was hydrolyzed by alcalase, flavourzyme, pepsin, and trypsin in sequence. The hydrolysates (NOGH) were purified using gel chromatography, reversed-phase high performance liquid chromatography (RP-HPLC). Finally, fraction D7d with the highest ACE-inhibitory was subjected to liquid chromatography-mass spectrometry analysis and 14 peptides were identified. Of which, peptide SSYYPFK (890.4 Da) was chose to synthesize based on in silico analysis. The SSYYPFK demonstrated high ACE-inhibitory activity (IC 50 : 91.82 µM) with competitive inhibition mode, and could effectively (P < 0.05) lower the systolic blood pressure and diastolic pressure of spontaneously hypertensive rats at the concentration of 100 to 150 mg/kg body weight. Molecular docking simulation demonstrated that SSYYPFK could bind with the active site S1 of ACE via short hydrogen bonds. It could remain the ACE-inhibitory activity after simulated gastrointestinal hydrolysis. Moreover, SSYYPFK showed acceptable renin and endothelin-1 suppressing capacity (47.59% and 27.88% at 1.5 mg/mL, respectively). These results indicated that SSYYPFK may have similar antihypertensive mechanism with captopril, and could be develop to natural antihypertensive products.Practical Application: One novel ACE-inhibitory peptide SSYYPFK (890.4 Da) was identified from naked oat globulin hydrolysates. It exhibited relatively high renin and intracellular endothelin-1 suppressing capacity, and could effectively (P < 0.05) lower the systolic blood pressure and diastolic pressure of spontaneously hypertensive rats. This peptide could be used as natural and safe nutraceuticals and/or functional ingredients.Additional supporting information may be found online in the Supporting Information section at the end of the article. Supplementary Table S1. Body weight (g) of the spontaneous hypertensive rats administrated with peptide SSYYPFK a Supplementary Table S2. Heart rate of the spontaneous hypertensive rats administrated with peptide SSYYPFK a

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“…It should be noted that the inhibition of ACE is performed by hydrophobic peptides that exert high affinity toward the active site of ACE [35]. In our previous study [25], it was shown that most of the proposed hypotensive peptides found in the hydrolyzed whey from Montasio cheese contain hydrophobic amino acid residues, including proline in the central position. Previously, Zeeb et al [36] reported that pectin can reduce the bitter taste of plant-derived proteins.…”

Section: In Vitro Antioxidant and Acei Activities Of Mousse Samplesmentioning

confidence: 97%

“…Enzymatic hydrolysis of whey from hard Montasio cheese was conducted under the previously selected conditions [25]: Protamex (Novozymes A/S, Bagsvaerd, Denmark) and Alcalase (Novozymes A/S, Bagsvaerd, Denmark) enzyme preparations (3:1 ratio, wt% of the protein content), 90 min reaction time, pH 7.0, and a temperature of 50 • C. The degree of hydrolysis was 12%.…”

Section: Hydrolysis Of Cheese Wheymentioning

confidence: 99%

“…One sample was prepared according to a commercial recipe, and the other four with the replacement of 25%, 50%, 75% and 100% of cow's milk by a Montasio cheese WPH. In our previous studies [25], the composition of this whey was characterized (19% α-lactalbumin, 56% β-lactoglobulin and 11% κ-casein), and the presence of peptides with potential antioxidant and ACEI activities in its hydrolysate was demonstrated.…”

Section: In Vitro Antioxidant and Acei Activities Of Mousse Samplesmentioning

confidence: 99%

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Whey Protein Hydrolysate and Pumpkin Pectin as Nutraceutical and Prebiotic Components in a Functional Mousse with Antihypertensive and Bifidogenic Properties

et al. 2019

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Systematical consumption of functional products has a significant positive effect on health and can reduce the risk of diseases. The aim of this study was to investigate the possibility of using whey protein hydrolysate (WPH) and pumpkin pectin as ingredients in a functional mousse, to evaluate the mousse’s antioxidant and hypotensive activities in vitro, and to evaluate the effect of the long-term intake of mousse samples on the progression of hypertension in spontaneously hypertensive rats (SHRs) and on the microbiome status in Wistar rats with antibiotic-induced dysbiosis. The experimental mousse’s in vitro antioxidant activity (oxygen radical absorbance capacity) increased by 1.2 times. The hypotensive (angiotensin-1-converting enzyme inhibitory) activity increased by 6 times in comparison with a commercial mousse. Moreover, the addition of pectin allowed the elimination of the bitter aftertaste of WPH. In vivo testing confirmed the hypotensive properties of the experimental mousse. The systolic blood pressure in SHRs decreased by 18 mmHg and diastolic blood pressure by 12 mmHg. The experimental mousse also showed a pronounced bifidogenic effect. The Bifidobacterium spp. population increased by 3.7 times in rats orally administered with the experimental mousse. The results of these studies confirm that WPH and pumpkin pectin are prospective ingredients for the development of functional mousses.

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Rational design of enzyme compositions for the production of functional hydrolysates of cow milk whey proteins

Cited by 28 publications

References 28 publications

Development of Antioxidant and Antihypertensive Properties during Growth of Lactobacillus helveticus, Lactobacillus rhamnosus and Lactobacillus reuteri on Cow’s Milk: Fermentation and Peptidomics Study

Development of Antioxidant and Antihypertensive Properties during Growth of Lactobacillus helveticus, Lactobacillus rhamnosus and Lactobacillus reuteri on Cow’s Milk: Fermentation and Peptidomics Study

Isolation of novel ACE‐inhibitory peptide from naked oat globulin hydrolysates in silico approach: Molecular docking, in vivo antihypertension and effects on renin and intracellular endothelin‐1

Whey Protein Hydrolysate and Pumpkin Pectin as Nutraceutical and Prebiotic Components in a Functional Mousse with Antihypertensive and Bifidogenic Properties

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