Obtaining of peptides with in vitro antioxidant and angiotensin I converting enzyme inhibitory activities from cañihua protein (Chenopodium pallidicaule Aellen)

Chirinos, Rosana; Ochoa, Karina; Aguilar‐Galvez, Ana; Carpentier, Sébastien; Pedreschi, Romina; Campos, David

doi:10.1016/j.jcs.2018.07.004

Cited by 31 publications

(49 citation statements)

References 27 publications

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“…Ren et al (2014) reported that pretreatment with fixed-frequency ultrasound at 40 kHz increased the ACE-inhibitory activity of zein hydrolysate by 97% compared to the control. The values of IC 50 found in this investigation are within the range (56 -1140 μg/mL) reported for protein concentrates from other plant sources, such as Phaseolus lunatus, Phaseolus vulgaris, chickpea seed, green soybeans, cañihua and oats (Torruco-Uco et al, 2009;Hanafi et al, 2018;Chirinos et al, 2018;Gupta and Bhagyawant, 2018;Wang et al, 2015). Therefore, it can be concluded that the ultrasonic pretreatment effectively increased the ACE-inhibitory activity of hydrolysed peptides from Erythrina edulis protein.…”

Section: Effect Of Ultrasound Pretreatment On Ace-inhibitory Activitysupporting

confidence: 82%

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Effect of ultrasound pretreatment on the antioxidant capacity and antihypertensive activity of bioactive peptides obtained from the protein hydrolysates of Erythrina edulis

et al. 2019

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The aim of this research was to evaluate the effect of ultrasound pretreatment on enzymatic hydrolysis with Flavourzyme® and Alcalase® enzymes and the ACE-inhibitory activity and the antioxidant capacity of protein hydrolysates of Erythrina edulis. A protein concentration of 78.8% was obtained after sonicating the protein solutions (10%, w/v) for 10 min at 80 kHz and 100% amplitude. The ultrasonic pretreatment (UP) increased the degree of hydrolysis (47.7%) up to 70 min, the IC50 values in both samples [with (UP) and without pretreatment (WP)] were 100 μg/mL, and the UP samples presented the highest percentage of inhibition at 57.3%. The UP hydrolysates showed the highest (p < 0.05) antioxidant (ABTS*) and radical (DPPH*) - scavenging activities, with IC50 values ranging from 64.52 to 77.62 μg/mL and from 151.13 to 173.22 μg/mL, respectively. In SDS-PAGE, the hydrolysates UP exhibited low molecular weight bands (8 - 20 kDa). The results of both, antioxidants and antihypertensive activities obtained in vitro, showed a higher percentage of activity for the peptides obtained after pretreatment with ultrasound than for those obtained without the use of ultrasound prior to enzymatic hydrolysis.

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Section: Effect Of Ultrasound Pretreatment On Ace-inhibitory Activitysupporting

confidence: 82%

“…However, alternatives that increase these activities have been sought. The sequential hydrolysis increases the degree of protein hydrolysis as shown by Chirinos et al (2018). Hydrolysates were obtained via enzymatic hydrolysis using food grade enzymes.…”

Section: Introductionmentioning

confidence: 99%

Effect of ultrasound pretreatment on the antioxidant capacity and antihypertensive activity of bioactive peptides obtained from the protein hydrolysates of Erythrina edulis

et al. 2019

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“…Quinoa bran albumin was digested according to the method indicated by Chirinos et al [9] with some modifications. Briefly, the quinoa bran albumin (dissolved in dH 2 O, 2 g/100 mL) was hydrolyzed by two enzymes in the following sequence-alcalase (45 • C, pH 9.0, 100 U/g protein, 1 h) and trypsin (37 • C, pH 7.0, 60 U/g protein, 30 min).…”

Section: Preparation Of Quinoa Bran Albumin Hydrolysates (Qbah)mentioning

confidence: 99%

“…Until now, many studies have reported the purification, identification, and characterization of antioxidant and ACE inhibition peptides from animal proteins as well as plant and marine proteins. However, the number of studies focused on their in vivo antihypertension, structural bioinformatics, bioavailability, and action mechanism is limited [3,[7][8][9][10][11].…”

Section: Introductionmentioning

confidence: 99%

Isolation of Novel ACE-Inhibitory and Antioxidant Peptides from Quinoa Bran Albumin Assisted with an In Silico Approach: Characterization, In Vivo Antihypertension, and Molecular Docking

et al. 2019

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Albumin is the major fraction of quinoa protein that is characterized as having high nutritional value. However, until now, scant information is available on the bioactivity of quinoa albumin or its hydrolysates. To promote its usage, we extracted albumin in this study from quinoa bran assisted with cellulase and hemicellulose, and hydrolyzed it by alcalase and trypsin to produce bioactive peptides. The hydrolysates (QBAH) were purified by gel filtration and reversed-phase high-performance liquid chromatography (RP-HPLC), followed by identification using liquid chromatography-mass spectrometry (LC-MS/MS). Furthermore, based on in silico analysis, one angiotensin-I converting enzyme (ACE)-inhibitory and antioxidant peptide, RGQVIYVL (946.6 Da), and two antioxidant peptides, ASPKPSSA (743.8 Da), and QFLLAGR (803.5 Da), from QBAH were synthesized. RGQVIYVL showed a high ACE-inhibitory activity (IC 50 = 38.16 µM) with competitive mode of inhibition, and showed significant antihypertensive effect in spontaneously hypertensive rats at a concentration of 100-150 mg/kg body weight (bw). Molecular docking simulation showed that it could interact with the active ACE site via hydrogen bonds with high binding power. Moreover, RGQVIYVL, ASPKPSSA, and QFLLAGR all demonstrated high ·OH scavenging activity (IC 50 = 61.69-117.46 µM), ABTS + scavenging activity (58.29-74.28%) and Fe 2+ chelating ability (32.54-82.48% at 0.5 mg/mL). They could also retain activity after gastrointestinal enzyme digestion. These results indicate that quinoa albumin is a potential source of bioactive peptides possessing antioxidant and ACE-inhibitory activities.

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“…The IC 50 value of 0.647 mg/ml determined also suggests WGPH as an attractive source of ACE‐inhibitory peptides. The ability of WGPH to inhibit ACE is thus related to particular amino acid compositions of WGPH peptides, in turn depending on the proteolytic activity (Chirinos et al, ).…”

Section: Resultsmentioning

confidence: 99%

Identification and synthesis of multifunctional peptides from wheat germ hydrolysate fractions obtained by proteinase K digestion

et al. 2019

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Wheat germ protein hydrolysate (WGPH) was obtained by proteinase K digestion, in order to produce bioactive antioxidant and antihypertensive peptides. Response surface methodology (RSM) was used to optimize hydrolysis conditions (enzyme‐to‐substrate ratio, time, and temperature) for antioxidant activity of hydrolysates. The crude WGPH produced in this way significantly inhibited angiotensin‐I converting enzyme (ACE) in a concentration‐dependent manner. It was next fractionated by reversed‐phase semi‐preparative High Performance Liquid Chromatography (HPLC) into 12 fractions that were examined for antioxidant and antihypertensive activities. Fractions with antioxidant and ACE‐inhibitory activities were then submitted to further analysis by nano‐LC‐ESI‐MS‐MS. Among the various peptides identified, MDATALHYENQK (IC50: 293.3 ± 6.5 µg/ml) and SGGSYADELVSTAK (IC50: 265.5 ± 8.3 µg/ml) displayed antioxidant activity and VALTGDNGHSDHVVHF (IC50: 189.3 ± 4.05 µg/ml), VDSLLTAAK (IC50: 159.7 ± 0.33 µg/ml), MDATALHYENQK (IC50: 303.6 ± 2.47 µg/ml), IGGIGTVPVGR (IC50: 125.7 ± 2.3 µg/ml) and SGGSYADELVSTAK (IC50: 128.2 ± 1.17 µg/ml) showed good ACE‐inhibitory activity. Practical applications Wheat milling industries produce massive amounts of wheat germ as by‐product that can be converted into valuable compounds. The present research indicates that proteinase K is useful to hydrolyze wheat germ proteins in a search for bioactive peptides with antioxidant and ACE‐inhibitory properties. The identified peptides can be regarded as functional food additives, or nutraceuticals to improve human health.

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Obtaining of peptides with in vitro antioxidant and angiotensin I converting enzyme inhibitory activities from cañihua protein (Chenopodium pallidicaule Aellen)

Cited by 31 publications

References 27 publications

Effect of ultrasound pretreatment on the antioxidant capacity and antihypertensive activity of bioactive peptides obtained from the protein hydrolysates of Erythrina edulis

Effect of ultrasound pretreatment on the antioxidant capacity and antihypertensive activity of bioactive peptides obtained from the protein hydrolysates of Erythrina edulis

Isolation of Novel ACE-Inhibitory and Antioxidant Peptides from Quinoa Bran Albumin Assisted with an In Silico Approach: Characterization, In Vivo Antihypertension, and Molecular Docking

Identification and synthesis of multifunctional peptides from wheat germ hydrolysate fractions obtained by proteinase K digestion

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