AI Chat Paper
Note: Please note that the following content is generated by AMiner AI. SciOpen does not take any responsibility related to this content.
{{lang === 'zh_CN' ? '文章概述' : 'Summary'}}
{{lang === 'en_US' ? '中' : 'Eng'}}
Chat more with AI
Powered by AMiner. Clicking this button will take you away from SciOpen.
Home Food Science and Human Wellness Article
PDF (722 KB)
Cite
EndNote(RIS) BibTeX
Collect
Submit Manuscript AI Chat Paper
Show Outline
Outline
Show full outline
Hide outline
Outline
Show full outline
Hide outline
Research Article | Open Access

Production of antihypertensive and antidiabetic peptide fractions from quinoa (Chenopodium quinoa Willd.) by electrodialysis with ultrafiltration membranes

Adrián González-Muñoza,b, Marion Vallec,d, Rotimi E. Alukoe, Laurent Bazinetc,f( ), Javier Enrionea,b( )
Biopolymer Research and Engineering Lab (BiopREL), School of Nutrition and Dietetics, Faculty of Medicine, Universidad de los Andes, Monseñor Álvaro del Portillo 12455, Chile
Centre for Biomedical Research and Innovation (CIIB), Universidad de los Andes, Chile, Monseñor Álvaro del Portillo 12455, Chile
Institute of Nutrition and Functional Foods (INAF), Université Laval, Québec QC G1V 0A6, Canada
Department of Anatomy and Physiology, Faculty of Medicine, Laval Hospital Research Center, Université Laval, Québec QC G1V 4G5, Canada
Department of Food and Human Nutritional Sciences, University of Manitoba, Winnipeg MB R3T 2N2, Canada
Department of Food Sciences, Laboratoire de Transformation Alimentaire et Procédés ÉlectroMembranaire (LTAPEM, Laboratory of Food Processing and Electro-Membrane Processes), Université Laval, Québec QC G1V 0A6, Canada

Peer review under responsibility of KeAi Communications Co., Ltd.

Show Author Information

Abstract

Processing bioactive peptides from natural sources using electrodialysis with ultrafiltration membranes (EDUF) have gained attention since it can fractionate in terms of their charge and molecular weight. Quinoa is a pseudo-cereal highlighted by its high protein content, amino acid profile and adapting growing conditions. The present work aimed at the production of quinoa peptides through fractionation using EDUF and to test the fractions according to antihypertensive and antidiabetic activity. Experimental data showed the production of peptides ranging between 0.4 and 1.5 kDa. Cationic (CQPF) (3.01%), anionic (AQPF) (1.18%) and the electrically neutral fraction quinoa protein hydrolysate (QPH)-EDUF (~95%) were obtained. In-vitro studies showed the highest glucose uptake modulation in L6 cell skeletal myoblasts in presence of QPH-EDUF and AQPF (17% and 11%) indicating potential antidiabetic activity. The antihypertensive effect studied in-vivo in spontaneously hypertensive rats (SHR), showed a decrease in systolic blood pressure in presence of the fractionated peptides, being 100 mg/kg a dose comparable to Captopril (positive control). These results contribute to the current knowledge of bioactive peptides from quinoa by reporting the relevance of EDUF as tool to produce selected peptide fractions. Nevertheless, further characterization is needed towards peptide sequencing, their respective role in the metabolism and scaling-up production using EDUF.

Keywords

AntidiabeticBioactive peptidesQuinoaElectrodialysis with ultrafiltration membranesAntihypertensive

References

[1]

N. Meyer, A. Reguant-Closa, Eat as if you could save the planet and win! Sustainability integration into nutrition for exercise and sport, Nutrients 9 (2017) 412-446. https://doi.org/10.3390/nu9040412.
Crossref Google Scholar
[2]

M. Hayes, Food proteins and bioactive peptides: new and novel sources, characterisation strategies and applications, Foods 7 (2018) 11-13. https://doi.org/10.3390/foods7030038.
Crossref Google Scholar
[3]

B. Zhu, H. He, T. Hou, A comprehensive review of corn protein-derived bioactive peptides: production, characterization, bioactivities, and transport pathways, Compr. Rev. Food Sci. Food Saf. 18 (2019) 329-345. https://doi.org/10.1111/1541-4337.12411.
Crossref Google Scholar
[4]

K.S. Bhullar, J. Wu, Dietary peptides in aging: evidence and prospects, Food Sci. Hum. Wellness 9 (2020) 1-7. https://doi.org/10.1016/j.fshw.2020.01.001.
Crossref Google Scholar
[5]

E.B.M. Daliri, B.H. Lee, D.H. Oh, Current trends and perspectives of bioactive peptides, Crit. Rev. Food Sci. Nutr. 58 (2018) 2273-2284. https://doi.org/10.1080/10408398.2017.1319795.
Crossref Google Scholar
[6]

P.B. Maffetone, I. Rivera-Dominguez, P.B. Laursen, Overfat adults and children in developed countries: the public health importance of identifying excess body fat, Front. Public Heal. 5 (2017) 190. https://doi.org/10.3389/fpubh.2017.00190.
Crossref Google Scholar
[7]

M. Saklayen, The global epidemic of metabolic syndrome, Curr. Hypertens. Rep. 20 (2018) 12. https://doi.org/10.1007/s11906-018-0812-z.
Crossref Google Scholar
[8]

H. Xu, X. Li, H. Adams, et al., Etiology of metabolic syndrome and dietary intervention, Int. J. Mol. Sci. 20 (2019) 128. https://doi.org/10.3390/ijms20010128.
Crossref Google Scholar
[9]

Y. Wu, Y. Ding, Y. Tanaka, et al., Risk factors contributing to type 2 diabetes and recent advances in the treatment and prevention, Int. J. Med. Sci. 11 (2014) 1185-1200. https://doi.org/10.7150/ijms.10001.
Crossref Google Scholar
[10]

P.G. Mora, E. Peñas, J. Frias, et al., High pressure-assisted enzymatic release of peptides and phenolics increase angiotensin converting enzyme I inhibitory and antioxidant activities of pinto bean hydrolysates, J. Agric. Food Chem. 64 (2016) 1730-1740. https://doi.org/10.1021/acs.jafc.5b06080.
Crossref Google Scholar
[11]

G.C.U. Marie, V. Perreault, L. Henaux, et al., Impact of a high hydrostatic pressure pretreatment on the separation of bioactive peptides from flaxseed protein hydrolysates by electrodialysis with ultrafiltration membranes, Sep. Purif. Technol. 211 (2019) 242-251. https://doi.org/10.1016/j.seppur.2018.09.063.
Crossref Google Scholar
[12]

T. Hatanaka, Y. Inoue, J. Arima, et al., Production of dipeptidyl peptidase Ⅳ inhibitory peptides from defatted rice bran, Food Chem. 134 (2012) 797-802. https://doi.org/10.1016/j.foodchem.2012.02.183.
Crossref Google Scholar
[13]

A. Connolly, M.B. O’Keeffe, A.B. Nongonierma, et al., Isolation of peptides from a novel brewers spent grain protein isolate with potential to modulate glycaemic response, Int. J. Food Sci. Technol. 52 (2017) 146-153. https://doi.org/10.1111/ijfs.13260.
Crossref Google Scholar
[14]

M. González-Montoya, B. Hernández-Ledesma, R. Mora-Escobedo, et al., Bioactive peptides from germinated soybean with anti-diabetic potential by inhibition of dipeptidylpeptidase-Ⅳ, α-amylase, and α-glucosidase enzymes, Int. J. Mol. Sci. 19 (2018) 2883-2897. https://doi.org/10.3390/ijms19102883.
Crossref Google Scholar
[15]

B.L. Graf, P. Rojas-Silva, L.E. Rojo, et al., Innovations in health value and functional food development of quinoa (Chenopodium quinoa Willd.), Compr. Rev. Food Sci. Food Saf. 14 (2015) 431-445. https://doi.org/10.1111/1541-4337.12135.
Crossref Google Scholar
[16]

M.I. González Martín, G. Wells Moncada, S. Fischer, et al., Chemical characteristics and mineral composition of quinoa by near-infrared spectroscopy, J. Sci. Food Agric. 94 (2014) 876-881. https://doi.org/10.1002/jsfa.6325.
Crossref Google Scholar
[17]

D. Bazile, S.E. Jacobsen, A. Verniau, The global expansion of quinoa: trends and limits, Front. Plant Sci. 7 (2016) 622. https://doi.org/10.3389/fpls.2016.00622.
Crossref Google Scholar
[18]

D. Orona-Tamayo, M.E. Valverde, O. Paredes-López, Bioactive peptides from selected latin american food crops – a nutraceutical and molecular approach, Crit. Rev. Food 59 (2018) 1949-1975. https://doi.org/10.1080/10408398.2018.1434480.
Crossref Google Scholar
[19]

R. Vilcacundo, B. Miralles, W. Carrillo, et al., In vitro chemopreventive properties of peptides released from quinoa (Chenopodium quinoa Willd.) protein under simulated gastrointestinal digestion, Food Res. Int. 105 (2018) 403-411. https://doi.org/10.1016/j.foodres.2017.11.036.
Crossref Google Scholar
[20]

Z. Shi, Y. Hao, C. Teng, et al., Functional properties and adipogenesis inhibitory activity of protein hydrolysates from quinoa (Chenopodium quinoa Willd.), Food Sci. Nutr. 7 (2019) 2103-2112. https://doi.org/10.1002/fsn3.1052.
Crossref Google Scholar
[21]

J. Capraro, S. De Benedetti, M. Di Dio, et al., Characterization of chenopodin isoforms from quinoa seeds and assessment of their potential anti-inflammatory activity in Caco-2 cells, Biomolecules 10 (2020) 795. https://doi.org/10.3390/biom10050795.
Crossref Google Scholar
[22]

J. Capraro, S. De Benedetti, G.C. Heinzl, et al., Bioactivities of pseudocereal fractionated seed proteins and derived peptides relevant for maintaining human well-being, Int. J. Mol. Sci. 29 (2021) 3543. https://doi.org/10.3390/ijms220073543.
Crossref Google Scholar
[23]

R.E. Aluko, E. Monu, Functional and bioactive properties of quinoa seed protein hydrolysates, J. Food Sci. 68 (2003) 1254-1258. https://doi.org/10.1111/j.1365-2621.2003.tb09635.x.
Crossref Google Scholar
[24]

Y. Zheng, X. Wang, Y. Zhuang, et al., 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, Molecules 24 (2019) 4562. https://doi.org/10.3390/molecules24244562.
Crossref Google Scholar
[25]

H. Guo, A. Richel, Y. Hao, et al., Novel dipeptidylpeptidase-Ⅳ and angiotensin-Ⅰ-converting enzyme inhibitory peptides released from quinoa protein by in silico proteolysis, Food Sci. Nutr. 8 (2020) 1415-1422. https://doi.org/10.1002/fsn3.1423.
Crossref Google Scholar
[26]

A.B. Nongonierma, S. Le Maux, C. Dubrulle, et al., Quinoa (Chenopodium quinoa Willd.) protein hydrolysates with in vitro dipeptidyl peptidase Ⅳ (DPP-Ⅳ) inhibitory and antioxidant properties, J. Cereal Sci. 65 (2015) 112-118. https://doi.org/10.1016/j.jcs.2015.07.004.
Crossref Google Scholar
[27]

R. Vilcacundo, C. Martínez-Villaluenga, B. Hernández-Ledesma, Release of dipeptidyl peptidase Ⅳ, α-amylase and α-glucosidase inhibitory peptides from quinoa (Chenopodium quinoa Willd.) during in vitro simulated gastrointestinal digestion, J. Funct. Foods 35 (2017) 531-539. https://doi.org/10.1016/j.jff.2017.06.024.
Crossref Google Scholar
[28]

L. Bazinet, L. Firdaous, Separation of bioactive peptides by membrane processes: technology and devices, Recent Patents Biotechnol. 7 (2013) 9-27. https://doi.org/10.2174/1872208311307010003.
Crossref Google Scholar
[29]

S. Suwal, C. Roblet, A. Doyen, et al., Electrodialytic separation of peptides from snow crab by-product hydrolysate: effect of cell configuration on peptide selectivity and local electric field, Sep. Purif. Technol. 127 (2014) 29-38. https://doi.org/10.1016/j.seppur.2014.02.018.
Crossref Google Scholar
[30]

C. Acquah, E. Di Stefano, C.C. Udenigwe, Role of hydrophobicity in food peptide functionality and bioactivity, J. Food Bioact. 4 (2018) 88-98. https://doi.org/10.31665/jfb.2018.4164.
Crossref Google Scholar
[31]

S. Suwal, É. Rozoy, M. Manenda, et al., Comparative study of in situ and ex situ enzymatic hydrolysis of milk protein and separation of bioactive peptides in an electromembrane reactor, ACS Sustain. Chem. Eng. 5 (2017) 5330-5340. https://doi.org/10.1021/acssuschemeng.7b00651.
Crossref Google Scholar
[32]

A. Doyen, C.C. Udenigwe, P.L. Mitchell, et al., Anti-diabetic and antihypertensive activities of two flaxseed protein hydrolysate fractions revealed following their simultaneous separation by electrodialysis with ultrafiltration membranes, Food Chem. 145 (2014) 66-76. https://doi.org/10.1016/j.foodchem.2013.07.108.
Crossref Google Scholar
[33]

C. Roblet, A. Doyen, J. Amiot, et al., Enhancement of glucose uptake in muscular cell by soybean charged peptides isolated by electrodialysis with ultrafiltration membranes (EDUF): activation of the AMPK pathway, Food Chem. 147 (2014) 124-130. https://doi.org/10.1016/j.foodchem.2013.09.108.
Crossref Google Scholar
[34]

J. White, R. Hart, J. Fry, An evaluation of the Waters Pico-Tag system for the amino-acid analysis of food materials, J. Autom. Chemis. 8 (1986) 170-177. https://doi.org/10.1155/s1463924686000330.
Crossref Google Scholar
[35]

M. del Mar Yust, M. del C. Millán-Linares, J.M. Alcaide-Hidalgo, et al., Hypocholesterolaemic and antioxidant activities of chickpea (Cicer arietinum L.) protein hydrolysates, J. Sci. Food Agric. 92 (2012) 1994-2001. https://doi.org/10.1002/jsfa.5573.
Crossref Google Scholar
[36]

P. Valencia, M. Pinto, S. Almonacid, Identification of the key mechanisms involved in the hydrolysis of fish protein by alcalase, Process Biochem. 49 (2014) 258-264. https://doi.org/10.1016/j.procbio.2013.11.012.
Crossref Google Scholar
[37]

M.E. Langevin, L. Bazinet, Ion-exchange membrane fouling by peptides: a phenomenon governed by electrostatic interactions, J. Memb. Sci. 369 (2011) 359-366. https://doi.org/10.1016/j.memsci.2010.12.031.
Crossref Google Scholar
[38]

L. Firdaous, P. Dhulster, J. Amiot, et al., Concentration and selective separation of bioactive peptides from an alfalfa white protein hydrolysate by electrodialysis with ultrafiltration membranes, J. Memb. Sci. 329 (2009) 60-67. https://doi.org/10.1016/j.memsci.2008.12.012.
Crossref Google Scholar
[39]

F. Tremblay, A. Marette, Amino acid and insulin signaling via the mTOR/p70 S6 kinase pathway. A negative feedback mechanism leading to insulin resistance in skeletal muscle cells, J. Biol. Chem. 276 (2001) 38052-38060. https://doi.org/10.1074/jbc.M106703200.
Crossref Google Scholar
[40]

M.B. O’Keeffe, R. Norris, M.A. Alashi, et al., Peptide identification in a porcine gelatin prolyl endoproteinase hydrolysate with angiotensin converting enzyme (ACE) inhibitory and hypotensive activity, J. Funct. Foods 34 (2017) 77-88.
Crossref Google Scholar
[41]

P. Garcia-Mora, E. Peñas, J. Frias, et al., Savinase, the most suitable enzyme for releasing peptides from lentil (Lens culinaris var. Castellana) protein concentrates with multifunctional properties, J. Agric. Food Chem. 62 (2014) 4166-4174. https://doi.org/10.1021/jf500849u.
Crossref Google Scholar
[42]

S. Medina-Godoy, D.L. Ambriz-Pérez, C.I. Fuentes-Gutiérrez, et al., Angiotensin-converting enzyme inhibitory and antioxidative activities and functional characterization of protein hydrolysates of hard-to-cook chickpeas, J. Sci. Food Agric. 92 (2012) 1974-1981. https://doi.org/10.1002/jsfa.5570.
Crossref Google Scholar
[43]

C.C. Udenigwe, A.P. Adebiyi, A. Doyen, et al., Low molecular weight flaxseed protein-derived arginine-containing peptides reduced blood pressure of spontaneously hypertensive rats faster than amino acid form of arginine and native flaxseed protein, Food Chem. 132 (2012) 468-475. https://doi.org/10.1016/j.foodchem.2011.11.024.
Crossref Google Scholar
[44]

R. Durand, E. Fraboulet, A. Marette, et al., Simultaneous double cationic and anionic molecule separation from herring T milt hydrolysate and impact on resulting fraction bioactivities, Sep. Purif. Technol. 210 (2019) 431-441. https://doi.org/10.1016/j.seppur.2018.08.017.
Crossref Google Scholar
[45]

C. Roblet, M.J. Akhtar, S. Mikhaylin, et al., Enhancement of glucose uptake in muscular cell by peptide fractions separated by electrodialysis with filtration membrane from salmon frame protein hydrolysate, J. Funct. Foods 22 (2016) 337-346. https://doi.org/10.1016/j.jff.2016.01.003.
Crossref Google Scholar
[46]

C.A. Ovando, J.C. de Carvalho, G.V. de Melo Pereira, et al., Functional properties and health benefits of bioactive peptides derived from Spirulina: a review, Food Rev. Int. 34 (2018) 34-51. https://doi.org/10.1080/87559129.2016.1210632.
Crossref Google Scholar
[47]

R.E. Aluko, Antihypertensive peptides from food proteins, Annu. Rev. Food Sci. Technol. 6 (2015) 235-262. https://doi.org/10.1146/annurev-food-022814-015520.
Crossref Google Scholar
[48]

L. Henaux, J. Thibodeau, G. Pilon, et al., How charge and triple size-selective membrane separation of peptides from Salmon protein hydrolysate orientate their biological response on glucose uptake, Int. J. Mol. Sci. 20 (2019) 1939. https://doi.org/10.3390/ijms20081939.
Crossref Google Scholar
[49]

S. Li, L. Liu, G. He, et al., Molecular targets and mechanisms of bioactive peptides against metabolic syndromes, Food Funct. 9 (2018) 42-52. https://doi.org/10.1039/c7fo01323j.
Crossref Google Scholar
[50]

R. Wa, M. Bradley, T. Elliott, Diabetes, metabolic syndrome and obesity: targets and therapy dovepress Akt/PKB activation and insulin signaling: a novel insulin signaling pathway in the treatment of type 2 diabetes metabolic dysfunction in type 2 diabetes, Diabetes, Metab. Syndr. Obes. Targets Ther. 7 (2014) 55-64. http://dx.doi.org/10.2147/DMSO.S48260.
Crossref Google Scholar
[51]

J.J. Song, Q. Wang, M. Du, et al., Casein glycomacropeptide-derived peptide IPPKKNQDKTE ameliorates high glucose-induced insulin resistance in HepG2 cells via activation of AMPK signaling, Mol. Nutr. Food Res. 61 (2016) 1600301. https://doi.org/10.1002/mnfr.201600301.
Crossref Google Scholar
[52]

C. Lammi, C. Zanoni, A. Arnoldi, Three peptides from soy glycinin modulate glucose metabolism in human hepatic HepG2 cells, Int. J. Mol. Sci. 16 (2015) 27362-27370. https://doi.org/10.3390/ijms161126029.
Crossref Google Scholar
[53]

H. Guo, Y. Hao, A. Richel, et al., Antihypertensive effect of quinoa protein under simulated gastrointestinal digestion and peptide characterization, J. Sci. Food Agric. 100 (2020) 5569-5576. https://doi.org/https://doi.org/10.1002/jsfa.10609.
Crossref Google Scholar
[54]

S.A. Malomo, J.O. Onuh, A.T. Girgih, et al., Structural and antihypertensive properties of enzymatic hemp seed protein hydrolysates, Nutrients 7 (2015) 7616-7632. https://doi.org/10.3390/nu7095358.
Crossref Google Scholar
Food Science and Human Wellness
Volume 11 Issue 6,
November 2022
Pages 1650-1659
DOI: 10.1016/j.fshw.2022.06.024
Cite this article:
González-Muñoz A, Valle M, Aluko RE, et al. Production of antihypertensive and antidiabetic peptide fractions from quinoa (Chenopodium quinoa Willd.) by electrodialysis with ultrafiltration membranes. Food Science and Human Wellness, 2022, 11(6): 1650-1659. https://doi.org/10.1016/j.fshw.2022.06.024

381

Views

28

Downloads

11

Crossref

11

Web of Science

12

Scopus

0

CSCD

Altmetrics
Received: 30 August 2021
Revised: 18 October 2021
Accepted: 23 November 2021
Published: 18 July 2022
© 2022 Beijing Academy of Food Sciences.

This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
Return