Characterization of peptides from common bean protein isolates and their potential to inhibit markers of type-2 diabetes, hypertension and oxidative stress

Journal of the Science of Food and Agriculture

Volumn 97, Issue 8, 2017, Pages 2401-2410

  Mojica, Luis ^a,b   Luna Vital, Diego A ^a,c   González de Mejía, Elvira ^a  

^a UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

^b CENTRO DE INVESTIGACIÓN Y ASISTENCIA EN TECNOLOGÍA Y DISEÑO DEL ESTADO DE JALISCO   (Mexico)

^c UNIVERSIDAD AUTÓNOMA DE QUERÉTARO   (Mexico)

Author keywords

ACE inhibition; antioxidant capacity; bioactive peptides; common beans; DPP IV inhibition; glucosidase inhibition

Indexed keywords

ALPHA GLUCOSIDASE; ANTIOXIDANT; DIPEPTIDYL CARBOXYPEPTIDASE INHIBITOR; DIPEPTIDYL PEPTIDASE IV; DIPEPTIDYL PEPTIDASE IV INHIBITOR; PEPTIDE; PLANT PROTEIN;

CHEMISTRY; DRUG EFFECTS; HYPERTENSION; METABOLISM; NON INSULIN DEPENDENT DIABETES MELLITUS; OXIDATIVE STRESS; PHASEOLUS;

ALPHA-GLUCOSIDASES; ANGIOTENSIN-CONVERTING ENZYME INHIBITORS; ANTIOXIDANTS; DIABETES MELLITUS, TYPE 2; DIPEPTIDYL PEPTIDASE 4; DIPEPTIDYL-PEPTIDASE IV INHIBITORS; HYPERTENSION; OXIDATIVE STRESS; PEPTIDES; PHASEOLUS; VEGETABLE PROTEINS;

EID: 85018953186     PISSN: 00225142     EISSN: 10970010     Source Type: Journal    
DOI: 10.1002/jsfa.8053     Document Type: Article

References (48)

1. American Diabetes Association, Statistics About Diabetes. [Online]. Available: http://www.diabetes.org/ [9 September 2014].
2. Drucker DJ, Enhancing the action of incretin hormones: a new whey forward? Endocrinology 147:3171–3172 (2006).
3. Nongonierma AB and FitzGerald RJ, Dipeptidyl peptidase IV inhibitory and antioxidative properties of milk protein-derived dipeptides and hydrolysates. Peptides 39:157–163 (2013).
4. Kobayashi D, Takamura M, Murai H, Usui S, Ikeda T, Inomata J et al., Effect of pioglitazone on muscle sympathetic nerve activity in type 2 diabetes mellitus with alpha-glucosidase inhibitor. Auton Neurosci 158:86–91 (2010).
5. Centers for Disease Control and Prevention, Heart Disease and Stroke Fact Sheets. [Online]. Available: http://www.cdc.gov/ [12 August 2014].
6. Sowers JR, Epstein M and Frohlich ED, Diabetes, hypertension and cardiovascular disease, an update. Hypertension 37:1053–1059 (2001).
7. Kearney PM, Whelton M, Reynolds K, Whelton PK and He J, Worldwide prevalence of hypertension: a systematic review. J Hypertens 22:11–19 (2004).
8. Anthony CS, Masuyer G, Sturrock ED and Acharya KR, Structure based drug design of angiotensin-I converting enzyme inhibitors. Curr Med Chem 19:845–855 (2012).
9. Roffman DS, High- versus low-dose ACE inhibitor therapy in chronic heart failure. Ann Pharmacother 38:831–838 (2004).
10. Gavras H and Gavras I, Angiotensin converting enzyme inhibitors. Properties and side effects. Hypertension 11:II37–II41 (1988).
11. Giacco F and Brownlee M, Oxidative stress and diabetic complications. Circ Res 107:1058–1070 (2010).
12. Girgih AT, Chao D, Lin L, He R, Jung S and Aluko RE, Enzymatic protein hydrolysates from high pressure-pretreated isolated pea proteins have better antioxidant properties than similar hydrolysates produced from heat pretreatment. Food Chem 188:510–516 (2015).
13. Xue Z, Wen H, Zhai L, Yu Y, Li Y, Yu W et al., Antioxidant activity and anti-proliferative effect of a bioactive peptide from chickpea (Cicer arietinum L.). Food Res Int 77:75–81 (2015).
14. Garcia-Mora P, Peñas E, Frias J, Gomez R and Martinez-Villaluenga C, High-pressure improves enzymatic proteolysis and the release of peptides with angiotensin I converting enzyme inhibitory and antioxidant activities from lentil proteins. Food Chem 171:224–232 (2015).
15. Luna-Vital DA, Mojica L, González de Mejía E, Mendoza S and Loarca-Piña G, Biological potential of protein hydrolysates and peptides from common bean (Phaseolus vulgaris L.): a review. Food Res Int 76:39–50 (2015).
16. Capriotti AL, Caruso G, Cavaliere C, Samperi R, Ventura S, Chiozzi RZ et al., Identification of potential bioactive peptides generated by simulated gastrointestinal digestion of soybean seeds and soy milk proteins. J Food Compos Anal 44:205–213 (2015).
17. Sarmadi H and Ismail A, Antioxidative peptides from food proteins: a review. Peptides 31:1949–1956 (2010).
18. Lacroix IME and Li-Chan ECY, Overview of food products and dietary constituents with antidiabetic properties and their putative mechanisms of action: a natural approach to complement pharmacotherapy in the management of diabetes. Mol Nutr Food Res 58:61–78 (2014).
19. Oseguera-Toledo ME, González de Mejía E, Dia VP and Amaya-Llano SL, Common bean (Phaseolus vulgaris L.) hydrolysates inhibit inflammation in LPS-induced macrophages through suppression of NF-κB pathways. Food Chem 127:1175–1185 (2011).
20. Megías C, Yust M, Pedroche J, Lquari H, Girón-Calle J, Alaiz M et al., Purification of an ACE inhibitory peptide after hydrolysis of sunflower (Helianthus annuus L.) protein isolates. J Agric Food Chem 52:1928–1932 (2004).
21. Luna-Vital DA, González de Mejía E, Dia VP and Loarca-Piña G, Peptides in common bean fractions inhibit human colorectal cancer cells. Food Chem 157:347–355 (2014).
22. FL)) of plasma and other biological and food samples. J Agric Food Chem 51:3273–3279 (2003).
23. Luna-Vital DA, González de Mejía E, Mendoza S and Loarca-Piña G, Peptides present in the non-digestible fraction of common beans (Phaseolus vulgaris L.) inhibit the angiotensin-I converting enzyme by interacting with its catalytic cavity independent of their antioxidant capacity. Food Funct 6:1470–1479 (2015).
24. Montoya C, Lalles J, Beebe S and Leterme P, Phaseolin diversity as a possible strategy to improve the nutritional value of common beans. Food Res Int 43:443–449 (2010).
25. Almeida PF and Pokornym A, Mechanisms of antimicrobial, cytolytic, and cell-penetrating peptides: from kinetics to thermodynamics. Biochemistry 48:8083–8093 (2009).
26. Betancur-Ancona D, Sosa-Espinoza T, Ruiz-Ruiz J, Segura-Campos M and Chel-Guerrero L, Enzymatic hydrolysis of hard-to-cook bean (Phaseolus vulgaris L.) protein concentrates and its effects on biological and functional properties. Int J Food Sci Technol 49:2–8 (2014).
27. Mohamed S, Functional foods against metabolic syndrome (obesity, diabetes, hypertension and dyslipidemia) and cardiovascular disease. Trends Food Sci Technol 35:114–128 (2014).
28. Jin S, Wu Y, Deng S, Zhang J and Chen XQ, Oxidants and antioxidants in metabolic syndrome and cancer. Oxid Med Cell Longevity 2014:178962 (2014).
29. Frostegård J, Wu R, Lemne C, Thulin T, Witztum JL and de Faire U, Circulating oxidized low-density lipoprotein is increased in hypertension. Clin Sci 105:615–620 (2003).
30. Velarde-Salcedo AJ, Barrera-Pacheco A, Lara-González S, Montero-Morán GM, Díaz-Gois A, González de Mejía E et al., In vitro inhibition of dipeptidyl peptidase IV by peptides derived from the hydrolysis of amaranth (Amaranthus hypochondriacus L.) proteins. Food Chem 136:758–764 (2013).
31. Mojica L, Chen K and González de Mejía, E, Impact of commercial precooking of common bean (Phaseolus vulgaris) on the generation of peptides, after pepsin–pancreatin hydrolysis, capable to inhibit dipeptidyl peptidase-IV. J Food Sci 80:H188–H198 (2015).
32. Bower AM, Real HLM, Berhow MA and González de Mejía E, Bioactive compounds from culinary herbs inhibit a molecular target for type 2 diabetes management, dipeptidyl peptidase IV. J Agric Food Chem 62:6147–6158 (2014).
33. Wiedeman PE and Trevillayn JM, Dipeptidyl peptidase IV inhibitors for the treatment of impaired glucose tolerance and type 2 diabetes. Curr Opin Investig Drugs 4:412–420 (2003).
34. Nongonierma AB, Mooney C, Shields DC and FitzGerald RJ, In silico approaches to predict the potential of milk protein-derived peptides as dipeptidyl peptidase IV (DPP-IV) inhibitors. Peptides 57:43–51 (2014).
35. Girgih AT, Udenigwe CC, Li H, Adebiyi AP and Aluko RE, Kinetics of enzyme inhibition and antihypertensive effects of hemp seed (Cannabis sativa L.) protein hydrolysates. J Am Oil Chem Soc 88:1767–1774 (2011).
36. i values for inhibitors of enzyme activity and ligand binding. Nucleic Acids Res 37(Suppl. 2):W441–W445 (2009).
37. i in a competitive enzyme-inhibition model: comparisons among three methods of data analysis. Drug Metabol Dispos 27:756–762 (1999).
38. Berg JM, Tymoczko JL and Stryer L, Biochemistry (5th edn). W.H. Freeman, New York, NY, pp. 319–341 (2002).
39. Akıllıoğlu HG and Karakaya S, Effects of heat treatment and in vitro digestion on the angiotensin converting enzyme inhibitory activity of some legume species. Eur Food Res Technol 229:915–921 (2009).
40. Lam LH, Shimamura T, Manabe S, Ishiyama M and Ukeda H, Assay of angiotensin I-converting enzyme-inhibiting activity based on the detection of 3-hydroxybutyrate with water-soluble tetrazolium salt. Anal Sci 24:1057–1060 (2008).
41. Ruiz-Ruiz J, Dávila-Ortíz G, Chel-Guerrero L and Betancur-Ancona D, Angiotensin I-converting enzyme inhibitory and antioxidant peptide fractions from hard-to-cook bean enzymatic hydrolysates. J Food Biochem 37:26–35 (2011).
42. Norris R and FitzGerald RJ, Antihypertensive peptides from food proteins, in Bioactive Food Peptides in Health and Disease, ed. by Hernández-Ledesma B and Hsieh CC. InTech, Rijeka, Croatia, pp. 45–72 (2013).
43. Wang XM, Wu SS, Xu DG, Xie DQ and Guo H, Inhibitor and substrate binding by angiotensin-converting enzyme: quantum mechanical/molecular mechanical molecular dynamics studies. J Chem Info Model 51:1074–1082 (2011).
44. Mojica L and González de Mejía E, Characterization and comparison of protein and peptide profiles and their biological activities of improved common bean cultivars (Phaseolus vulgaris L.) from Mexico and Brazil. Plant Foods Hum Nutr 70:105–112 (2015).
45. Oseguera-Toledo ME, González de Mejía E and Amaya-Llano SL, Hard-to-cook bean (Phaseolus vulgaris L.) proteins hydrolyzed by alcalase and bromelain produced bioactive peptide fractions that inhibit targets of type-2 diabetes and oxidative stress. Food Res Int 76:839–851 (2015).
46. De Souza Rocha T, Real Hernandez LM, Mojica L, Johnson MH, Chang YK and González de Mejía E, Germination of Phaseolus vulgaris and alcalase hydrolysis of its proteins produced bioactive peptides capable of improving markers related to type-2 diabetes in vitro. Food Res Int 76:150–159 (2015).
47. Rui X, Boye J, Ribereau S, Simpson B and Prasher S, Comparative study of the composition and thermal properties of protein isolates prepared from nine Phaseolus vulgaris legume varieties. Food Res Int 44:2497–2504 (2011).
48. Carrasco-Castilla J, Hernández-Álvarez AJ, Jiménez-Martínez C, Jacinto-Hernández C, Alaiz M, Girón-Calle J et al., Antioxidant and metal chelating activities of Phaseolus vulgaris L. var. Jamapa protein isolates, phaseolin and lectin hydrolysates. Food Chem 131:1157–1164 (2012).