Inhibition of the in vitro activities of α-amylase, α-glucosidase and pancreatic lipase by yellow field pea (Pisum sativum L.) protein hydrolysates

International Journal of Food Science and Technology

Volumn 54, Issue 6, 2019, Pages 2021-2034

  Awosika, Temitola O ^a   Aluko, Rotimi E ^a  

^a UNIVERSITY OF MANITOBA   (Canada)

Author keywords

Enzyme inhibition kinetics; pancreatic lipase; protein hydrolysates; ultrafiltration; Amylase; glucosidase

Indexed keywords

BIOLOGICAL MATERIALS; ENZYME ACTIVITY; ENZYME INHIBITION; HYDROLYSIS; PEPTIDES; PLANTS (BOTANY); ULTRAFILTRATION;

ENZYME INHIBITION KINETICS; GLUCOSIDASE; MEMBRANE ULTRAFILTRATION; PANCREATIC LIPASE; PANCREATIC LIPASE ACTIVITY; PEA PROTEIN CONCENTRATES; PEPTIDE SEQUENCE ANALYSIS; PROTEIN HYDROLYSATE;

AMYLASES;

EID: 85059578658     PISSN: 09505423     EISSN: 13652621     Source Type: Journal    
DOI: 10.1111/ijfs.14087     Document Type: Article

References (52)

1. Adebiyi, APP. & Aluko, I.E. (2011). Functional properties of protein fractions obtained from commercial yellow field pea (Pisum sativa L.) seed protein isolate. Food Chemistry, 128, 902–908.
2. Aluko, I.E., Mofolasayo, O.A. & Watts, BUM (2009). Emulsifying and foaming properties of commercial yellow pea (Pisum sativa L.) seed flours. Journal of Agricultural and Food Chemistry, 57, 9793–9800.
3. Aluko, I.E., Girgih, AT, He, R. et al. (2015). Structural and functional characterization of yellow field pea seed (Pisum sativa L.) protein-derived antihypertensive peptides. Food Research International, 77, 10–16.
4. Barbana, C. & Boye, I.E. (2010). Angiotensin I-converting enzyme inhibitory activity of chickpea and pea protein hydrolysates. Food Research International, 43, 1642–1649.
5. Chi, C.-F., Hub, F.-H., Wang, B., Li, T. & Ding, G.-F. (2015). Antioxidant and anticancer peptides from the protein hydrolysate of blood clam (Tegillarca granosa) muscle. Journal of Functional Foods, 15, 301–313.
6. Ciau-Solis, NAB, Acevedo-Fernandez, JUJU & Betancur-Ancona, D. (2018). In vitro renin-angiotensin system inhibition and in vivo antihypertensive activity of peptide fractions from lima bean (Phaseolus lunatus L.). Journal of the Science of Food and Agriculture, 98, 781–786.
7. Girgih, AT, Udenigwe, C.C., Li, H., Adebiyi, APP. & Aluko, I.E. (2011). Kinetics of enzyme inhibition and antihypertensive effects of hemp seed (Cannabis sativa L.) protein hydrolysates. Journal of the American Oil Chemists’ Society, 88, 1767–1774.
8. Girgih, AT, Akashi, A.M., He, R., Malomo, S.A. & Aluko, I.E. (2014). Preventive and treatment effects of hemp seed (Cannabis sativa L.) meal protein hydrolysate against high blood pressure in spontaneously hypertensive rats. European Journal of Nutrition, 53, 1237–1246.
9. Girgih, AT, He, R., Has an, FEM., Udenigwe, C.C., Gill, TAX & Aluko, I.E. (2015). Evaluation of the in vitro antioxidant properties of a cod (Gauds morgue) protein hydrolysate and peptide fractions. Food Chemistry, 173, 652–659.
10. Golay, A. & Ybarra, J. (2005). Link between obesity and type 2 diabetes. Best Practice and Research in Clinical Endocrinology and Metabolism, 19, 649–663.
11. Gropper, S.S. & Smith, JELL (2012). Advanced Nutrition and Human Metabolism. Boston, MA: Engage Learning.
12. Halo, W., Wang, M. & Live, M. (2017). The inhibitory effects of Fixing black tea extracts on α- glucosidase. Journal of Food Biochemistry, 41, e12269.
13. He, R., Malomo, S.A., Akashi, A., Girgih, AT, Jug, X. & Aluko, I.E. (2013). Purification and hypertensive activity of rapeseed protein-derived renin and angiotensin converting enzyme inhibitory peptides. Journal of Functional Foods, 5, 781–789.
14. Humiski, LAMA & Aluko, I.E. (2007). Physicochemical and bitterness properties of enzymatic pea protein hydrolysates. Journal of Food Science, 72, S605–S611.
15. Irondi, E.A., Angola, SO & Obligor, I.E. (2018). Inhibitory effects of tropical almond leaf extract on xanthenes oxidize, pancreatic lipase, and angiotensin 1-converting enzyme, in vitro. Journal of Food Biochemistry, 42, e12481.
16. Jara, A.M.R., Leggier, COST & Bruno, M.A. (2018). Preparation of soy protein hydrolysates with antioxidant activity by using peptidases from latex of Macular pomifera fruits. Food Chemistry, 264, 326–333.
17. Kazeem, M.I., Adamson, J.O. & Ogunwande, I.A. (2013). Modes of inhibition of α-amylase and α-glucosidase by aqueous extract of Benth leaf. BioMed Research International, 2013, 527570.
18. Kido, Y., Hiramoto, S., Murao, M. et al. (2003). ε-Polylysine inhibits pancreatic lipase activity and suppresses postprandial hypertriacylglyceridemia in rats. Journal of Nutrition, 133, 1887–1891.
19. Lee, S.S., Esa, N.M. & Loh, S.P. (2015). In vitro inhibitory activity of selected legumes against pancreatic lipase. Journal of Food Biochemistry, 39, 485–490.
20. Lin, H.J., Li, L., Tian, Y.J., Zhang, X. & Li, B. (2012). Protein hydrolysate from brewer's spent grain and its inhibitory ability of α-glucosidase. Advanced Materials Research, 581(582), 138–141.
21. Lunagariya, NAB, Patel, N.K., Jagtap, S.C. & Bhutani, K.K. (2014). Inhibitors of pancreatic lipase: state of the art and clinical perspectives. EXCLI Journal, 13, 897–921.
22. Lunder, M., Bratkovič, T., Kreft, S. & Štrukelj, B. (2005). Peptide inhibitor of pancreatic lipase selected by phage display using different elution strategies. Journal of Lipid Research, 46, 1512–1516.
23. Ma, Y., Wu, Y. & Li, L. (2018). Relationship between primary structure or spatial conformation and functional activity of antioxidant peptides from Pinctada fucata. Food Chemistry, 264, 108–117.
24. Malomo, S.A. & Aluko, I.E. (2016). In vitro acetylcholinesterase-inhibitory properties of enzymatic hemp seed protein hydrolysates. Journal of the American Oil Chemists’ Society, 93, 411–420.
25. Markwell, M.A.K., Haas, S.M., Bieber, L.L. & Tolbert, N.E. (1978). A modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples. Analytical Biochemistry, 87, 206–210.
26. Merovci, A., Solis-Herrera, C., Daniele, G. et al. (2014). Dapagliflozin improves muscle insulin sensitivity but enhances endogenous glucose production. Journal of Clinical Investigation, 124, 509–514.
27. Mora, L. & Hayes, M. (2015). Cardioprotective cryptides derived from fish and other food sources: generation, application, and future markets. Journal of Agricultural and Food Chemistry, 63, 1319–1331.
28. Mudgil, P., Kamal, H., Yuen, G.C. & Maqsood, S. (2018). Characterization and identification of novel antidiabetic and anti-obesity peptides from camel milk protein hydrolysates. Food Chemistry, 259, 46–54.
29. Ngoh, Y.-Y. & Gan, C.Y. (2016). Enzyme- assisted extraction and identification of antioxidative and α- amylase inhibitory peptides from Pinto beans (Phaseolus vulgaris cv. Pinto). Food Chemistry, 190, 331–337.
30. Ngoh, Y.Y., Choi, S.B. & Gan, C.Y. (2017). The potential roles of Pinto bean (Phaseolus vulgaris cv. Pinto) bioactive peptides in regulating physiological functions: protease activating, lipase inhibiting and bile acid binding activities. Journal of Functional Foods, 33, 67–75.
31. Nongonierma, A.B., Paolella, S., Mudgil, P., Maqsood, S. & FitzGerald, R.J. (2017). Dipeptidyl peptidase IV (DPP-IV) inhibitory properties of camel milk protein hydrolysates generated with trypsin. Journal of Functional Foods, 34, 49–58.
32. Oliveros, E., Somers, V.K., Sochor, O., Goel, K. & Lopez-Jimenez, F. (2014). The concept of normal weight obesity. Progress in Cardiovascular Diseases, 56, 426–433.
33. Oseguera-Toledo, M.E., Gonzalez de Mejia, E. & Amaya-Llano, S.L. (2015). 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 Research International, 76, 839–851.
34. Osman, A., Goda, H.A., Abdel-Hamid, M., Badran, S.M. & Otte, J. (2016). Antibacterial peptides generated by Alcalase hydrolysis of goat whey. LWT - Food Science and Technology, 65, 480–486.
35. Patil, P., Mandal, S., Tomar, S.K. & Anand, S. (2015). Food protein-derived bioactive peptides in management of type 2 diabetes. European Journal of Nutrition, 54, 863–880.
36. Ranilla, L.G., Kwon, Y.-I., Apostolidis, E. & Shetty, K. (2010). Phenolic compounds, antioxidant activity and in vitro inhibitory potential against key enzymes relevant for hyperglycemia and hypertension of commonly used medicinal plants, herbs and spices in Latin America. Bioresource Technology, 101, 4676–4689.
37. Sanchez-Rivera, L., Santos, P.F., Miralles, B., Carron, R., Montero, M.J. & Recio, I. (2016). Peptide fragments from β-casein f(134-138), HLPLP, generated by the action of rat blood plasma peptidases show potent antihypertensive activity. Food Research International, 88, 348–353.
38. Segura Campos, M.R., Peralta González, F., Chel Guerrero, L. & Betancur Ancona, D. (2013). Angiotensin I-converting enzyme inhibitory peptides of chia (Salvia hispanica) produced by enzymatic hydrolysis. International Journal of Food Science, 2013, 158482.
39. Shobana, S., Sreerama, Y.N. & Malleshi, N.G. (2009). Composition and enzyme inhibitory properties of finger millet (Eleusine coracana L.) seed coat phenolics: mode of inhibition of α-glucosidase and pancreatic amylase. Food Chemistry, 115, 1268–1273.
40. Silva, C., Da Fonseca, R. & Prentice, C. (2014). Comparing the hydrolysis degree of industrialization byproducts of Withemout croaker (Micropogonias furnieri) using microbial enzymes. International Food Research Journal, 21, 1757–1761.
41. Siow, H.-L. & Gan, C.-Y. (2017). Optimization study in extracting antioxidative and a-amylase inhibitor peptides from cumin seeds (Cuminum cyminum). Journal of Food Biochemistry, 41, e12280.
42. Siow, H.-L., Lim, T.S. & Gan, C.Y. (2017). Development of a workflow for screening and identification of α- amylase inhibitory peptides from food source using an integrated Bioinformatics- phage display approach: case study – Cumin seed. Food Chemistry, 214, 67–76.
43. Tang, Y., Zhang, B., Li, X. et al. (2016). Bound phenolics of quinoa seeds released by acid, alkaline, and enzymatic treatments and their antioxidant and alpha-glucosidase and pancreatic lipase inhibitory effects. Journal of Agricultural and Food Chemistry, 64, 1712–1719.
44. To, J., Chen, J., Zhu, S., Zhang, C., Chen, H. & Liu, Y. (2013). Inhibition of wheat bran and it′s active compoments on α-glucosidase in vitro. Pharmacognosy Magazine, 9, 309–314.
45. Udenigwe, C.C. (2013). In silico analysis of the large and small subunits of cereal RuBisCO as precursors of cryptic bioactive peptides. Process Biochemistry, 48, 1794–1799.
46. Uraipong, C. & Zhao, J. (2016a). Rice bran protein hydrolysates exhibit strong in vitro α-amylase, β-glucosidase and ACE-inhibition activities. Journal of the Science of Food and Agriculture, 96, 1101–1110.
47. Uraipong, C. & Zhao, J. (2016b). Identification and functional characterisation of bioactive peptides in rice bran albumin hydrolysates. International Journal of Food Science & Technology, 51, 2201–2208.
48. Vasquez-Villanueva, R., Munoz-Moreno, L., Carmena, M.J., Marina, M.L. & Garcia, M.C. (2018). In vitro antitumor and hypertensive activity of peptides from olive seeds. Journal of Functional Foods, 42, 177–184.
49. WHO. (2017). Diabetes. Fact sheet. [Online]. World Health Organization. Available: http://www.who.int/mediacentre/factsheets/fs312/en/ [Accessed September 20 2018].
50. Wing, R.R., Lang, W., Wadden, TAX et al. (2011). Benefits of modest weight loss in improving cardiovascular risk factors in overweight and obese individuals with type 2 diabetes. Diabetes Care, 34, 1481–1486.
51. Yumuk, V., Fruhbeck, G., Oppert, J.M., Woodward, E. & Toplak, H. (2014). An EASO position statement on multidisciplinary obesity management in adults. Obesity Facts, 7, 96–101.
52. Zambad, S.P., Tuli, D., Mathur, A. et al. (2013). TRC210258, a novel TGR5 agonist, reduces glycemic and dyslipidemic cardiovascular risk in animal models of diabesity. Diabetes, Metabolic Syndrome and Obesity, 7, 1–14.