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Article

Bioactive Peptides from Germinated Soybean with Anti-Diabetic Potential by Inhibition of Dipeptidyl Peptidase-IV, α-Amylase, and α-Glucosidase Enzymes

by
Marcela González-Montoya
1,
Blanca Hernández-Ledesma
2,
Rosalva Mora-Escobedo
1 and
Cristina Martínez-Villaluenga
3,*
1
Escuela Nacional de Ciencias Biológicas-Instituto Politécnico Nacional. Campus Zacatenco, Unidad Profesional “Adolfo López Mateos”, Calle Wilfrido Massieu esquina Cda. Manuel Stampa. C.P, Ciudad de México 07738, Mexico
2
Instituto de Investigación en Ciencias de la Alimentación (CIAL, CSIC-UAM, CEI UAM+CSIC), Nicolás Cabrera 9, 28049 Madrid, Spain
3
Institute of Food Science, Technology and Nutrition (ICTAN-CSIC), Juan de la Cierva 3, 28006 Madrid, Spain
*
Author to whom correspondence should be addressed.
Int. J. Mol. Sci. 2018, 19(10), 2883; https://doi.org/10.3390/ijms19102883
Submission received: 30 July 2018 / Revised: 14 September 2018 / Accepted: 19 September 2018 / Published: 22 September 2018
(This article belongs to the Special Issue Peptides for Health Benefits)

Abstract

Functional foods containing peptides offer the possibility to modulate the absorption of sugars and insulin levels to prevent diabetes. This study investigates the potential of germinated soybean peptides to modulate postprandial glycaemic response through inhibition of dipeptidyl peptidase IV (DPP-IV), salivary α-amylase, and intestinal α-glucosidases. A protein isolate from soybean sprouts was digested by pepsin and pancreatin. Protein digest and peptide fractions obtained by ultrafiltration (<5, 5–10 and >10 kDa) and subsequent semipreparative reverse phase liquid chromatography (F1, F2, F3, and F4) were screened for in vitro inhibition of DPP-IV, α-amylase, maltase, and sucrase activities. Protein digest inhibited DPP-IV (IC50 = 1.49 mg/mL), α-amylase (IC50 = 1.70 mg/mL), maltase, and sucrase activities of α-glucosidases (IC50 = 3.73 and 2.90 mg/mL, respectively). Peptides of 5–10 and >10 kDa were more effective at inhibiting DPP-IV (IC50 = 0.91 and 1.18 mg/mL, respectively), while peptides of 5–10 and <5 kDa showed a higher potency to inhibit α-amylase and α-glucosidases. Peptides in F1, F2, and F3 were mainly fragments from β-conglycinin, glycinin, and P34 thiol protease. The analysis of structural features of peptides in F1–F3 allowed the tentative identification of potential antidiabetic peptides. Germinated soybean protein showed a promising potential to be used as a nutraceutical or functional ingredient for diabetes prevention.
Keywords: germinated soybean; gastrointestinal digestion; peptides; inhibitors; dipeptidyl peptidase; α-amylase; α-glucosidase germinated soybean; gastrointestinal digestion; peptides; inhibitors; dipeptidyl peptidase; α-amylase; α-glucosidase

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MDPI and ACS Style

González-Montoya, M.; Hernández-Ledesma, B.; Mora-Escobedo, R.; Martínez-Villaluenga, C. Bioactive Peptides from Germinated Soybean with Anti-Diabetic Potential by Inhibition of Dipeptidyl Peptidase-IV, α-Amylase, and α-Glucosidase Enzymes. Int. J. Mol. Sci. 2018, 19, 2883. https://doi.org/10.3390/ijms19102883

AMA Style

González-Montoya M, Hernández-Ledesma B, Mora-Escobedo R, Martínez-Villaluenga C. Bioactive Peptides from Germinated Soybean with Anti-Diabetic Potential by Inhibition of Dipeptidyl Peptidase-IV, α-Amylase, and α-Glucosidase Enzymes. International Journal of Molecular Sciences. 2018; 19(10):2883. https://doi.org/10.3390/ijms19102883

Chicago/Turabian Style

González-Montoya, Marcela, Blanca Hernández-Ledesma, Rosalva Mora-Escobedo, and Cristina Martínez-Villaluenga. 2018. "Bioactive Peptides from Germinated Soybean with Anti-Diabetic Potential by Inhibition of Dipeptidyl Peptidase-IV, α-Amylase, and α-Glucosidase Enzymes" International Journal of Molecular Sciences 19, no. 10: 2883. https://doi.org/10.3390/ijms19102883

APA Style

González-Montoya, M., Hernández-Ledesma, B., Mora-Escobedo, R., & Martínez-Villaluenga, C. (2018). Bioactive Peptides from Germinated Soybean with Anti-Diabetic Potential by Inhibition of Dipeptidyl Peptidase-IV, α-Amylase, and α-Glucosidase Enzymes. International Journal of Molecular Sciences, 19(10), 2883. https://doi.org/10.3390/ijms19102883

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