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. 2023 Jun 30;28(2):149-159.
doi: 10.3746/pnf.2023.28.2.149.

Production of Dipeptidyl Peptidase-IV Inhibitory Peptides from Germinated Jack Bean [ Canavalia ensiformis (L.) DC.] Flour

Friska Citra Agustia  1   2 , Agnes Murdiati  1 , Supriyadi  1 , Retno Indrati  1
Affiliations

Production of Dipeptidyl Peptidase-IV Inhibitory Peptides from Germinated Jack Bean [ Canavalia ensiformis (L.) DC.] Flour

Friska Citra Agustia et al. Prev Nutr Food Sci. .

Abstract

An alternate plant-based protein, jack bean sprout, was explored as a source of bioactive peptides. Germination to increase dipeptidyl peptidase-IV (DPP-IV) inhibitory peptide in jack bean sprout flour has yet to be reported. Therefore, this study aimed to investigate the optimal condition to maximize the content of bioactive peptides with maximum DPP-IV inhibitory activity. The relationship between germination and DPP-IV inhibitory activity was determined by analyzing the proteolytic activity, percentage of degree of hydrolysis (%DH), and peptide content. Peptide samples with the most potent DPP-IV inhibitory activity were subsequently fractionated, identified, and characterized. The 60-h germinated jack bean had the best DPP-IV inhibitory activity (41.57%; half maximal inhibitory concentration=2.24 mg/mL). Proteolytic activity (15.24 unit/g), %DH (11.43%), and peptide content (59.71 mg/g) supported this result. Furthermore, the <1.0 kDa peptide fraction of this sprouted flour had the highest molecular weight (MW) distribution (32.60%) and DPP-IV inhibitory activity (71.99%). Peptide sequences identified from MW <1.0 and 1.0∼3.5 kDa peptide fractions had valine, leucine, isoleucine, glycine, and tryptophan at the N-terminal and also had alanine at the penultimate N-terminal, verifying their presence as DPP-IV inhibitors. Furthermore, peptide sequences generated exhibited other biological activities, including angiotensin-converting enzyme, renin, and α-glucosidase inhibitors.

Keywords: dipeptidyl peptidase-IV inhibitors; germination; jack bean sprout flour; peptide fraction; peptide sequence.

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Conflict of interest statement

AUTHOR DISCLOSURE STATEMENT The authors declare no conflict of interest.

Figures

Fig. 1
Fig. 1
Proteolytic activity of jack bean sprout flour. Different letters (a-d) show significant differences (Duncan’s test, P < 0.05).
Fig. 2
Fig. 2
The percentage of degree of hydrolysis (%DH) and peptide content of jack bean sprout flour. Capital letters (A-F) show significant differences (Duncan’s test, P<0.05) between DH samples, and small letters (a-f) show significant differences (Duncan’s test, P<0.05) between peptide content samples.
Fig. 3
Fig. 3
Dipeptidyl peptidase-IV (DPP-IV) inhibitory activity of jack bean sprout flour. Capital letters (A-E) show significant differences (Duncan’s test, P<0.05) between DPP-IV inhibitory activity samples, and small letters (a-g) show significant differences (Duncan’s test, P<0.05) between DPP-IV inhibitory half maximal inhibitory concentration (IC50) samples.
Fig. 4
Fig. 4
Molecular weight (MW) distribution of the jack bean sprout flour peptide fraction. Small letters (a-d) in the same sample and different fractions show a significant difference (Duncan’s test, P<0.05). Capital letters (A, B) in the same fraction and different samples show a significant difference (t-test, P<0.05).
Fig. 5
Fig. 5
Dipeptidyl peptidase-IV (DPP-IV) inhibitory activity of the jack bean sprout flour peptide fraction. Small letters (a-d) in the same sample and different fractions show a significant difference (Duncan’s test, P<0.05). Capital letters (A, B) in the same fraction and different samples show a significant difference (t-test, P<0.05).
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