Abstract

Chickpea hydrolysates have shown bioactivity towards type 2 diabetes by inhibiting dipeptidyl peptidase (DPPIV) activity. The objective was to compare the effect of adding different levels of an optimized bromelain hydrolysate from chickpea isolated protein on DPPIV inhibition capacity and physicochemical properties of maize tortilla. White and blue maize tortillas, with no added chickpea hydrolysates were compared with fortified tortillas at the levels of 5%, 10%, and 15% w/w. Changes in color (L* a* b*, hue angle, and ), texture (hardness, cohesiveness, and puncture force), and moisture were tested. Soluble protein determination and SDS-PAGE electrophoresis were used to characterize the protein profiles, and LC-MS-MS was used to sequence the peptides. DPPIV inhibition was evaluated before and after simulated gastrointestinal digestion. Peptides in the hydrolysates had high hydrophobicity (7.97–27.05 kcal * mol −1) and pI (5.18–11.13). Molecular docking of peptides showed interaction with DPPIV with an energy of affinity of –5.8 kcal/mol for FDLPAL in comparison with vildagliptin (−6.2 kcal/mol). The lowest fortification level increased soluble protein in 105% (8 g/100 g tortilla). DPPIV inhibition of white maize tortilla increased from 11% (fresh control) to 91% (15% fortification), and for blue tortilla from 26% to 95%. After simulated digestion, there was not a difference between blue or maize tortillas for DPPIV inhibition. Fortification of maize tortilla with chickpea hydrolysate inhibits DPPIV and can potentially be used in the prevention and management of type 2 diabetes. However, due to observed physicochemical changes of the fortified tortilla, sensory properties and consumer acceptance need to be evaluated.

Highlights

  • Chickpea (Cicer arietinum L.) is one of the most consumed pulses worldwide

  • Information on the peptides originated from chickpea storage proteins is shown in Figure 1b,c (FDLPAL), where the peptide mass and precursor ion for this peptide is shown

  • Analyzing the solubility in the composite chickpea hydrolysate, we observed similar behavior reported in previous studies [42] as a result of the enzymatic hydrolysis that provides better solubility, stability, and functional properties to the hydrolysates in comparison with protein concentrates or isolates

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Summary

Introduction

Chickpea (Cicer arietinum L.) is one of the most consumed pulses worldwide. It has shown important bioactivities such as antioxidant capacity; antifungal, antibacterial, and analgesic properties; and angiotensin I-converting enzyme inhibition; as well as hypocholesterolemic, anticancer, and anti-inflammatory properties [1,2,3,4]. DM is associated with heart disease and stroke, blindness, kidney failure, and lower-limb amputation [10]; DM is a burden on public health. Effective management mechanisms are needed to decrease the burden of DM; an exercise program and a diet that includes pulses are effective in managing the disease [11]

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