Conjugation of gum Arabic and lentil protein hydrolysates through Maillard reaction: Antioxidant activity, volatile compounds, functional and sensory properties

Lentil protein hydrolysates (LPH) and lentil protein hydrolysates cross-linked (LPHC) were grafted with gum Arabic (GA) through a wet Maillard reaction at 100 degrees C for 2 h and called MLPH and MLPHC. The samples were assessed for absorption, degree of grafting (DG), surface hydrophobicity, antioxidant activity, molecular weight (MW) profile, chemical alteration, volatile compounds, functional and sensory properties. Results showed that Maillard grafting led to increase in absorption and DG (maximum value: MLPHC), and led to the reduction of the surface hydrophobicity and antioxidant activity (minimum value: MLPHC). MW profiles indicated that MLPH and MLPHC formed new bands at MW >250 kDa. Regarding the Fourier transform infrared spectroscopy (FTIR), Maillard conjugation led to the occurrence of peaks at 1759 and 1765 cm(-1), while the intensities of amide I bands at 1637 and 1659 cm(-1) and amide II bands at 1498 and 1495 cm(-1) were decreased. Hydrolysis, cross-linking, and especially Maillard grafting provided well-balanced content of volatile components. Indeed, the proportions of alcohols, ketones, aldehydes, and acids were changed, thereby, the inherent grassy and planty tastes were diminished while new umami taste was developed. Maillard grafting led to significant improvement of functional proper -ties, while MLPH and MLPHC indicated the highest emulsifying activity at pH 10.0 (73.76 and 70.12 m(2)/g, respectively) and stability (369.64 and 288.22 min), foaming capacity (88.57% and 142.86%) and stability (60.57% and 72%). Sensory analysis has demonstrated that umami taste was highly developed in MLPH and MLPHC, which can be well considered as meat proteins and flavor enhancers such as monosodium glutamate (MSG).