Modified whey protein isolate gel prepared by thermal aggregation combined with transglutaminase crosslinking achieves Casein-like slow digestion in vitro and in vivo

Abstract

Our study aimed to fabricate a modified slow-digestive whey protein isolate (WPI), which can supply enough branched-chain amino acids (BCAAs) during long-term fasting. The WPI aqueous solution (10 % w/v) was treated by heat (80 ℃) to unfold the protein tertiary structure, and subsequently treated with transglutaminase to form a gel via cross-linking. The powder of the WPI gel was obtained by spray drying, which can dissolve in water easily and self-assemble into gels again. This modified WPI contained protein aggregates with high molecular weight, and kept a stable gel-like structure under simulated gastric digestion conditions (pH = 3, 37 ℃). A dense honeycomb internal microstructure of the freeze-dried gel was observed. Further, we found that the WPI gel successfully achieved a casein-like digestible ratio (37.37 %) and released more BCAAs (0.18 mg/mL) than casein during the 4 h of in vitro simulated digestion based on the INFOGEST method. Finally, our results showed that the C57BL/6 mice oral administrated with the modified WPI gel had consistently higher BCAAs concentration (0.052 mg/mL) in their blood serum than the mice with normal WPI intake during the 6 h of in vivo digestion.