New insights into the cross-linking between myosin and alkali-treated pea protein by transglutaminase under low ionic conditions: Contribution of legumin and vicilin fractions

Abstract

This study investigated the cross-linking of myosin with pH12-shifted legumin (11SpH) or vicilin (7SpH), and the gel properties of composite gels, with or without transglutaminase, in 0.3 M NaCl. The free sulfhydryl content of 7SpH/11SpH increased significantly (P < 0.05). The covalent cross-linking degree between 7SpH/11SpH and myosin was enhanced, with the vicilin of approximately 45 kDa showing more pronounced cross-linking. SDS–PAGE analysis of myosin subfragments revealed that S1 and light meromyosin were the primary cross-linking regions for 11SpH, reducing the Ca2+-ATPase activity of the myosin head, while S2 was an alternative cross-linking region for 7SpH. The cross-linking of 7SpH/11SpH enhanced the thermal aggregation of S1. The cross-linking degree of tails followed this order: myosin > myosin+7SpH > myosin+11SpH. Thus, the use of 7SpH/11SpH and transglutaminase offers a new approach to improving texture in low-salt meat products.