Evaluation of red bean protein [Vigna angularis] isolate on rheological properties of pork myofibrillar protein gels induced by microbial transglutaminase

The effects of 1% red bean protein isolate (RBPI) on the gel properties of myofibrillar protein (MP) in various levels of microbial transglutaminase (MTG: 0%, 0.1%, 0.5%, & 1%) were evaluated. The cooking yield (CY) of the MP gels decreased with increasing MTG level, while the addition of RBPI improved the CY of the MP gels. Gel strength (GS) was also improved when RBPI was incorporated into the MP gels containing higher than 0.5% of MTG. The addition of MTG and RBPI was slightly changed the endothermic peak temperatures. Scanning electron microscopy (SEM) showed that the three‐dimensional structure of MP with RBPI alone or in combined with MTG was compacted as compared to the control. Based on the results, RBPI could be functioned as a substrate for MTG (0.5–1.0%) and a water binder of meat protein gel mediated by MTG.