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

Abstract

Summary 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.

l‐histidine improves water retention of heat‐induced gel of chicken breast myofibrillar proteins in low ionic strength solution

“…The rigidity of a protein gel is determined by the amount of particles (aggregates) incorporated into the gel network and the strength of the interactions between these particles (Jiang & Xiong, ). Although l ‐His induced high amount of elastic aggregates with increased G′ value, the lack of disulphide bonding and compact protein cross‐linking that stabilised gel net work as we discussed in section 3.2 might lead to weak gel strength of MPs gel in low ionic strength (Jang et al ., ).…”

“…. On the other hand, the corresponding changes of MP gel strength could be explained by the three‐dimensional structures of MPs (Chen et al ., ; Jang et al ., ). Low strength demonstrated in MPs gel in 1 m m NaCl containing l ‐His (Fig.…”

“…Water‐binding capacity and the textural properties are of great significance for the quality of comminuted meat products, which highly depend on the properties of heat‐induced gel of myofibrillar proteins (MPs), the major proteins in meat (Hemung & Chin, ; Li et al ., ). MPs are salt‐soluble proteins which can be induced to form gels via heating (Jang et al ., ), of which myosin and actin contribute most to the development of desirable gel characteristics. Thermal gelation of MPs involves partial denaturation of protein followed by irreversible aggregation, which forms a multidimensional network that holds water and thus produces a gel (Sun & Holley, ).…”

Evaluation of Porcine Myofibrillar Protein Gel Functionality as Affected by Microbial Transglutaminase and Red Bean [Vignia angularis] Protein Isolate at Various pH Values

“…A previous study described the high protein solubility and emulsion stability of red bean protein isolate (RBPI) at various pHs ( Meng and Ma, 2002a ). In our previous study, RBPI improve the gelling properties and cooking yield of meat protein gels mediated by MTG, which could improve the textural and functional properties of meat proteins as a potential water and meat binder ( Jang and Chin, 2011 ; Jang et al , 2015 ), which could improve the textural properties of meat products ( Hong and Chin, 2010 ). In our previous study, Jang et al (2015) reported that the optimum condition was 1% RBPI induced with 1% MTG.…”

The globalisation of food research in the development of safe and health‐promoting foods

“…Other main areas of research were the potential utilisation of food waste streams/by‐products as added value ingredients (Jang et al ., ; Peng et al ., ; Riedel et al ., ; Rocha Parra et al ., ; Lu et al ., ; Lucas‐González et al ., ; Teixeira et al ., ; Wu et al ., ) and novel food‐processing technologies (de Carvalho Rodrigues et al ., ; Shi & Maleky, ; Juodeikiene et al ., ; Xue et al ., ; Wang et al ., ).…”