Effects of Red Bean (Vigna angularis) Protein Isolates on Rheological Properties of Microbial Transglutaminase Mediated Pork Myofibrillar Protein Gels as Affected by Fractioning and Preheat Treatment

Abstract

Fractioning and/or preheating treatment on the rheological properties of myofibrillar protein (MP) gels induced by microbial transglutaminase (MTG) has been reported that they may improve the functional properties. However, the optimum condition was varied depending on the experimental factors. This study was to evaluate the effect of red bean protein isolate (RBPI) on the rheological properties of MP gels mediated by MTG as affected by modifications (fractioning: 7S-globulin of RBPI and/or preheat treatment (pre-heating; 95℃/30 min): pre-heating RBPI or pre-heating/7S-globulin). Cooking yields (CY, %) of MP gels was increased with RBPI (p<0.05), while 7S-globulin decreased the effect of RBPI (p<0.05); however, preheating treatments did not affect the CY (p>0.05). Gel strength of MP was decreased when RBPI or 7S-globulin added, while preheat treatments compensated for the negative effects of those in MP. This effect was entirely reversed by MTG treatment. Although the major band of RBPI disappeared, the preheated 7S globulin band was remained. In scanning electron microscopic (SEM) technique, the appearance of more cross-linked structures were observed when RBPI was prepared with preheating at 95℃ to improve the protein-protein interaction during gel setting of MP mixtures. Thus, the effects of RBPI and 7S-globulin as a substrate, and water and meat binder for MTG-mediated MP gels were confirmed to improve the rheological properties. However, preheat treatment of RBPI should be optimized.

Effect of Faba Bean Isolate and Microbial Transglutaminase on Rheological Properties of Pork Myofibrillar Protein Gel and Physicochemical and Textural Properties of Reduced-Salt, Low-Fat Pork Model Sausages

“…This interaction improved the GS of MPGs by activating the catalysis of 7S globulin by MTG (Jang et al, 2016). Because of the presence of globulins in FBPI, the MP structure was changed due to the formation of hydrophobic interactions in this study.…”

“…As reported by Jiang and Xiong (2013) , components of soy protein, such as conglycinin and glycinin, contributed to gel formation and improved GS due to the interaction between soy protein and myosin in the protein matrix. This interaction improved the GS of MPGs by activating the catalysis of 7S globulin by MTG ( Jang et al, 2016 ). Because of the presence of globulins in FBPI, the MP structure was changed due to the formation of hydrophobic interactions in this study.…”

“…It is considered that these differences are due to the action of MTG on the combination of FBPI and MTG. Several studies reported that the incorporation of legume proteins, such as peanut ( Lin et al, 2019 ), red bean ( Jang et al, 2016 ), and pea ( Borderías et al, 2020 ), modified to compact surface and decrease the porosity of gels in protein structure. These results suggest that many legume proteins have the potential to improve the functional properties of gel matrices.…”

Controlling Ingredients for Healthier Meat Products: Clean Label

“…There are many other proteinsespecially fish sarcoplasmic protein (Hemung and Chin, 2013, 2015-and nonmeat ingredients such as mungbean protein Chin, 2013a, 2013b;Lee et al, 2014a). The addition of red bean protein isolate, mediated by MTGase in myofibrillar protein gels, can improve water-holding capacity because MTGase can promote interaction among proteins (Jang et al, 2015(Jang et al, , 2016Lee et al, 2017).…”