Effect of Red Bean Protein and Microbial Transglutaminase on Gelling Properties of Myofibrillar Protein

Abstract

The effects of soy protein isolate (SPI) and red bean protein isolate (RBPI) on gelling properties of pork myofibrillar protein (MP) in the presence of microbial transglutaminase (MTG) were studied at 0.45 M NaCl. MP paste was incubated with MTG (0.1%) at various levels (0.1, 0.3, 0.5, and 1%) of SPI and RBPI before incubating at 4 o C for 4 h. The rheological property results showed that MP gel shear stress increased with increasing RBPI concentration. Cooking yield (CY) of the MP gel increased with increasing RBPI and SPI, whereas gel strength (GS) was not affected by adding RBPI or SPI. Thus, effects of incubation time (0, 4, 8, 10, and 12 h) were measured at 0.1% SPI and RBPI. GS values of the MP gel at 10 and 12 h were similar and were higher than those of the others. CY values were highest when RBPI (0.1%) was added, regardless of incubation time. The protein patterns indicated that incubating the MP with MTG for 10 h resulted in protein crosslinking between MP and RBPI or SPI. Based on these results, RBPI and SPI could be used as an ingredient to increase textural properties and cooking yield of meat protein gel.

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

“…. In the previous study, the addition of MTG (0.1%) and various levels of RBPI (0.1–1.0%) did not improve the GS of MP gels due to the low level (0.1%) of MTG (Jang & Chin, ). However, the addition of MTG (0.1%) improved the GS of the MP gels without RBPI; in addition, continuous increases were not observed with increases of the level up to 1.0%.…”

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

“…MP concentration was adjusted to 40 mg/mL using the Biuret method (Gornall et al , 1949). RBPI was prepared from red bean (Saecharmdeul Co., Korea) according to the previous study (Jang and Chin, 2011; Kim et al , 1990). RBPI 7S globulin protein was prepared by fractioning (Hong et al , 2012) and/or preheating at 95℃ for 30 min (pre-heating RBPI and pre-heating/7S-globulin) (Fig.…”

“…SEM was performed to observe the differences of three-dimensional structure among treatments using a JSM-7500F microscope (JEOL Ltd., Japan) as previously described (Jang and Chin, 2011). According to prior methods for sample preparation (Haga and Ohashi, 1984), cubic samples (3 mm 3 ) were fixed by soaking for 24 h in 2.5% glutaraldehyde buffer solutions (0.1 M sodium phosphate buffer with glutaraldehyde, pH 7.0) at 4±1℃.…”

“…A post-fixation procedure was followed with osmium tetraoxide (OsO 4 ) buffer solution. Post-fixed samples were washed and dehydrated by dipping in increased levels of ethanol (50, 60, 70, 80, 90%, and three times with 100%) and acetone for 10 min per each step (Jang and Chin, 2011). To observe the microstructure (magnification, ×2000), samples were gold-coated and then measured using a SEM analyzer at 15 kV.…”

“…Red bean protein isolate (RBPI) has been suggested as a useful substrate for improving the water binding ability and textural properties, as well as emulsion stability in different addition levels, pH values, and salt concentrations to optimize processing conditions (Jang and Chin, 2011) when incorporated into myofibrillar protein (MP) gels mediated by microbial transglutaminase (MTG). Because MP gels can be affected by processing conditions including pH, salt concentration, temperature, and functional ingredients, their optimized application has attracted research interest (Chin et al , 2009a; Chin et al , 2009b; Doerscher et al , 2003; Kerry et al , 1999; Ramirez-Suarez and Xiong, 2003).…”