Heat-induced gelation of a mixture of myosin B and soybean protein.

Abstract

On observation by scanning electron microscopy, the respective diameters of heat-induced gel networks ofmyosin B and soybean protein CIF were found to be above 1 /mi and below 1 /mi. In a mixture of the proteins, it was observed that the denatured soybean protein CIF had associated continuously around myosin B networks. These reactions reinforced the rough myosin B networks. The structures of the reinforced networks were considerably different from those of the individual proteins. Furthermore, when both the proteins were mixed, formation of the networks was already found before heating. It was suggested that the reaction was related to disulfide bonds between the two proteins.

Hydroxytyrosol extracts, olive oil and walnuts as functional components in chicken sausages

“…Scanning electron microscopy (SEM) analysis of the sausages was performed according to Haga and Ohashi. 25 Cubes of sausage samples (3 × 3 × 3 mm 3 ) were fixed for 24 h at 4 ∘ C in a 0.1 mol L −1 phosphate buffer (pH 7.0) containing 2.5 g 100 mL −1 glutaraldehyde. The fixed samples were washed three times, each time with 0.1 mol L −1 phosphate buffer (pH 7.0) for 10 min, and dehydrated in incremental concentrations of ethanol (50, 60, 70, 80, 90, 95, and 100, 100, 100% for 30 min per step).…”

Textural Properties of Pork Frankfurters Containing Thermally/Enzymatically Modified Soy Proteins

“…Microscopic examination of cooked frankfurters was performed as described by Haga and Ohashi (1984) with slight modifications. Samples (4 ϫ 4 ϫ 2 mm 3 ), obtained by cutting from the interior of frankfurters, were fixed for 24 h at 4 °C in a 0.1 M phosphate buffer (pH 7.00) containing 2.5% glutaraldehyde.…”

“…The latter was also observed by Inouye and others (2002) in a coagulation study. Myosin could interact not with native soy 11S protein but with dissociated soy 11S components (Peng and others 1982a,b) and the interaction enhanced the formation of a rigid gel structure (Haga and Ohashi 1984;Feng and Xiong 2002a). On the other hand, NS F and HS F treatments decreased frankfurter hardness, cohesiveness, and breaking strength (by 20 to 80%), rendering the gel more deformable.…”

“…The presence of these structurally modified soy proteins ostensibly altered the aggregation pattern of myofibrillar proteins and transformed them into a more interactive matrix system that was more resilient to compression, namely, showing increased hardness (Figure 1). Haga and Ohashi (1984), when studying the microstructure of heat-induced gels consisting only of purified myosin and soy 11S protein at a 16:50 mixing ratio, found that denatured soy 11S globulins enhanced myosin gelation by associating continuously around myosin networks. Presumably, this was also true in the present study except that glycinin and other 11S proteins, dissociated either by a brief preheat treatment or by Alcalase hydrolysis, probably reinforced the gel network by forming complexes with mixed muscle fiber, myofibrils, and myosin.…”

Effect of mungbean [Vigna radiata (L.) Wilczek] protein isolates on the microbial transglutaminase‐mediated porcine myofibrillar protein gels at various salt concentrations

“…Briefly, cubic samples (3 mm 3 ) were fixed by dipping in 0.1 M sodium phosphate buffer solutions (pH 7.0) including 2.5% glutaraldehyde for 24 h in refrigeration (4 AE 1°C) and then postfixed in 1% osmium tetraoxide (OsO 4 ) was added. The postfixed samples were dehydrated with increased concentrations of ethanol from 50% to 100% for 10 min each step (Haga & Ohashi, 1984) with being soaked in acetone for 10 min (Hong & Chin, 2010).…”