DYNAMIC RHEOLOGICAL BEHAVIOR OF MYOFIBRIL LAR PROTEINS AND SOYBEAN PROTEINS DURING HEAT-INDUCED GELATION

The thermal gel-formation properties of muscle proteins, soybean prote ins and their mixture with or without urea were examined by means of d ynamic theological measurements and SDS-PAGE. The following results we re obtained. (1) In the systems of natural actomyosin and myosin, the thermal gelation was promoted by mixing soybean 11 S protein in either case, and their thermal behavior was influenced by actin. (2) The gel -formation of natural actomyosin and myosin was largely suppressed by the addition of 2 M urea, on the other hand, gelation of the mixture o f each myofibrillar protein and soybean 11 S protein was completely in hibited by the addition of 1 M urea. These results indicated that hydr ophobic interactions played a role in the heat-induced gelation of the single myofibrillar protein systems, while hydrogen bonds became mark edly involved in gelation by mixing soybean 11 S protein.