| Budget Amount *help |
¥2,000,000 (Direct Cost: ¥2,000,000)
Fiscal Year 1987: ¥200,000 (Direct Cost: ¥200,000)
Fiscal Year 1986: ¥200,000 (Direct Cost: ¥200,000)
Fiscal Year 1985: ¥1,600,000 (Direct Cost: ¥1,600,000)
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| Research Abstract |
It is well known from our eating experience that each fish meat has its own specific texture. The object of this study is to estimate objectively the species difference, and to estimate the factors affecting the difference. Five fish species, skipjack, flying fish, common horse mackerel, plaice, and channel rock fish were stored at 4゜C for 14 days. The measured values of firmness, cohesiveness, and penetration of raw meat decreased during storage. The rate of the change varied from species to species. The extractability of myofibrillar-, sarcoplasmic-, alkali-soluble-, and stroma-fraction of five fish muscle did not show any significant changes in 14 days.
The SDS-polyacrylamide gel electrophoretic pattarns of these extracted protein fraction showed no difference with respect to the storage time. The degree of fragmentation and the value of cell fragility varied significantly during storage. The changes in physical properties during post harvest storage were affected by the changes of the muscle tissue structures than the changes of the component proteins.
Contribution of the connective tissue content on the meat texture was clearly shown in teh raw meat of five species. There was a significant correlation between the collagen content and the firmness value. However, between the cooked meat and collagen content, any appreciable correlation was seen.
The rheological properties of five fish muscle were characterized to each other in terms of the creep-compliance. The fish muscle was described by the rheological model having 6 elements. Values of the instantaneous modulus or the permanent viscosity modulus differed from the texture we have feel. It was suggested that our mouthfeel about "firmness" is not based on the difference in the elastic modulus but on the ease of biting which is related to collagen content.
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