The structure formation of minced rainbow trout was monitored during heating from 30°C to 85°C by a dynamic rheological method. The maxima of storage modulus (G') were found at 37°C and in the range of 45°C to 60°C. The largest differences in rigidity resulted from seasonal variations. Firmest protein matrix was obtained by using well-fed fish as raw material, by setting the gels at 35°C and using a pH value around 6.1. Sodium chloride in the range l-2% had little effect on the final rigidity of the minced rainbow trout gels.
The decomposition of ATP was followed to evaluate the freshness of whitefish (Coregonus wartmznni). Decomposition rate was lower in whitefish caught in August than those caught in other seasons. No seasonal differences were found in sensory quality. Whitefish were acceptable with a maximum K value of 80% and a minimum inosine monophosphate concentration of 1.0 micromoles/g.
Globin prepared from pig blood ceII concentrate by a new method based on heme precipitation with dilute carboxymethylcellulose (CMC)-solution at acid pH showed very good water-binding capacity compared with soy protein, la&albumin and glutein. Water-holding ability of globin decreased with increasing pH, drastically at pH-value over 6.0, and with increasing ionic strength. Preheating at different temperatures decreased water-binding capacity only slightly. A great increase in viscosity of 5% globin solution occurred between pH 5.2 and 5.8 at 95'C and a firm gel formed. Freeze-dried gels had excellent water-binding capacities compared with unheated samples or samples heated at other pH values. Isoelectric focusing studies showed three or four bands below Ip 7.4 for globins prepared by CMC-precipitation method or cold acetone method and one intensive band near 7.8 for heat-denatured globins.
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