Abstract
ABSTRACT: The properties of total sarcoplasmic proteins from oil sardine (Sardinella longiceps)have been assessed. Ammonium sulfate fractionation of total sarcoplasmic proteins yielded 5 different fractions. The UV‐ab‐sorption spectra of all 5 sarcoplasmic proteins fraction showed a peak in the wavelength range of 275 to 280 nm indicating aromatic amino acid residues in its composition. The SDS‐PAGE of different fractions showed components in the molecular weight range of 97 to 29 kD. The thermal stability in the temperature range of 40° to 80 °C of different fractions were varied in nature. The flow profile of different fractions indicated pseudo‐plastic behavior and minimum structural impairment for fraction V at 30 and 40 °C, respectively. The gelation profile of washed sardine meat in combination with different sarcoplasmic proteins fraction revealed fraction V could enhance the storage modulus values during heating regime.
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