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Fractionation of Muscle Proteins of Fresh Water Fish and Changes during Iced Storage
Author(s) -
BALIGA B. R.,
MOORJANI M. N.,
LAHIRY N. L.
Publication year - 1969
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1969.tb12098.x
Subject(s) - solubility , dilution , fractionation , chemistry , chromatography , ionic strength , food science , aqueous solution , organic chemistry , physics , thermodynamics
SUMMARY: Fractionation of muscle proteins of four varieties of fresh water fish after storage in ice was carried out by serial dilution of a buffer extract of ionic strength 0.55. Precipitation of actomyosin was complete at an ionic strength of 0.175 and fibrillar fraction at 0.05. In Ophiceohalus sp. the initial solubility of proteins was 91‐93%. The solubility fell to 82% by the 5th day and increased on further storage up to 13 days. Further storage indicated a fall in solubility. The fall in solubility on the 5th day coincided with the highest level of actomyosin and maximum rigor rigidity of the round fish. Actin solubility in buffer showed the same pattern as solubility of total proteins. The quantity of actin not reconvertible into f‐actin showed an increase during storage. Viscosity of buffer extracts showed an increase during development of rigor and decrease on further storage as reflected by level of preformed actomyosin.