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A circular dichroism study of the effect of some organic solvents on the actomyosin of sardine (Sardinops melanosticta)
Author(s) -
WON M. PEREZ,
IYAMA S.,
SHINOHARA K.,
MURAKAMI H.,
OMURA H.
Publication year - 1988
Publication title -
international journal of food science and technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.831
H-Index - 96
eISSN - 1365-2621
pISSN - 0950-5423
DOI - 10.1111/j.1365-2621.1988.tb00595.x
Subject(s) - sardine , circular dichroism , chemistry , dichloromethane , defatting , aqueous solution , random coil , butanol , solvent , ethanol , methanol , chromatography , crystallography , organic chemistry , biology , fishery , fish <actinopterygii>
Summary Circular dichroism (CD) was used to study changes in conformation of sardine ( Sardinops melanosticta ) actomyosin after treatment with some organic solvents. Untreated sardine actomyosin showed two negative bands at 208 and 222 nm, typical of proteins possessing α‐helix configurations. The water‐miscible alcohols methanol, ethanol, isopropanol and n‐butanol, and the water‐immiscible solvents n‐hexane, n‐octanol, and dichloromethane altered the native conformation of sardine actomyosin. The degree of alteration of native sardine actomyosin was principally dependent on the alcohol concentration and temperature used for dewatering. The least damage occurred with isopropanol, or with 10 or 90% aqueous ethanol; most damage occurred with 40–50% aqueous ethanol. Dichloromethane and n‐butanol increased the α‐helical content of the native protein. Treatment with hydrophilic and hydrophobic solvents at 70 and 20°C unfolded the protein to form a random coil, but defatting treatment at 2°C caused little damage.