ISSN:
1365-2621
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Process Engineering, Biotechnology, Nutrition Technology
Notes:
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.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1365-2621.1988.tb00595.x
Permalink
