Blackwell Publishing Journal Backfiles 1879-2005
Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
Process Engineering, Biotechnology, Nutrition Technology
Bovine SH-k-casein (k-C-pool) was fractionated into five components based on carbohydrate and sialic acid contents (k-C-P1 〈 k-C-P2 〈 k-C-P3 〈 k-C-P4 〈 k-C-P5) by ion-exchange chromatography (DEAE-cellulose). Chymosin susceptibility observed by monitoring changes in optical density during enzyme action, varied among the components. This was a reflection of the difference in self-association of the proteins in aqueous dispersion as determined by hydrophobic interaction chromatograph. There was an inverse relationship between surface hydrophobicity of the protein polymers (k-C-P2 〉k-C-P3 〉k-C-P4 〉 k-C-P5 〉 k-C-P4 〉 k-C-pool) and their susceptibility to chymosin at 37°C, pH 6.8 (k-C-pool 〉k-C-P1 〉k-C-P5 〉 k-C-P4 〉 k-C-P3 〉 k-C-P2). Mild heating decreased susceptibility and affected flocculation of all except the highly glycosilated components k-C-P4 and k-C-P5 reflecting amphipathicity imparted thermostability.
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