Abstract
The physicochemical and functional characteristics of the major coconut storage protein, 11S globulin or cocosin, were investigated.Cocosin was purified by a combination of salt extraction, selective precipitation, and gel filtration chromatography. The solubility of cocosin at different pH was higher at µ=0.5 than at µ=0.08. The 24 and 21 kDa basic polypeptides of cocosin were more resistant to chymotrypsin digestion than the 35 and 32 kDa acidic polypeptides. Cocosin emulsions were most stable at 0 M NaCl, followed by emulsions in 0.1 M and 0.4 M NaCl. The available SH groups were found to be 21.6 mole SH/mole cocosin. Cocosin was observed to be stable under various pasteurization conditions from 63°C, 30 min to 100°C, 10 sec. However, heating at 100°C for 10 min and longer degraded cocosin up to 60%. The thermal denaturation midpoint temperature, Tm, of the trimeric cocosin was 77.6°C while that of the hexameric form was 100.5°C.
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