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KMID : 0903519850280020088
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Journal of the Korean Society of Agricultural Chemistry and Biotechnology
1985 Volume.28 No. 2 p.88 ~ p.91
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Solubility and Electrophoretic pattern of Korea Ginseng Protein
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Roh Seung-Moon
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Abstract
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For the systematic investigation of biochemical characteristics of Korean ginseng protein, protein fractions were analyzed by the techniques of sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis. The effect of pH and various salts on extractibility of ginseng protein were determined while the amino acid composition u-a studied by amino acid autoanalyzer. The protein was, consisted of 66.08% of albumin and 20.51% of glutelin. Extractability of ginseng protein was the lowest in pH 3.0 and the highest in pH 6.0∼8.0. Among the neutral salts solution, 0.4 M Na₂CO₃ showed maximum extractability while 1.0M MgSO₄ solution showed the least extractability. Resonable precipitation was obtained by 40% of acetone and ammonium sulfate. It has been shown by SDS polyacrylamide gel electrophoresis Thai the soluble protein had 11 bands. The molecular weight for the main protein of the soluble protein wasestimated to be 43,000. In amino acid composition of water extracted protein, arginine content was the highest 47.17% while on the contray, proline and cystine contents were very low.
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