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KMID : 0903519860290020212
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Journal of the Korean Society of Agricultural Chemistry and Biotechnology
1986 Volume.29 No. 2 p.212 ~ p.218
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Studies on the Removal of Phytate from Korean Rapeseed(Brassica napus , L) Proteins
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Abstract
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Proteins in Korean rapeseeds, as in many other plantseeds, are usually bound to phytate molecules. These phytate-bound proteins are of little value as foodstuffs because of their poor solubility in digestive systems. Therefore it is necessary to remove phytates from proteins in order to convert these proteins io a useful foodstuff.
In the work, an efficient procedure for removal of phytates from defatted Korean rapeseed was found.
The influence of pH on the solubility of protein and phytate of rapeseed flour showed that the former was the lowest at pH 5.0 and began to increase as pH further raised. Meanwhile, the latter was the highest at pH 6.0, however, it was decreased abruptly at alkaline pH, especially to content of 1.3% at pH 11.5.
The solubility cf protein was relatively high in NaCl aqueous solution at pH 6.0∼8.0, and did not male any noticeable difference depending on NaCl concentration. On the other hand, the solubility of phytate was high at pH of below 6.0 showing an abrupt decrease at pH of above 6.0.
The solubility of protein in CaCl₂ aqueous solution was highest at pH 6.0∼8.0, however, there was no significant change at the whole range of tested pH of the solution. A maximum solubility of phytate was shown at pH 3.0∼4.0. And it was decreased abruptly at a higher pH of the above range and also decreased at a lower pH with higher CaCl₂ concentration.
The solubility of phytate in Na₂SO₃ aqueous solution was highest at pH 5.0∼8.0. As the concentration goes up the maximum value of solubility was found to move to higher pHs. Depending on the concentration of Na₂SO₃, the decreasing pattern was changed in an alkaline solution.
The solubility of phytate in the solution containing low concentration of Ca^(2+) ion was low in all treatments at pH of above 7.0 and showed the maximum value at low pH as Ca^(2+) ion concentration increases.
The solubility of protein at pH 11.5 showed the highest value in 1mM Ca^(2+) ion solution.
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