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KMID : 1007520030120020122
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Food Science and Biotechnology
2003 Volume.12 No. 2 p.122 ~ p.127
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Changes in Physicochemical Properties of Glycinin Due to Maleylation
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Kwon, Dae Young
Kim, Seran/Kim, Hye Young L./Kim, Kang Sung
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Abstract
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Conformation and functionality changes of soy glycinin due to maleylation were studied. Glycinin sequentially purified by isoelectric point precipitation, and ion exchange, adsorption, and gel filtration chromatographies were used. Purity of the final protein was over 95%. Physicochemical properties of glycinin was chemically changed by reacting the protein with maleic anhydride to 65 and 95% at the lysine residues. Accessigility of tyrosine and tryptophan residues increased as modification percent increased. Differential scanning calorimetry (DSC) result of native glycinin indicates that glycinin has high thermal stability. Enthalphy as obtained from DSC dropped from 3.4 cal/g native protein to 0 cal/g protein when lysine residues were maleylated above 65%, which indicates complete denaturation. Circular dichroism spectra of native and maleylated gllycinins show decrease in the ordered structure and increase in the unordered structure upon maleylation.
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