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Conformation of Soymilk Protein Treated by Pretense  

변진원 (수원여자대학 식품영양과)
Publication Information
The Korean Journal of Food And Nutrition / v.15, no.4, 2002 , pp. 331-336 More about this Journal
Abstract
Conformation of soymilk protein was examined to obtain basic information for improved calcium intolerence of soymilk protein partially hydrolyzed with protease. Surface hydrophobicities of three proteins showed the order of SMP(soymilk protein) < SPI(soy protein isolate) < PT-SMP(protease treated soymilk protein). Total thiol group contents of SMP and PT-SMP were similar but larger than that of SPI. Reducing rate of disulfide bond in PT-SMP after 2-mercaptoethanol treatment was laster than that in SMP. And so, this result indicates that PT-SMP may be less compacting due to protease treatement. From circular dichroism result, PT-SMP showed different pattern from SMP and SPI suggesting change of secondary structure by hydrolysis. And analysis of heat denaturating property by DSC showed that denaturation enthalpy of three proteins were all small. Especially enthalpy of PT-SMP was least, and this result suggested that PT-SMP was denatured easily by heating due to less compacting structure.
Keywords
soymilk protein; pretense treatment; surface hydrophobicity; thiol group; circular dichroism; DSC;
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