본 연구는 두유에 칼슘을 강화하고자 두유단백질의 칼슘내인성을 높이기 위한 방법으로 단백분해효소를 처리한 경우 효소처리 전, 후에 나타나는 단백질의 구조적 특성을 비교 분석하였다. 표면소수도는 MP

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 faster than that in SMP. And so, this result indicates that PT-SMP may be less compacting due to protease treatment. 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.