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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) < SP...
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RISS 인기검색어
부가정보
다국어 초록 (Multilingual 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 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 lee compacting structure.
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 lee compacting structure.
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분석정보
인용정보 인용지수 설명보기
학술지 이력
| 연월일 | 이력구분 | 이력상세 | 등재구분 |
|---|---|---|---|
| 2026 | 평가예정 | 재인증평가 신청대상 (재인증) | |
| 2020-01-01 | 평가 | 등재학술지 유지 (재인증) |  |
| 2017-01-01 | 평가 | 등재학술지 유지 (계속평가) | |
| 2013-01-01 | 평가 | 등재 1차 FAIL (등재유지) | |
| 2010-01-01 | 평가 | 등재학술지 유지 (등재유지) | |
| 2007-01-01 | 평가 | 등재학술지 선정 (등재후보2차) | |
| 2006-01-01 | 평가 | 등재후보 1차 PASS (등재후보1차) |  |
| 2005-01-01 | 평가 | 등재후보학술지 유지 (등재후보1차) | |
| 2003-01-01 | 평가 | 등재후보학술지 선정 (신규평가) | |
학술지 인용정보
| 기준연도 | WOS-KCI 통합IF(2년) | KCIF(2년) | KCIF(3년) |
|---|---|---|---|
| 2016 | 0.55 | 0.55 | 0.67 |
| KCIF(4년) | KCIF(5년) | 중심성지수(3년) | 즉시성지수 |
| 0.74 | 0.76 | 1.104 | 0.11 |
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