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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 발행연도
- 2007.8
- 수록면
- 565 - 571 (7page)
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This study was carried out to investigate an optimum condition for the high angiotensin-I converting enzyme (ACE) inhibitory activity and the yield on enzyme concentration, casein concentration, and hydrolysis time. The optimum condition was performed by response surface methodology for acquirement of casein hydrolysate of milk which shows high ACE inhibitory activity. Among 8 tested enzymes, Protamex showed the highest activation degree with 77.03 unit/g from casein. Their hydrolysis degrees of flovourzyme 500MG, protamex, mixture from 1% casein were 85.5, 88.5, and 93.5%, respectively. The ranges of enzyme concentration (0.25-1.25%), casein concentration (2.5-12.5%), and hydrolysis time (20-100 min) as 3 independent variables through preliminary experiments of the yield of casein hydrolysate and ACE inhibitory activity, and it shows optimum response surface at a saddle point. It shows enzyme concentration (0.64%), casein concentration (8.38%), and hydrolysis time (55.81 min) in the yield aspect and showed the highest activity at enzyme concentration (0.86%), casein concentration (5.97%), and hydrolysis time (63.86 min) in ACE inhibitory aspect. The R2 value of a fitted optimum formula on the hydrolysis yield was 0.9751 as the significant level of 1%. The R2 value of a fitted optimum formula on ACE inhibitory activity is 0.8398, and the significance is recognized in the range of 5%.
목차
Abstract
Introduction
Materials and Methods
Results and Discussion
References
참고문헌 (17)
참고문헌 신청
Cushman DW , 1971 , Spectrophotometric assay andproperties of the angiotensin-converting enzyme of rabbit lung : 1637 ~ 1648
Webster J , 1996 , Aspects of tolerability of centrally actingantihypertensive drugs 3 : S49 ~ S54
Mulaly M , 1997 , Identification of a novelangiotensin-I-converting enzyme inhibitory peptide correspondingto a tryptic fragment of bovine beta-lactoglobulin 3 : 99 ~ 101
Miyoshi S , 1991 , Structures and activity of angiotensin-converting enzyme inhibitorsin an alpha-zein hydrolysate : 1313 ~ 55 1318
Matsui T , 1993 , Inhibition of angiotensin I-converting enzyme by Bacilluslicheniformis alkaline protease hydrolyzates derived from sardinemuscle : 922 ~ 925
Webster J , 1996 , Aspects of tolerability of centrally actingantihypertensive drugs 3 : S49 ~ S54
Mulaly M , 1997 , Identification of a novelangiotensin-I-converting enzyme inhibitory peptide correspondingto a tryptic fragment of bovine beta-lactoglobulin 3 : 99 ~ 101
Miyoshi S , 1991 , Structures and activity of angiotensin-converting enzyme inhibitorsin an alpha-zein hydrolysate : 1313 ~ 55 1318
Matsui T , 1993 , Inhibition of angiotensin I-converting enzyme by Bacilluslicheniformis alkaline protease hydrolyzates derived from sardinemuscle : 922 ~ 925
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UCI(KEPA) : I410-ECN-0101-2013-573-001023208