Earticle

초록

영어

The angiontensin converting enzyme (ACE) inhibitory peptides were separated from beef sarcoplasmic protein extract and their amino acid sequences were identified as GFHI, DFHINQ, FHG, and GLSDGEWQ. The 4 peptides were synthesized in a laboratory and the ACE inhibitory activities of pep tides was measured after 2 months of storage at 4℃ under different pH conditions (6.0, 6.5, 7.0, 7.5, and 8.0) and the exposure of different temperatures (70, 80, 90, and 100℃) for 20 min to evaluate industrial use. No significant difference was detected by pH and temperature abuse for 20 min during storage. When the synthetic peptides were digested by pepsin, trypsin, and chymotrypsin, the ACE inhibitory activity was not changed. These results indicated that the 4 synthetic peptides with ACE inhibitory activity were pH-stable, heat-stable, and resistant to proteinases in gastro-intestinal tracts. Therefore, those 4 peptides can be used as a source for functional food product with various applications.

목차

Abstract
 Introduction
 Materials and Methods
 Results and Discussion
 Acknowledgments
 References

키워드

저자

• Jang, Ae-Ra [ Department of Food and Animal Biotechnology, Seoul National University ]
• Jo, Cheo-Run [ Department of Animal Science and Biotechnology, Chungnam National University ]
• Lee, Moo-Ha [ Department of Food and Animal Biotechnology, Seoul National University ]

참고문헌

발행기관

간행물

표지보기 관심저널 등록

• 간행물명

  Food Science and Biotechnology

• 간기

  격월간

• pISSN

  1226-7708

• 수록기간

  1992~2009

• 십진분류

  KDC 574 DDC 664