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Purification and Characterization of Angiotensin Ⅰconverting Enzyme Inhibitory Peptides from the Rotifer, Brachionus rotundiformis

첫 페이지 보기
  • 발행기관
    한국생물공학회 바로가기
  • 간행물
    한국생물공학회 학술대회 바로가기
  • 통권
    2007 추계학술대회 및 국제심포지엄 (2007.10)바로가기
  • 페이지
    pp.11-12
  • 저자
    Jung-Kwon Lee, Hae-Jin Wo, Joong-Kyung Jeon, Se-Kwon Kim, Hee-Guk Byun
  • 언어
    영어(ENG)
  • URL
    https://www.earticle.net/Article/A100037

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원문정보

초록

영어
Recently, functional materials have been screened from protein hydrolysates of various fishery sources, and a number of functional peptides have been identified. The peptides isolated from protein hydrolysates were studied to determine the bioactive substances such as antioxidative activity, angiotensinⅠ converting enzyme (ACE) inhibitor activity and antibiotic activity1). The peptides regulating blood pressure are known to be potent inhibitors of ACE. Rotifers are
commonly used as live feed for fish. Larval fish generally have a high demand for dietary protein due to their high growth rates, and extensive catabolism of amino acids for the production of metabolic energy2). In this study, the hydrolysates of the peptides from the rotifer, Brachionus
rotundiformis were investigated for ACE inhibitors. The proximate compositions of the rotifer were measured to be 63.25% crude protein, 17.77% lipid, 7.72% carbohydrate, 6.54% moisture, and 4.72% ash. In addition, the major amino acid composition of the rotifer was glutamic acid (11.14%), aspartic acid (9.93%), leucine (9.69%), and glycine (8.47%). The rotifer protein was hydrolyzed using Alcalase, α-chymotrypsin, Neutrase, pepsin, papain, and trypsin in a batch
reactor. Among the six hydrolysates, the peptic hydrolysate had the highest ACE inhibitory activity compared to the other hydrolysates. The peptides with strong ACE inhibitory activity were isolated from the hydrolysate using consecutive chromatographic methods including Sephadex G-25 Gel-chromatography and high-performance liquid chromatography. Further study is planned to analyze the amino acid sequence of peptides purified from the peptic hydrolysates of the rotifer.

저자

  • Jung-Kwon Lee [ Faculty of Marine Bioscience and Technology, Kangnung National University ]
  • Hae-Jin Wo [ Faculty of Marine Bioscience and Technology, Kangnung National University ]
  • Joong-Kyung Jeon [ Faculty of Marine Bioscience and Technology, Kangnung National University ]
  • Se-Kwon Kim [ Department of Chemistry, Pukyong National University ]
  • Hee-Guk Byun [ Faculty of Marine Bioscience and Technology, Kangnung National University ]

참고문헌

자료제공 : 네이버학술정보

간행물 정보

발행기관

  • 발행기관명
    한국생물공학회 [The Korean Society for Biotechnology and Bioengineering]
  • 설립연도
    1984
  • 분야
    공학>생물공학
  • 소개
    이 법인은 생물 공학의 발전과 보급에 이바지하고, 회원 상호 간의 연구 협력과 친목을 도모함을 목적으로 한다 1. 생물공학 분야의 발전을 위한 연구 협력 2. 생물공학의 실용화를 촉진시키기 위한 산학 협동 3. 학술연구 발표회, 강연회, 연수회 등 학술활동의 개최 4. 국,영문 학술지,소식지,학술회의 Proceedings 및 학술도서의 발간 5. 생물공학 발전을 위한 정책 건의 6. 기타 국제 교류 등 본 학회의 목적 달성을 위한 제반 활동

간행물

  • 간행물명
    한국생물공학회 학술대회
  • 간기
    반년간
  • 수록기간
    1985~2013
  • 십진분류
    KDC 476 DDC 576

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