earticle

논문검색

포스터 발표 : 식품 및 바이오신소재

Purification and characterization of an angiotensin-I-converting enzyme inhibitory peptide from seaweed pipefish, Syngnathus schlegeli

원문정보

Isuru WIJESEKARA, Zhong-Ji QIAN, Bo-Mi RYU, Se-Kwon KIM

한국생물공학회 한국생물공학회 학술대회 2010 춘계학술대회 및 국제심포지움 2010.04 pp.162-162
피인용수 : 0건 (자료제공 : 네이버학술정보)

초록

영어

Angiotensin-I-converting enzyme (ACE-I) inhibitory peptide (SPP) was isolated from the seaweed pipefish muscle protein. Papain, Alcalase, Neutrase, pronase, pepsin and trypsin were used to hydrolyze seaweed pipefish muscle protein and among them the Alcalase hydrolysate exhibited the highest ACE-I inhibitory activity. The Alcalase hydrolysate was separated in to three fractions (F1, F2 and F3) by fast protein liquid chromatography on a Hiprep 16/10 DEAE FF anion exchange column. Among three fractions, F1 has shown the highest ACE-I inhibitory
activity and it was further purified using reverse-phase high performance liquid chromatography on a Primesphere 10 C18 (20 × 250 mm) column. The purified peptide SPP has shown potent ACE-I inhibitory activity, which might be incorporated as a functional ingredient in functional
foods.

키워드

저자정보

  • Isuru WIJESEKARA Department of Chemistry, Pukyong National University,.
  • Zhong-Ji QIAN Marine Bioprocess Research Center, Pukyong National University.
  • Bo-Mi RYU Department of Chemistry, Pukyong National University,.
  • Se-Kwon KIM Department of Chemistry, Pukyong National University,. Marine Bioprocess Research Center, Pukyong National University.

참고문헌

자료제공 : 네이버학술정보

    함께 이용한 논문

      ※ 원문제공기관과의 협약기간이 종료되어 열람이 제한될 수 있습니다.

      0개의 논문이 장바구니에 담겼습니다.