연구논문 : 어류 알로부터 Protease Inhibitors의 크로마토그래피법에 의한 분획
분야
수해양 > 수산생물학
저자
김진수 ( Jin Soo Kim ) , 김기현 ( Ki Hyun Kim ) , 김현정 ( Hyeon Jeong ) , 김민지 ( Min Ji Kim ) , 박성환 ( Sung Hwan Park ) , 이현지 ( Hyun Ji Lee ) , 허민수 ( Min Soo Heu )
발행기관
한국수산과학회(구 한국수산학회)
간행물정보
한국수산과학회지 2013년, 제46권 제4호, 351~358페이지(총8페이지)
파일형식
05907536.pdf [무료 PDF 뷰어 다운로드]
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    영문초록
    A protease inhibitor from fish eggs was fractionated using chromatographic methods. The fractionation efficiency was evaluated in terms of specific inhibitory activity (SIA, U/mg), purity (fold), total inhibitory activity (TIA, U), and recovery (%). The protease inhibitor (PI) from egg extracts of skipjack tuna (ST Katsuwonus pelamis), yellowfin tuna (YT Thunnus albacares) and Alaska pollock (AP Theragra chalcogramma) was fractionated using Sephadex G-50 gel filtration and DEAE-Sepharose CL-6B anion exchange chromatography based on protein size exclusion and net charge, respectively. Fractions exhibiting strong inhibitory activity were contained in the 30-50 kDa fraction on gel filtration and in the range of 0.4-0.7 M NaCl gradient fraction on anion exchange chromatography. The respective TIA and percent recovery of the fraction obtained with gel filtration toward trypsin and Nα-benzoyl-L-arginine-pnitroanilide (BAPNA) were 2,758.7 U and 29.6% for ST, 1,005.5 U and 25.6% for YT, and 1,267.5 U and 26.0% for AP. Gel filtration chromatography was more effective at fractionating PI than using ion exchange chromatography. These results suggest that fish eggs act as serine protease inhibitors and might be useful for protease inhibition in foodstuffs.
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