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http://dx.doi.org/10.5657/KFAS.2013.0351

Chromatographic Fractionation of Protease Inhibitors from Fish Eggs  

Kim, Jin-Soo (Department of Seafood Science & Technology/Institute of Marine Industry, Gyeongsang National University)
Kim, Ki Hyun (Department of Seafood Science & Technology/Institute of Marine Industry, Gyeongsang National University)
Kim, Hyeon Jeong (Department of Seafood Science & Technology/Institute of Marine Industry, Gyeongsang National University)
Kim, Min Ji (Department of Seafood Science & Technology/Institute of Marine Industry, Gyeongsang National University)
Park, Sung Hwan (Department of Food & Nutrition/Institute of Marine Industry, Gyeongsang National University)
Lee, Hyun Ji (Department of Food & Nutrition/Institute of Marine Industry, Gyeongsang National University)
Heu, Min Soo (Department of Food & Nutrition/Institute of Marine Industry, Gyeongsang National University)
Publication Information
Korean Journal of Fisheries and Aquatic Sciences / v.46, no.4, 2013 , pp. 351-358 More about this Journal
Abstract
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 $N{\alpha}$-benzoyl-L-arginine-p-nitroanilide (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.
Keywords
Column chromatography; Fractionation; Protease inhibitor; Fish eggs; Trypsin inhibitory activity;
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Times Cited By KSCI : 5  (Citation Analysis)
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