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http://dx.doi.org/10.5657/KFAS.2013.0119

Fractionation and Characterization of Protease Inhibitors from Fish Eggs Based on Protein Solubility  

Kim, Hyeon Jeong (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)
Song, Sang Mok (Department of Food & Nutrition/Institute of Marine Industry, Gyeongsang National University)
Kim, Il Yong (Department of Food & Nutrition/Institute of Marine Industry, Gyeongsang National University)
Park, Sung Hwan (Department of Food & Nutrition/Institute of Marine Industry, Gyeongsang National University)
Gu, Eun Ji (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)
Kim, Jin-Soo (Department of Seafood Science & Technology/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.2, 2013 , pp. 119-128 More about this Journal
Abstract
A protease inhibitor was fractionated from fish eggs using methods based on protein solubility. Fractionation efficiency was evaluated with regard to percent recovery and total inhibitory activity (U). The fractionation of protease inhibitor (PI) from egg extracts of skipjack tuna (ST, Katsuwonus pelamis), yellowfin tuna (YT, Thunnus albacores), and Alaska pollock (AP, Theragra chalcogramma) was performed by precipitation with cold acetone or ammonium sulfate (AS). Fractions exhibiting the strongest inhibitory activity contained 20-40% (v/v) cold acetone or 40-60% saturated AS fractions. AS fractionation was more effective in isolating PI than was precipitation with acetone. The total inhibitory activity and percent recovery of fraction obtained with AS 40-60% toward trypsin and $N{\alpha}$-benzoyl-L-arginine-p-nitroanilide (BAPNA) were 4,976 U and 24.2% for ST, 3,331 U and 38.1% for YT, and 4,750 U and 43.8% for AP, respectively. In comparisons against six commercial proteases, 40-80% AS fractions, made by combining the 40-60% and 60-80% AS fractions from fish egg extract, exhibited the strongest inhibition of trypsin when using a casein substrate. These results suggest that fish eggs act as serine protease inhibitors and may be useful for protease inhibition in foodstuffs.
Keywords
Fractionation; Protease inhibitor; Fish eggs; Trypsin inhibitory activity;
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