• 한국수산과학회지
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• 제38권2호
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• pp.83-88
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• 2005

Protease inhibitors were purified from the eggs of Alaska pollock (Theragra chalcogramma) using the following purification steps: ammonium sulfate precipitation, ion exchange, gel permeation, and high performance liquid chromatographies (HPLC). The protease inhibitor from the heated eggs of Alaska pollock was not as well purified. In addition, the heated eggs showed lower specific inhibitory activity than the unheated eggs. The purification yields after ammonium sulfate precipitation, ion exchange, and gel permeation chromatographies were 22.7$\%,\;15.3\%$,and $4.4\%$, respectively. There were two kinds of protease inhibitors on the gel permeation chromatography pattern Their molecular weights were estimated to be 66,700 and 16,000 Da, respectively. Both were classified as a cysteine protease inhibitor because of the existence of inhibiting papain, which is one of cysteine proteases.

• 한국식품영양과학회지
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• 제35권1호
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• pp.96-103
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• 2006

명태 절란을 원료로 한 명란훈연소시지의 품질특성은 다음과 같다. 대조구 및 셋 소시지에서 카라기난의 양이 많을 수록 hardness, cohesiveness, elasticity, brittleness 및 gumminess가 높게 측정되었고, 명란훈연소시지 제조시 setting은 텍스쳐 강도를 크게 증가시켰다. 셋 소시지에 있어서 원료성분의 최적 배합비율은 명태 절란, 전분 및 카라기난 함량이 각각 88.5, 5.0 및 $2.0\%$인 제품이 가장 좋게 나타났다. 모든 시료에서 pH는 저장 4개월째까지 증가하였다가 감소 하였으며, 진공 및 질소포장은 대조구보다 pH 변화가 낮았다. 휘발성염기질소량 및 TBA 값은 대조구는 저장기간이 증가할수록 증가하였으며, 진공 및 질소포장 제품은 저장 2개월째까지는 변화가 없었다가 저장 4개월째부터 저장기간이 증가할수록 다소 증가하였다. 총균수는 대조구가 진공 및 질소포장 제품에 비하여 저장기간 동안에 높은 수치를 나타내었으며, 대장균군은 모든 시료에서 저장기간 동안에 음성으로 나타나 대장균군에 의한 오염여부의 측면에서는 안전한 것으로 평가되었다.

• 한국식품과학회지
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• 제34권2호
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• pp.220-224
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• 2002

폐기물로 버려지는 명태 가공부산물인 절란을 효율적으로 이용할 수 있는 방안을 찾기 위해, 절란 젓을 제조하여 cellulose casing에 포장한 다음 숙성 중에 일어나는 여러 가지 화학적 및 미생물 변화를 측정하였다. 상온숙성$(25^{\circ}C)$에서는 냉장숙성$(5^{\circ}C)$보다 pH가 급격히 감소하는 것으로 나타났으며, 젖산량은 숙성이 진행됨에 따라 상온숙성에서는 급격한 증가를 보였고 냉장숙성에서는 서서히 증가하였다. 아미노태 질소는 상온숙성시 숙성기간 1주일째 급격한 증가 후 서서히 증가하였고 냉장숙성$(5^{\circ}C)$시 3주째까지 증가하다가 감소하였다. 휘발성 염기성 질소는 상온숙성$(25^{\circ}C)$시 급격한 증가를 보였고, 냉장숙성$(5^{\circ}C)$시 서서히 증가함을 보였다. 미생물의 변화는 상온숙성$(25^{\circ}C)$시 냉장숙성$(5^{\circ}C)$보다 미생물의 수치가 높았으며, 대장균군은 초기에 나타났다가 모두 제거되었다. 명태 절란젓의 최적 생산공정 및 유통기간 설정을 위해서는 관능검사 등을 통한 보충연구가 필요하다고 본다.

• 한국수산과학회지
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• 제46권4호
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• pp.351-358
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• 2013

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.

• 한국수산과학회지
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• 제44권5호
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• pp.435-442
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• 2011

This study was conducted to optimize the processing of high quality surimi gel from unmarketable cultured bastard halibut Paralichthys olivaceus. According to endogenous enzyme activity and processing optimization, high quality surimi gel from unmarketable cultured bastard halibut was prepared by mixing 3.0% (w/w) salt, 2.4% (w/w) starch, 5.0% (w/w) egg white and 4.8% (w/w) ice water in a Stephan mixer, set at $5^{\circ}C$ for 24 h, followed by boiling for 30 min, and finally cooling for 30 min. The strength of the surimi gel from unmarketable cultured bastard halibut prepared by the above processing method was $1,257\;g{\times}cm$, which was 33% higher than that of a commercial surimi gel from Alaska pollock, grade SA.

• 한국수산과학회지
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• 제46권2호
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• pp.119-128
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• 2013

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.

• 한국수산과학회지
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• 제53권3호
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• pp.403-416
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• 2020

The purpose of this study was to evaluate the food functional properties and in vitro bioactivity of vacuum freeze-dried fish roe concentrates (FRCs) prepared from Alaska pollock Theragra chalcogramma (AP), bastard halibut Paralichthys olivaceus (BH) and skipjack tuna Katsuwonus pelamis (ST). All three species showed better buffering capacity on the alkaline side (pH 10-12) than on the acidic side. The water-holding capacities of the FRCs were 3.5, 8.5 and 4.2 g/g protein for AP, BH and ST, respectively, and were significantly higher than that of commercial egg white. The protein solubilities of the FRCs were 42.5% (AP), 50.0% (BH) and 13.9% (ST). The foaming capacities of the FRCs were not significantly different among the species (128.0% for AP, 128.3% for BH, and 143.3% for ST; P>0.05), and their foam stability was maintained at 53.0-74.2% for 60 minutes. The oil-in-water emulsifying activity indexes of AP and BH (19.5 and 20.2 ㎡/g protein, respectively) were significantly superior to that of ST (P<0.05). The 2,2-diphenyl-1-picrylhydrazyl and 2,2'-azino-bis-3-ethylbenzothia-zoline-6-sulfonic acid radical-scavenging activities (IC₅₀, mg/mL) of the FRCs were in the ranges of 1.05-3.26 and 0.13-0.18 mg/mL, respectively, and the angiotensin I converting enzyme inhibitory activity was in the range of 0.97-1.89 mg/mL.