• Korean Journal of Fisheries and Aquatic Sciences
• /
• v.38 no.2
• /
• pp.83-88
• /
• 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.

• Journal of the Korean Society of Food Science and Nutrition
• /
• v.35 no.1
• /
• pp.96-103
• /
• 2006

Alaska pollock roe is mainly used as the production salted instead of salt-seasoned seafood (Myungranjeot). Alaska pollock roes with broken egg membrane are usually discarded as a waste product. In order to utilize the broken roes of Alaska pollock, imitated fish sausage was manufactured for commercial production. Hardness, cohesiveness, elasticity, brittleness, and gumminess of Alaka pollock roe sausage were evaluated based on mixture design and regression models. The higher amounts of carrageenan and tile lower amounts of starch caused the higher the texture intensity of Alaska pollock roe sausage. The pHs of control, vacuum and $N_2$ packages, increased up to 6.28, 6.23 and 6.24, respectively, during 4 months storage and then decreased. The values of volatile basic nitrogen (VBN), thiobarbituric acid (TBA), and total viable cell counts increased during storage periods, while the parameters were higher in control than in vacuum and Na packages. Coliform bacteria was not detected in all treatments during storage periods.

• Korean Journal of Food Science and Technology
• /
• v.34 no.2
• /
• pp.220-224
• /
• 2002

Alaska pollock roe is mainly used for the production of salt-seasoned and fermented seafood (Myungran-jeot). Alaska pollock roes with broken egg membrane are usually discarded as a waste product. In this study, the broken roes of Alaska pollock were salt-seasoned and stuffed into cellulose casing for commercial production. The chemical and microbial changes of the broken roes of Alaska pollock stuffed into cellulose casing fermented at 5 and $25^{\circ}C$, respectively, were analyzed at different ripening periods. On 5 week fermentation, pH decreased down to 5.60 and 5.10 at 5 and $25^{\circ}C$, respectively, but the amounts of lactic acid, amino-nitrogen, and volatile basic nitrogen increased continously as ripening period increased, higher at 25 than $5^{\circ}C$. The amounts of amino-nitrogen, 620 and 780 mg/100 g, were the highest on 3 week fermentation at $5^{\circ}C$ and on 1 week at $25^{\circ}C$, respectively. The numbers of total viable cell and lactic acid bacteria, $3.1{\times}10^6$ and $3.1{\times}10^5\;CFU/g$ at $5^{\circ}C$, and $1.9{\times}10^7$ and $2.8{\times}10^6\;CFU/g$ at $25^{\circ}C$, respectively, were the highest on 2 week fermentation.

• Korean Journal of Fisheries and Aquatic Sciences
• /
• v.46 no.4
• /
• pp.351-358
• /
• 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.

• Korean Journal of Fisheries and Aquatic Sciences
• /
• v.44 no.5
• /
• pp.435-442
• /
• 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.

• Korean Journal of Fisheries and Aquatic Sciences
• /
• v.46 no.2
• /
• pp.119-128
• /
• 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.

• Korean Journal of Fisheries and Aquatic Sciences
• /
• v.53 no.3
• /
• pp.403-416
• /
• 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.