• Korean Journal of Fisheries and Aquatic Sciences
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• v.46 no.4
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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.

• Fisheries and Aquatic Sciences
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• v.19 no.5
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• pp.25.1-25.8
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• 2016

The fractionation of serine protease inhibitor (SPI) from fish roe extracts was carried out using polyethylene glycol-4000 (PEG4000) precipitation. The protease inhibitory activity of extracts and PEG fractions from Alaska pollock (AP), bastard halibut (BH), skipjack tuna (ST), and yellowfin tuna (YT) roes were determined against target proteases. All of the roe extracts showed inhibitory activity toward bromelain (BR), chymotrypsin (CH), trypsin (TR), papain-EDTA (PED), and alcalase (AL) as target proteases. PEG fractions, which have positive inhibitory activity and high recovery (%), were the PEG1 fraction (0-5 %, w/v) against cysteine proteases (BR and PA) and the PEG4 fraction (20-40 %, w/v) against serine proteases (CH and TR). The strongest specific inhibitory activity toward CH and TR of PEG4 fractions was AP (9278 and 1170 U/mg) followed by ST (6687 and 2064 U/mg), YT (3951 and 1536 U/mg), and BH (538 and 98 U/mg). The inhibitory activity of serine protease in extracts and PEG fractions from fish roe was stronger than that of cysteine protease toward common casein substrate. Therefore, SPI is mainly distributed in fish roe and PEG fractionation effectively isolated the SPI from fish roes.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.51 no.4
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• pp.351-361
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• 2018

This study investigated the potential of collagenous protein fractions (CPFs) as functional foods. The specific CPFs studied were recovered from the roe of bastard halibut (BH), Paralichthys olivaceus; skipjack tuna (ST), Katsuwonus pelamis; and yellowfin tuna (YT), Thunnus albacares through the alkaline solubilization process at pH 11 and 12. The buffer capacity, water-holding capacity and solubility of CPFs with pH-shift treatment were significantly better at alkaline pH (10-12) than at acidic pH (2.0). At pH-shift treatment (pH 2 and 12), the foaming capacities of CPFs from ST and YT were improved compared to those of controls, but they were unstable compared to BH CPFs. The emulsifying activity index (EAI, $m^2/g$ protein) of CPFs (controls) was 16.0-21.1 for BH, 20.1-23.9 for ST and 9.3-13.7 for YT (P<0.05). CPFs adjusted to pH 12 showed improved EAI and YT CPFs showed significantly greater emulsifying ability than those from BH and ST. CPFs recovered from fish roe are not only protein sources but also have a wide range of food functionalities, confirming the high availability of fish sausage and surimi-based products as protein or reinforcing materials for functional foods and alternative raw materials.

• Journal of Fisheries and Marine Sciences Education
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• v.7 no.2
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• pp.182-200
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• 1995

Thirty two vessels of the Korean purse seiner had been operated in the Western Pacific Ocean for mainly skipjack tuna, Katsuwonus pelmis LINNAEUS and yellowfin tuna, Thunnus albacares BONNATERRE from January to December in 1991. Among them, fourteen vessels were chosen for this research. During the year their daily operated vessels totalled 4,153 vessels, their total casting net were 2,982 times, in caught 1,798 times, and their total catch was 106,300 M/T. We investigate the distribution of their catch by species, by body size, and by surfance water temperature, and also investigate the distribution of their catch by month and section of the sea, where the sections are separated by 30' of longitude and latitude from the monthly operated sea. We summarize these as follows : 1. The rate of catch by species is 75r/o skipjack tunas, 22.3% yellowfin tunas, and 2.7% bigeye and other tunas. 2. Of the caught skipjack tunas, those of weight 2.0~10kg are most and 68%, those of 1.5~8kg are 11.6%, and those of 3.0~8kg are 9.9%. Of the caught yellowfin tunas, those of weight 5~50kg and 10~50kg are most and 23.1%, and 28.3% respectively, those of 20~50kg are 15.8%, weight 30~50kg are 12.5%, and weight 2~50kg are 9.7%. 3. On the distribution of catch by surface water temperature, 49% of catch are taken between $29.0^{\circ}C$ and $29.4^{\circ}C$, 37% are taken between $29.5^{\circ}C$ and $29.9^{\circ}C$, and about 6% are taken between $28.5^{\circ}C$ and $28.9^{\circ}C$, but very little, only about 1% are taken below $28.4^{\circ}C$ and above $30.5^{\circ}C$. 4. On the distribution of catch by month and section of sea, skipjack tunas are most caught 10,618M/T in August and 10,412M/T in September in the section of Lat. $3^{\circ}{\sim}6^{\circ}S$ and Long. $174^{\circ}E{\sim}176^{\circ}W$, caught much 8,825M/I' in June and 8,057M/T in January in section of Lat. $1^{\circ}S{\sim}3^{\circ}N$ and Long. $142^{\circ}{\sim}151^{\circ}$E, but caught very little in May, November and December in the costal area of New Guinea. Yellowfin tunas are mostly caught 4,070M/T in June in the section of Lat. $0^{\circ}{\sim}4^{\circ}$N and Long. $142^{\circ}{\sim}151^{\circ}$E, and caught much over 2,000M/T in February~April and October~December in the section of coastal area and near islands, but caught very little in distant water area.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.50 no.5
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• pp.506-519
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• 2017

This study evaluated the protein recovery and functional properties and biological activity of boiled and steamed process water (BPW and SPW, respectively) generated from the preparation of concentrated roe of bastard halibut (BH; Paralichthys olivaceus), skipjack tuna (ST; Katsuwonus pelamis), and yellowfin tuna (YT; Thunnus albacares) using the cook-dry process. The protein loss from the water extracts (EXT) of 100 g of roe protein was 15.05-19.71% and was significantly (P<0.05) higher than that of BPW (5.47-10.34%) and SPW (3.88-8.18%). The foam capacity of BPW (166-203%) and SPW (15-194%) was better than that of EXT. The emulsifying activity index of the original samples was lower than those ($15.40-107.86m^2/g$) of diluted protein samples. The 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical scavenging activity and the reducing power of BPW and SPW were stronger than those of EXT. The 2,2'-azino-bis-3-ethylbenzothiazoline-6-sulfonic acid ($ABTS^+$) radical scavenging activity of EXT (0.028-0.045mg/mL) was significantly higher those of BPW and SPW. The angiotensin I-converting enzyme (ACE) inhibitory activity of SPW was the highest for BH (1.04 mg/mL), followed by YT and ST. The predominant amino acids in SPW were Glu, Ala, Leu, and His. These results demonstrate that processing water containing diluted organic components, including protein, can be consumed directly by humans as a functional reinforcing material after appropriate concentration processes.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.46 no.2
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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.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.50 no.6
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• pp.694-706
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• 2017

This study evaluated the protein recovery, functional properties and biological activity of isolate processed water (IPW) generated in the preparation of protein isolates from fish roes (BH, bastard halibut Paralichthys olivaceus; ST, skipjack tuna Katsuwonus pelamis; YT, yellowfin tuna Thunnus albacares) by an isoelectric solubilization and precipitation process. The IPWs contained 2.7-5.4 mg/mL of protein, and the protein losses were 8-21% (P<0.05). The form capacity of IPW-3 for BH and ST, and IPW-4 for YT was 155, 194, and 164%, respectively. The emulsifying activity index ($27-43m^2/g$) of the YT-IPWs was the strongest, followed by ST ($7-29m^2/g$) and BH ($10-19m^2/g$). The 2,2-diphenyl-1-picrylhydrazyl scavenging activities of IPW-1 and -3 were higher than those of IPW-2 and -4. The 2,2'-azino-bis-3-ethylbenzothiazoline-6-sulfonic acid scavenging activity ($IC_{50}$, mg/mL) of IPW-2 and -4 was 0.03 mg/mL for BH, 0.04-0.08 mg/mL for ST, and 0.04-0.07 mg/mL for YT. BH IPW-3 had the strongest reducing power (0.41 mg/mL) and superoxide dismutase-like activity (1.68 mg/mL). The angiotensin-I converting enzyme inhibitory activity of IPW-3 was the highest for ST (1.52 mg/mL), followed by BH and YT. The common predominant amino acids in the IPWs were the essential amino acids Val, Leu, Lys, and Arg and the non-essential amino acids Ser, Glu, and Ala.