• Fisheries and Aquatic Sciences
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• v.25 no.1
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• pp.31-39
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• 2022

To clarify the factors influencing the physical properties of fish after heat treatments, we investigated changes in the properties of proteins in the dorsal ordinary and dark muscle of yellowtail (Seriola quinqueradiata) heated under different conditions commonly used for the purposes of food hygiene. High-temperature/short-time heating (85℃ for 90 s and 75℃ for 60 s) affected the protein solubility more than low-temperature/long-time heating (63℃ for 30 min). Sodium dodecyl sulphate-polyacrylamide gel electrophoresis and differential scanning calorimetry showed that low-temperature/long-time heating reduced the degree of actin denaturation in fish compared with that by other heating conditions. In addition, collagen solubility was enhanced with low-temperature/long-time heating. Therefore, these results suggest that differences in the degree of actin and collagen denaturation are responsible for the enhanced meat tenderness and diminished meat shrinkage, resulting from low-temperature/long-time heating.

• Ocean and Polar Research
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• v.33 no.2
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• pp.159-169
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• 2011

Antifreeze proteins (AFPs) have ice binding affinity, depress freezing temperature and inhibit ice recystallization which protect cellular membranes in polar organisms. Recent structural studies of antifreeze proteins have significantly expanded our understanding of the structure-function relationship and ice crystal growth inhibition. Although AFPs (Type I-IV AFP from fish, insect AFP and Plant AFP) have completely different fold and no sequence homology, they share a common feature of their surface area for ice binding property. The conserved ice-binding sites are relatively flat and hydrophobic. For example, Type I AFP has an amphipathic, single ${\alpha}$-helix and has regularly spaced Thr-Ala residues which make direct interaction with oxygen atoms of ice crystals. Unlike Type I AFP, Type II and III AFP are compact globular proteins that contain a flat ice-binding patch on the surface. Type II and Type III AFP show a remarkable structural similarity with the sugar binding lectin protein and C-terminal domain of sialic acid synthase, respectively. Type IV is assumed to form a four-helix bundle which has sequence similarity with apolipoprotein. The results of our modeling suggest an ice-binding induced structural change of Type IV AFP. Insect AFP has ${\beta}$-helical structure with a regular array of Thr-X-Thr motif. Threonine residues of each Thr-X-Thr motif fit well into the ice crystal lattice and provide a good surface-surface complementarity. This review focuses on the structural characteristics and details of the ice-binding mechanism of antifreeze proteins.

• Food Science of Animal Resources
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• v.39 no.2
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• pp.229-239
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• 2019

The objectives of this study were to determine the interaction between porcine myofibrillar proteins and various gelatins (bovine hide, porcine skin, fish skin, and duck skin gelatins) and their impacts on gel properties of porcine myofibrillar proteins. Porcine myofibrillar protein was isolated from pork loin muscle (M. longissimus dorsi thoracis et lumborum). Control was prepared with only myofibrillar protein (60 mg/mL), and gelatin treatments were formulated with myofibrillar protein and each gelatin (9:1) at the same protein concentration. The myofibrillar protein-gelatin mixtures were heated from $10^{\circ}C$ to $75^{\circ}C$ ($2^{\circ}C/min$). Little to no impacts of gelatin addition on pH value and color characteristics of heat-induced myofibrillar protein gels were observed (p>0.05). The addition of gelatin slightly decreased cooking yield of heat-induced myofibrillar protein gels, but the gels showed lower centrifugal weight loss compared to control (p<0.05). The addition of gelatin significantly decreased hardness, cohesiveness, gumminess, and chewiness of heat-induced myofibrillar gels. Further, sodium dodecyl poly-acrylamide gel electrophoresis (SDS-PAGE) showed no interaction between myofibrillar proteins and gelatin under non-thermal conditions. Only a slight change in the endothermic peak (probably myosin) of myofibrillar protein-gelatin mixtures was found. The results of this study show that the addition of gelatin attenuated the water-holding capacity and textural properties of heat-induced myofibrillar protein gel. Thus, it could be suggested that well-known positive impacts of gelatin on quality characteristics of processed meat products may be largely affected by the functional properties of gelatin per se, rather than its interaction with myofibrillar proteins.

• Journal of fish pathology
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• v.9 no.2
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• pp.177-183
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• 1996

A new RNA virus isolated from abnormally swimming behavior has caused mortalities in salmonid fish (Oh et al., 1995 a), A reverse transcriptase (RTase) activity of the virus was determined by using poly r(A) : oligo d(T) as templete : primer. This RTase activity was associated with virus particles of buoyant density of 1.16 g/ml. The virus particles in sucrose fractions were enveloped and were about 85 nm diameter with central electron-dense core. The brain and kidney samples of artificially infected fish showed RTase activity. Virus particle associated proteins about 120, 80, 65, 61, 48, 42, 35, 30, 25, 19, and 15 kDa were observed when examined by polyacrylamide gel electrophoresis analysis. This study showed the presence of a new retrovirus in salmonid fish, which tentatively called RVS (Retrovirus of salmonid).

• KSBB Journal
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• v.18 no.6
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• pp.495-499
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• 2003

The effect of operating parameters (reaction temperature and time) and reaction modes (batch and semi-batch) on the behavior of amino acid production from hydrothermal decomposition of fish-derived wastes was investigated. The amino acids obtained in batch experiments at temperature of 250$^{\circ}C$ were mainly alanine (Ala) and glycine (Gly) at maximum yield of 65 and 28mg/g-dry fish, respectively. At relatively lower temperature of 200$^{\circ}C$, the yield of high-molecular-weight amino acids such as aspartic acid (Asp) and serine (Ser) is high, but decreases as temperature increases. It is likely that high-molecular-weight amino acids decompose faster than low-molecular ones. Semi-batch mode of reaction suppressed decomposition of amino acids into organic acids (or volatile materials) by continuously removing the products from the reaction zone as soon as they are formed. Thus, large amount of high-molecular-weight amino acids such as Asp and Ser at this reaction mode was observed.

• Journal of fish pathology
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• v.25 no.3
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• pp.165-172
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• 2012

Vibrio alginolyticus (V. alginolyticus), which is one of bacterial pathogens evoking severe infection in fish and shellfish as well as in human has been found at high frequency around all coast areas in Korea. Both V. alginolyticus and V. alginolyticus specific bacteriophage were isolated from sea water and various fishes from fish farms on west coast in Korea. In a morphological study based on electron microscope, the purified phage appeared to be composed of hexagon head of 60 nm and short tail of 20 nm. In the denatured SDS-PAGE analysis, the structural proteins of the phage were found to be 7 different protein fractions ranging from 37.8 to 198 kda. The kind of nucleic acid of the phage was ascertained to a double stranded DNA.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.52 no.2
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• pp.149-158
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• 2019

This study investigated the effects of replacing fish meal (FM) with a mixture of four protein sources (wheat gluten, soy protein concentrate, tankage meal, and poultry byproduct meal) in an extruded pellet (EP) diet for olive flounder Paralichthys olivaceus. Five experimental diets were formulated with alternative proteins replacing 0%, 20%, 30%, 40%, and 50% of FM. Taurine and betaine were added as attractants in the diets. Triplicate groups of fish (initial body weight: $196{\pm}2g$) were fed the diets to apparent satiation. Over the course of a 6-month feeding trial, there were no significant differences between the groups in growth performance, feed utilization, survival, or villus height. The dry matter and protein digestibility of FM50 diet were significantly lower than those of the control diet at water temperatures below $18.5^{\circ}C$ in months 4 and 6. This is a highly significant first report on FM replacement in an EP diet given to olive flounder over a 6-month-long feeding period. It shows that the proper mixture of protein sources can replace up to 50% of FM in olive flounder EP diets with taurine and betaine supplementation. It also shows that 40% of FM could be safely replaced in EP diets during periods of low water temperature.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.29 no.3
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• pp.296-308
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• 1996

Proteolytic enzymes responsible for post-mortem degradation of the fish tissues have been studied in regard with screening the proteases distributed in the fish body by reacting with the specific synthesized substrates. Activities of cathepsin L, B, H, G, and D like enzymes were detected in the muscle crude protease from the both kind of fish, dark fleshed fish (anchovy, Engraulis japonica, and gizzard-shad, Clupanodo punctatus) and white fleshed fish (seabass, Lateolabrax japonicus, and sole, Pleuronichthys cornutus), however, those of chymotrypsin, trypsin, pepsin, and peptidase like enzymes were observed 3n the viscera crude pretense from the fish. Proteolytic activities of the muscle crude protease at pH 6.0 were similar to those of the viscera crude protease at pH 8.0, but, those of the viscera crude protease at pH 8.0 were about 2 times higher than those at pH 6.0. The muscle and viscera crude protease from anchovy showed the strongest proteolytic activity among the four fish crude proteases and the proteolytic activity of the viscera crude protease was approximately 100 times higher than that of the muscle crude protease, which suggest that viscera proteases were more contributed on the development of post-mortem changes than muscle proteases. With the degradation patterns on SDS-polyacrylamide gel electrophoresis against yellowtail myofibrillar proteins, the muscle and viscera crude protease of the four fishes were primary responsible for the degradation of myosin heavy chain, and myosin light chain and actin, respectively.

• Proceedings of the Korean Society of Fisheries Technology Conference
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• 2002.10a
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• pp.216-217
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• 2002

Vitellogenin (VTG) is a Precursor form of egg yolk Proteins, which appear only in the blood circulation of female fish and its synthesis in the liver is considered to be regulated by several hormones. It has been reported that in addition to estradiol-17 $\beta$ (E2) several hormones are also involved in the production site of VTG, the liver (Peyon et al., 1996; Mori et al., 1998). (omitted)

• Proceedings of the Korean Society of Fisheries Technology Conference
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• 1996.06a
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• pp.197-198
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• 1996