• Food Science and Biotechnology
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• v.16 no.4
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• pp.549-556
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• 2007

The study was carried out to examine on the refiner discharge from Alaska pollock as a collagen resource by characterizing biochemical and functional properties of collagen. The refiner discharge from Alaska pollock surimi manufacturing was a good resource for collagen extraction according to the results of total protein, heavy metal, volatile basic nitrogen, collagen content, amino acid composition, and thermal denaturation temperature (TDT). TDT of acid soluble collagen from refiner discharge showed $20.7^{\circ}C$, which was similar to that of collagen from Alaska pollock muscle and was higher than that of collagen from Alaska pollock skin. TDT of acid-soluble collagen from refiner discharge was, however, lower than those of skin collagens from warm fish and land animal. Acid-soluble collagen from refiner discharge of Alaska pollock could be used as a functional ingredient for food and industrial applications according to the results of water and oil absorption capacities, and emulsion properties. In addition, if the thermal stability of the acid-soluble collagens is improved, collagen from refiner discharge from Alaska pollock could be more effectively used.

• Fisheries and Aquatic Sciences
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• v.24 no.12
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• pp.406-414
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• 2021

The objective of this study was to investigate the yield and characteristics of collagen protein extracted from the muscle of four different species of mantis shrimp: Miyakella nepa, Harpiosquilla harpax, Erugosquilla woodmasoni, and Odontodactylus cultrifer. Mantis shrimp muscle was extracted by using a pepsin-solubilization technique, with 0.5 M acetic acid and 5% pepsin enzyme. The highest collagen yield was from M. nepa muscle (0.478 ± 0.06%), which was significantly greater (p < 0.05) than that from H. harpax, O. cultrifer, and E. woodmasoni (0.313 ± 0.03%, 0.123 ± 0.02%, and 0.015 ± 0.00%, respectively). The freeze-dried collagen appeared as thin fibers, and formed an opaque film. The pepsin-soluble collagen (PSC) from four mantis shrimp species was analyzed by gel electrophoresis. The results showed that all species of mantis shrimp contained type I collagen, consisting of β, α1, and α2 subunits with average molecular weights of 250, 145, and 118 kDa, respectively. The study of the solubility of collagen showed that, for NaCl, collagen had the highest relative solubility in 2% NaCl (80.20 ± 4.95%). In contrast, the solubility decreased at higher NaCl concentrations. However, in terms of pH, collagen had the highest relative solubility at pH 3 (91.32 ± 5.14%), and its solubility decreased at higher pH. FT-IR spectroscopy was used to compare the collagen with a model compound. Five wavenumbers in the spectrum for model collagen were identified: Amide A (3,406-3,421 cm^-1), amide B (2,916-2,940 cm^-1), amide I (1,639-1,640 cm^-1), amide II (1,539-1,570 cm^-1), and amide III (1,234-1,250 cm^-1).

• Korean Journal of Fisheries and Aquatic Sciences
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• v.48 no.1
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• pp.1-15
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• 2015

Tissue engineering is an emerging, innovative technology to improve or replace the biological functions of damaged tissues and organs. Scaffolds are important materials for tissue engineering as they support cell attachment, migration, and differentiation. Marine sponges naturally contain scaffolds formed by extracellular matrix proteins (collagen and sponging) and strengthened by a siliceous or calcium carbonate skeleton. Coral skeletons are also derived naturally formed by essential calcium carbonate in the form of aragonite, and are similar to human bone. In addition, collagen extracted from jellyfish is a biosafe alternative to bovine and porcine collagen and gained attention as a potential source for tissue engineering. Moreover, cuttlefish bone is an excellent calcium source and can be used to generate bio-synthetic calcium phosphate. It has become a natural candidate for biomimetic scaffolds. This review describes the use of natural products derived from marine invertebrates for applications in bone tissue engineering based on studies from 2008 to 2014.

• Fisheries and Aquatic Sciences
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• v.12 no.1
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• pp.6-15
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• 2009

Biochemical and functional properties of acid-soluble collagen (ASC) and pepsin-soluble collagen (PSC) from rockfish skin were characterized. Yield of PSC (90.0%) was higher than that of ASC (63.2%). Both ASC and the PSC consisted of ${\alpha}1$ and ${\alpha}2$ chains, and $\alpha$-cross-linked components. According to the results of hydroxylation of proline and lysine, and FT-IR, no difference between the helical structure of ASC and PSC was identified. Thermal denaturation temperature (TDT) of ASC from rockfish skin was $22.8^{\circ}C$, the same as exhibited in PSC. Both ASC and PSC were higher in water absorption capacity (WAC) and oil absorption capacity (OAC) than other vegetable proteins. According to the results of emulsifying activity (EA) and cooking stability (CS), both ASC and PSC from rockfish skin were inferior compared to the commercial emulsifier (Tween-80). The results of FT-IR suggested that the structure of PSC was slightly different when compared to that of ASC. No differences in solubility were established between ASC and PSC from rockfish skin at various pH and NaCl concentrations.

• Polymer(Korea)
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• v.36 no.2
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• pp.124-130
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• 2012

The uniform nanofibers of poly(L-lactide-$co$-${\varepsilon}$-caprolactone) (PLCL) with different contents of marine collagen (MC) were successfully prepared by electrospinning method. The effects of the major parameters in electrospinning process such as tip to target distance (TTD), voltage, nozzle size and flow rate on the average diameter of the electrospun nanofiber were investigated in generating composite nanofiber. The diameter and morphology of the nanofibers were confirmed by a scanning electron microscopy (SEM). Also, we measured a water contact angle to determine the surface wettability of the nanofibers. The average diameter of the nanofibers decreased as the value of TTD, MC contents, and voltages increased in comparison with that of pristine PLCL nanofiber. In contrast, the diameter of the nanofibers increased as the flow rate and inner diameter of nozzle increased in comparison with that of pristine PLCL. In addition, the hydrophilicity of the nanofiber and attachment of MG-63 cells on the sheets increased as incorporated collagen contents increased. Therefore, the marine collagen would be a potential material to enhance cellular interactivity of synthetic materials by mimicking the natural tissue.

• Preventive Nutrition and Food Science
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• v.18 no.2
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• pp.124-132
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• 2013

In this study, novel peptides (NIPP-1, NIPP-2) derived from Navicula incerta (microalgae) protein hydrolysate were explored for their inhibitory effects on collagen release in hepatic fibrosis with the investigation of its underlying mechanism of action. TGF-${\beta}1$ activated fibrosis in LX-2 cells was examined in the presence or absence of purified peptides NIPP-1 and NIPP-2. Besides the mechanisms of liver cell injury, protective effects of NIPP-1 and NIPP-2 were studied to show the protective mechanism against TGF-${\beta}1$ stimulated fibrogenesis. Our results showed that the core protein of NIPP-1 peptide prevented fibril formation of type I collagen, elevated the MMP level and inhibited TIMP production in a dose-dependent manner. The treatment of NIPP-1 and NIPP-2 on TGF-${\beta}1$ induced LX-2 cells alleviated hepatic fibrosis. Moreover, ${\alpha}$-SMA, TIMPs, collagen and PDGF in the NIPP-1 treated groups were significantly decreased. Therefore, it could be suggested that NIPP-1 has potential to be used in anti-fibrosis treatment.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.55 no.4
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• pp.397-407
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• 2022

This study investigated the collagen and texture properties of commonly consumed sliced raw fish species (CC-SRF) [olive flounder (OF), red seabream (RS), Atlantic salmon (AS), coho salmon (CoS) and sockeye salmon (SS)] distributed in Korea as sliced raw fishes. The crude lipid contents of CC-SRF were 5.5% for OF, 6.8% for RS, 18.5% for AS, 16.1% for CoS, and 5.7% for SS. The collagen content and solubility from CC-SRF were 622 mg/100 g and 78.0%, respectively, in OF, 270 mg/100 g and 75.6%, respectively, in RS, 237 mg/100 g and 24.1%, respectively, in AS, 341 mg/100 g and 65.7%, respectively, in CoS, and 246 mg/100 g and 17.9%, respectively, in SS. The texture of CC-SRF was affected by the lipid content, collagen content, acid solubility, hydroxylation, and cross linkage degree. The highest hardness of CC-SRF was obtained from OF, followed by RS, SS, AS and CoS. There was, however, no difference (P>0.05) in hardness between OF and RS and between AS and CoS.

• Applied Biological Chemistry
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• v.39 no.2
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• pp.134-139
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• 1996

In order to effectively utilize marine animal skin wastes in marine processing manufacture, conger eel skin, file fish skin and arrow squid skin as raw material of edible gelatin were screened. Conger eel skin was the highest in the collagen content, followed by Ole fish skin and arrow squid skin, in the order named. In the fish skins, the soluble and insoluble collagens occupied $67.4%{\sim}72.3%\;and\;27.7{\sim}32.6%$, respectively, and in the arrow squid skin, 30.4ft and 69.6ft, respectively. No difference in the amino acid composition between soluble and insoluble collagens was detected. Collagen from the marine animal skin catched in coasted and offshore water in Korea consisted ${\alpha}$ chain and ${\beta}$ chain, and ${\alpha}$ chain were hetero type. The sum of proline and hydroxyproline contents in conger eel skin collagen was higher than that in the other skin collagens, while was lower than that pork skin collagen. Conger eel skin collagen exhibited a higher denaturation temperature in solution and a higher degree of proline hydroxylation, compared with skin collagen of the respective species. The physical properties such as gel strength, melting point and gelling point of conger eel skin gelatin were superior to those of file fish skin and arrow squid skin gelatins.

• Korean Journal of Materials Research
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• v.32 no.4
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• pp.186-192
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• 2022

Collagen is one of the most widely used biological materials in medical design. Collagen extracted from marine organisms can be a good biomaterial for tissue engineering applications due to its suitable properties. In this study, collagen is extracted from fish skin of Ctenopharyngodon Idella; then, the freeze drying method is used to design a porous scaffold. The scaffolds are modified with the chemical crosslinker N-(3-Dimethylaminopropyl)-N'-ethyl carbodiimide hydrochloride (EDC) to improve some of the overall properties. The extracted collagen samples are evaluated by various analyzes including cytotoxicity test, SDS-PAGE, FTIR, DSC, SEM, biodegradability and cell culture. The results of the SDS-PAGE study demonstrate well the protein patterns of the extracted collagen. The results show that cross-linking of collagen scaffold increases denaturation temperature and degradation time. The results of cytotoxicity show that the modified scaffolds have no toxicity. The cell adhesion study also shows that epithelial cells adhere well to the scaffold. Therefore, this method of chemical modification of collagen scaffold can improve the physical and biological properties. Overall, the modified collagen scaffold can be a promising candidate for tissue engineering applications.

• Food Science and Preservation
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• v.16 no.3
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• pp.419-426
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• 2009

The antioxidant and antimicrobial effects of acid-soluble and pepsin-solubilizable shark (Isurus oxyrinchus) collagens (SC) (ASSC: acid-soluble shark skin collagen, ASMC: acid-soluble shark meat collagen, PSSC: pepsin-solubilizable shark skin collagen, PSMC: pepsin-solubilizable shark meat collagen) and standard marine collagen (STMC) as materials, and the ability of these materials to inhibit tyrosinase and elastase, were investigated. The electron-donating ability of SC ($1{\sim}5\;g/mL$) was $14.91{\sim}17.21%$, which was $3.0{\sim}3.6$-fold higher than that of STMC at the same concentration. Also, the SOD(superoxide dismutase)-like activity of SC (5.80 mg/mL) was $4.67{\sim}37.28%$, thus $3.0{\sim}3.6$-fold greater than that of STMC. The MIC values of SC against Staphylococcus aureus and Salmonella enteritidis were $5{\mu}g$/disc, which were remarkably lower than that of STMC ($200{\mu}g$/disc). There was no antimicrobial activity against Escherichia coli in STMC, but the MIC against E. coli was $200{\mu}g$/disc for acid-soluble SC and $100{\mu}g$/disc for pepsin-solubilizable SC. The inhibition of tyrosinase by SC (3-5 mg/mL) was $58.95{\sim}98.16%$, $3.34{\sim}3.74$-fold higher than that of STMC ($17.67{\sim}26.25%$). Also, elastase inhibition by SC (at 1 mg/mL) was $53.33{\sim}80.0%$, $1.1{\sim}4.0$-fold greater than that of STMC. These results indicated that shark collagens may be valuable new functional materials owing to their antioxidant and antimicrobial properties, and because the inhibitory activities against elastase and tyrosinase are better than those of standard marine collagen.