• Food Science and Preservation
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• v.17 no.1
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• pp.91-99
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• 2010

Extraction and bleaching of citric acid- and pepsin-soluble collagens (ASC and PSC, respectively) from shark (Isurus oxyrinchus) skin and muscle were investigated. The optimal sodium hydroxide concentration for extraction was 0.3 M and the optimal treatment time for removal of foreign material was 9 h. The optimal sodium hypochlorite level for bleaching of shark skin was 0.48% (w/v), and sodium hypochlorite was a better bleaching agent than acetone, hydrogen peroxide (10%, v/v), sodium sulfite (0.48%, w/v), sodium thiosulfate (0.48%, w/v), or sodium metabisulfite (0.48%, w/v). Optimal citric acid concentration and extraction time for ASC were 0.3 M and 72 h, respectively, whereas optimal conditions for extraction of PSC were treatment with 0.1 M citric acid containing 0.1% (w/v) pepsin for 24 h. Protein contents in ASSC (acid-soluble shark skin collagen), ASMC (acid-soluble shark meat collagen), PSSC (pepsin-soluble shark skin collagen), and PSMC (pepsin-soluble shark meat collagen) were 88.66%, 83.09%, 90.33%, and 84.81% (on a dry weight basis), respectively, similar to that of commercial marine collagen (88.86%). Net collagen contents of ASSC, ASMC, PSSC, and PSMC, calculated from hydroxyproline levels, were 70.31%, 25.70%, 83.09%, and 32.94%, respectively. The yields of freeze-dried ASSC, ASMC, PSSC,and PSMC were 57.22%, 53.85%, 23.28%, and 20.61%.

• 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).

• 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.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.42 no.6
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• pp.574-579
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• 2009

Acid- and pepsin-solubilized collagens were extracted from the skin of shark (Isurus oxyrinchus) and their physicochemical properties were characterized by amino acid analysis, SDS-PAGE, the composition of collagen types, solubility and denaturation temperature. Acid - and pepsin-solubilized collagens from shark skin had an imino acid of 188.8 and 186.2 residues/1,000 amino acids, respectively. SDS-PAGE showed two different${\alpha}$ chains ($\alpha1$ and $\alpha2$) and $\beta$-component. The component ratio of type I and V was 10:1, and the type III was not found. Solubility of acid-soluble collagen was low in the range of pH 6.0 to pH 11.0. On the other hand, pepsin-solubilized collagen showed a low solubility in the range of pH 7.0-9.0. Temperature for denaturation of acid- and pepsin-solubilized collagens were $25^{\circ}C$ and $27^{\circ}C$, respectively.

• Fisheries and Aquatic Sciences
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• v.10 no.2
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• pp.53-59
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• 2007

In order to utilize skin of bullfrog (Rana catesbeiana Shaw) as an alternative source of collagen, we investigated and compared biochemical and physical properties of collagens isolated from bullfrog skin. Two kinds of collagen (BSASC; bullfrog skin acid-soluble collagen and BSPSC; bullfrog skin pepsin-solubilized collagen) were isolated by subsequent treatments with acetic acid and pepsin. The amounts of skin collagen isolated in the subsequent treatments were 7.3% BSASC and 18.2% BSPSC on the basis of lyophilized bullfrog skin weight, respectively. According to the electrophoretic pattern and CM-cellulose column chromatogram, the BSASC has the chain composition of ${\alpha}1{\alpha}2{\alpha}3$ heterotrimer, and the BSPSC consists of two ${\alpha}$ chains of ${\alpha}1{\alpha}2$. In addition, the denaturation temperatures of all collagens tested were ranged from $30^{\circ}C\;to\;38^{\circ}C$. This study suggests that there is a possibility to use bullfrog skin collagen as an alternative source of collagen for industrial purposes, and subsequently it may increase the economical value of the bullfrog.

• 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.

• Food Science of Animal Resources
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• v.36 no.5
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• pp.665-670
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• 2016

The objectives of this study were conducted to characterize pepsin-soluble collagen (PSC) extracted from bones (PSC-B), skins (PSC-S), and tendons (PSC-T) of duck feet and to determine their thermal and structural properties, for better practical application of each part of duck feet as a novel source for collagen. PSC was extracted from each part of duck feet by using 0.5 M acetic acid containing 5% (w/w) pepsin. Electrophoretic patterns showed that the ratio between α₁ and α₂ chains, which are subunit polypeptides forming collagen triple helix, was approximately 1:1 in all PSCs of duck feet. PSC-B had slightly higher molecular weights for α₁ and α₂ chains than PSC-S and PSC-T. From the results of differential scanning calorimetry (DSC), higher onset (beginning point of melting) and peak temperatures (maximum point of curve) were found at PSC-B compared to PSC-S and PSC-T (p<0.05). Fourier transform infrared spectroscopy (FT-IR) presented that PSC-S and PSC-T had similar intermolecular structures and chemical bonds, whereas PSC-B exhibited slight difference in amide A region. Irregular dense sheet-like films linked by random-coiled filaments were observed similarly. Our findings indicate that PSCs of duck feet might be characterized similarly as a mixture of collagen type I and II and suggest that duck feet could be used for collagen extraction without deboning and/or separation processes.