• Journal of Life Science
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• v.19 no.12
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• pp.1794-1801
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• 2009

This study was conducted to examine the effects of soluble collagen peptides extract supplementation on the improvement of blood glucose, lipid components and enzyme activities in the sera of streptozotocin (STZ, 55 mg/kg BW, IP injection)-induced diabetic rats fed on experimental diets for 5 weeks. The concentrations of blood glucose, total cholesterol, atherosclerotic index, LDL, LDL-cholesterol, free cholesterol, cholesteryl ester ratio, triglycerides (TG) and phospholipids (PL) in serum were remarkably higher in the diabetic group (group SW) and STZ (IP)+collagen peptides extract supplementation group (group SFW) than those in the control group (group CG, basal diet + water). However the concentrations of blood glucose, total cholesterol, atherosclerotic index, LDL, LDL-cholesterol, free cholesterol, cholesteryl ester ratio, TG and PL in serum were lower in the SFW group than in the SW group, whereas the ratio of HDL-cholesterol concentration to total cholesterol and HDL-cholesterol concentration in the SFW group were higher than in the SW group. The activities of alkaline phosphatase (ALP) and aminotransferase (AST, ALT) in serum were lower in the SFW group than in the diabetic SW group. The results shown above suggest that soluble collagen peptides extract supplementation effectively improves blood glucose, lipid compositions and enzyme activities in the sera of STZ induced diabetic rats.

• 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.

• Journal of the Korean Applied Science and Technology
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• v.30 no.3
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• pp.560-566
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• 2013

In this research we extracted water-soluble collagen peptide from flatfish skin and compared it with commercially available collagen peptide extracted from Tilapia scale currently placed on the market in the aspect of physiochemical property. The physical property and nutritional components of FSCP appeared almost similarly to those of TSCP, and also in calorie, FSCP marking 3.82 Kcal showed no differences from TSCP marking 3.84 Kcal. As for forming amino acids, in aspartic acid, serine, histidine, tyrosine, methionine, FSCP had higher content than TSCP, but in OH-proline, proline and alanine FSCP had lower content than TSCP. Especially the content of essential amino acids of FSCP marked 22.74% with a higher content compared with 13.64% of TSCP. In the distribution of molecular weight FSCP with 1,000 Da showed comparatively low compared with TSCP, and in emulsion property and stability FSCP and TSCP showed similar excellent trend.

• Applied Biological Chemistry
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• v.34 no.3
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• pp.265-272
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• 1991

In order to utilize fish skin effectively, the acid-soluble collagen was extracted from the skin of filefish, Novoden modestrus, and the filefish skin collagen(FSG) was modified by papain-catalyzed incorporation of L-leucine alkyl ester(Leu-OCn). The functional properties of an enzymatically modified collagen were measured. The $FSC-Leu-OC_8$ showed very good emulsifiability and foamability and was suitable for use as a low-fat content proteinaceous surfactant.

• Animal Bioscience
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• v.36 no.6
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• pp.953-961
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• 2023

Objective: This study aimed to investigate the effect of dorsal cranial myopathy (DCM) on chicken meat quality. Methods: Sixty-six Ross 308 AP broilers, 47 days old, of both sexes, weighing about 3.51 kg, were slaughtered according to standard industrial practices, and evaluated for meat color, pH, chemical composition, collagen content, fatty acid profile, and histopathological parameters. Comparisons between normal and DCM-affected meat were performed using Student's t-test at the 5% significance level. Results: Histological analysis of muscle tissues affected by DCM showed myofiber degeneration, proliferation of inflammatory cells, fibroplasia, and necrosis with fibrosis. DCM samples had lower protein content and higher moisture, ash, insoluble collagen, total collagen, and pH. DCM-affected meat was redder and more yellowish. There were no differences in lipid or soluble collagen contents between groups. DCM-affected meat had higher percentages of arachidonic acid (C20:4n-6) and eicosapentaenoic acid (C20:5n-3). Conclusion: This study revealed that DCM-affected meat exhibits considerable changes in quality parameters.

• 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.

• Medical Lasers
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• v.10 no.2
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• pp.96-105
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• 2021

Background and Objectives Skin aging is reportedly associated with regulation in collagen and elastin synthesis. This study investigated the potential of combining light-emitting diode (LED) treatments using a 630-nm and 850-nm LED with simultaneous microcurrent application. Materials and Methods The dorsal skin of female pigs was treated with a home-use device. We examined the treatment effects using photography, thermocamera, microscopic pathology, and histological examination to determine the mechanism of action, efficacy, and safety of the procedure. A histological observation was performed using hematoxylin and eosin, Masson's trichrome, Victoria blue, and immunohistochemical staining. We also used the Sircol soluble collagen and elastin assay kit to measure the amounts of collagen and elastin in the porcine back skin tissue after 2 and 6 weeks. Results Evaluation by visual inspection and devices showed no skin damage or heat-induced injury at the treatment site. Histological staining revealed that accurate treatment of the targeted dermis layer effectively enhanced collagen and elastin deposition. Collagen type I, a protein defined by immunohistochemical staining, was overexpressed in the early stages of weeks 2 and 6. Combined therapy findings showed the superior capability of the 630-nm and 850-nm LED procedures to induce collagen; in contrast, elastin induction was more pronounced after microcurrent treatments. Conclusion The home-use LED device, comprising a combination of 630-nm and 850-nm LEDs and microcurrent, is safe and can be used as an adjunctive treatment for self-administered facial rejuvenation.

• Korean Journal of Food Science and Technology
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• v.27 no.4
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• pp.571-575
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• 1995

Transition temperature$(T_m)$ and $enthalpy({\Delta}H)$ were examined by means of DSC to obtain basic information on heat stability of skin tissue collagen. From DSC properties of insoluble collagen on hydration time and moisture content, it was found that moisture content had more effect on structural stability of collagen than hydration time. As moisture content increased, $({\Delta}H)$ increased while $(T_m)$ decreased. DSC properties of acetone dried skin on the variation of age and sex showed higher heat stability in case of male rat and heat stability seemed to be connected with age, as $(T_m)$ and $({\Delta}H)$increased with age. Meanwhile, DSC properties of salt soluble collagen showed higher values in female rat than in male rat, and the $(T_m)$ and $({\Delta}H)$ decreased significantly with age in female rat. These results seemed to suggest indirectly that collagen structure varied with age or sex in the same tissue.

• Archives of Pharmacal Research
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• v.28 no.11
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• pp.1311-1316
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• 2005

To better define the relationship between dermal regeneration and wound contraction and scar formation, the effects of epidermal growth factor (EGF) loaded in collagen sponge matrix on the fibroblast cell proliferation rate and the dermal mechanical strength were investigated. Collagen sponges with acid-soluble fraction of pig skin were prepared and incorporated with EGF at 0, 4, and 8 $\mu$g/1.7 $cm^{2}$. Dermal fibroblasts were cultured to 80$\%$ confluence using DMEM, treated with the samples submerged, and the cell viability was estimated using MTT assay. A deep, $2^{nd}$ degree- burn of diameter 1 cm was prepared on the rabbit ear and the tested dressings were applied twice during the 15-day, post burn period. The processes of re-epithelialization and dermal regeneration were investigated until the complete wound closure day and histological analysis was performed with H-E staining. EGF increased the fibroblast cell proliferation rate. The histology showed well developed, weave-like collagen bundles and fibroblasts in EGF-treated wounds while open wounds showed irregular collagen bundles and impaired fibroblast growth. The breaking strength (944.1 $\pm$ 35.6 vs. 411.5 $\pm$ 57.0 Fmax, $gmm^{-2}$) and skin resilience (11.3 $\pm$ 1.4 vs. 6.5 $\pm$ 0.6 mJ/$mm^{2}$) were significantly increased with EGF­treated wounds as compared with open wounds, suggesting that EGF enhanced the dermal matrix formation and improved the wound mechanical strength. In conclusion, EGF-improved dermal matrix formation is related with a lower wound contraction rate. The impaired dermal regeneration observed in the open wounds could contribute to the formation of wound contraction and scar tissue development. An extraneous supply of EGF in the collagen dressing on deep, $2^{nd}$ degree-burns enhanced the dermal matrix formation.

• 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.