• Proceedings of the Korean Fiber Society Conference
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• 2003.10b
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• pp.31-33
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• 2003

실크 피브로인은 대표적인 섬유상 단백질의 하나로 생체적합성, 생분해성, 저독성 등의 유용한 특성을 가지므로 생체재료로 상당한 관심과 연구의 대상이 되어 왔다. 콜라겐 또한 우수한 생체적합성과 생분해성을 가지고 있어 유용한 생채재료로서 조직배양용 지지체나 창상피복재와 같은 의료용 분야에 적절하게 응용될 수 있는 장점을 가진다. 본 실험에서는 1,1,1,3,3,3-Hexafluoro-2-propanol (HFIP)을 공용매로 하여 실크 피브로인/HFIP 용액과 콜라겐/HFIP 용액을 각각 제조하여, 이들 용액을 75/25, 50/50, 25/75의 비율로 혼합하여 방사용액을 제조하고, 이 용액을 전기방사법으로 방사하여 실크 피브로인/콜라겐 블렌드 나노섬유를 얻었다. (중략)

• Korean Journal of Fisheries and Aquatic Sciences
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• v.30 no.1
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• pp.55-61
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• 1997

In order to effectively utilize the fish and squid skin wastes derived from marine processing manufacture, the skin wastes of some pelagic fishes such as yellowfin sole, red cod, cod, Allaska pollack and flying squid were screened for the raw material of edible gelatin and studied some properties of those gelatins. The content of total collagen in the red cod skin was the highest (28.4 g/100 g wet skin), while that in the flying squid skin was the lowest (11.1 g/100 g wet skin) and those of another fishes were similar. Acid soluble collagens in the skins of the fishes and flying squid were $68.9\~84.8\%\;and\;44.3\%$, respectively. But showed no difference in the amino acid composition between acid soluble and insoluble collagens. Those collagens were consisted $\alpha\;and\;\beta$ chain and $\alpha$ chains extracted from fish skins except red cod and flying squid skins were hetero. The collagen of yellowfin sole skin exhibited slightly higher denaturation temperature $(25.4^{\circ}C)$ and also physical properties such as gel strength, melting point and gelling point were better than those of the other species.

• Journal of the Korean Society of Food Science and Nutrition
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• v.43 no.10
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• pp.1535-1542
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• 2014

This study was conducted to investigate the physicochemical properties and biological activities of collagens with different molecular weights from Alaska pollack (Theragra chalcogramma) skin as well as their efficacies as functional materials. The molecular weights of collagens were between 1~10 kDa (below 1 kDa (AP1), 1~3 kDa (AP2), 3~10 kDa (AP3), and above 10 kDa (AP4). The protein content of AP4 (40.19 g/100 g) was the highest. Collagen contents of AP1, AP2, AP3, and AP4 were 36.43, 32.23, 19.23, and 14.89%, respectively. The free amino acid and essential amino acid contents of AP1 were higher than those of AP2, AP3, and AP4. Fourier transform infrared spectroscopy spectra of collagens with different molecular weights showed wavenumbers representing the regions of amide I, amide II, amide III, and amide A, respectively. The electron-donating ability (29.51%) and SOD-like activity (38.45%) of AP1 were higher than those of AP2, AP3, and AP4. Tyrosinase inhibition activity of AP1 improved with higher treatment concentration. The rate of inhibition of MMP-1 production in HS68 cells exposed to UVB was suppressed by treatment with AP1 (29.78%) and AP2 (26.49%) at 1 mg/mL. Furthermore, there was a strong correlation between DPPH, superoxide dismutase, tyrosinase activity, and MMP-1 inhibition rate of collagens with different molecular weights.

• Journal of the Korea Academia-Industrial cooperation Society
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• v.11 no.9
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• pp.3277-3283
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• 2010

In this study, in order to find effects of collagen manipulation on hair in permanent wave treatment, it was conducted measurement and analysis on hair curl formation, thickness, tensile strength, methylene blue absorbance, and moisture loss after manipulating concentration proportion of collagen in permanent wave treatment on normal hair. As a result, it was found that by contrast with applying the reductant, hair thickness, tensile strength, methylene blue absorbance, and moisture loss were decreased when applied collagen in permanent wave treatment the higher concentration proportion of collagen was applied, the less damage was occurred on hair However curl formation capacity was decreased in permanent wave treatment as concentration proportion of collagen was increased. Therefore, the appropriate concentration proportion of collagen was 2% in order to reduce hair damage in permanent wave treatment.

• Korean Journal of Plant Resources
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• v.25 no.2
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• pp.240-245
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• 2012

In this study, we investigated the boosting effects on collagen biosynthesis of $Anthriscus$ $sylvestris$ ethanol extract (ASE) in human dermal fibroblasts. To obtain more effective fraction and subfraction for collagen biosynthesis, standard solvent partition and open column chromatography were performed. The EtOH extract, solvent fractions, and 8 EtOAc subfractions were tested for their collagen synthesis capacity by [$^3H$]Proline-incorporation and ELISA assay. ASE increased 25% of total collagen synthesis and 27% of procollagen biosynthesis. The total collagen biosynthesis was increased by EtOAc fraction and E6 subfraction to 28% and 50% respectively. Type I procollagens were also upregulated by EtOAc fraction and E6 subfraction to 30% and 47%, each. Taken together, our data suggest that potential anti-aging effect of ASE on skin is via increasing collagen biosynthesis and effective subtraction is E6 subfraction of EtOAc fraction.

• Journal of the Korean Ceramic Society
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• v.38 no.11
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• pp.1030-1036
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• 2001

Hydroxyapatite[COL] nanocomposite was prepared through coprecipitation process. The chemical bond formation between HAP and COL was confirmed by diffusive reflectance FT-IR and TEM observation. Higher concentration of COL in the preparation induced tiny nanocrystalline composite particles, but lower concentration of COL contributed to form the well developed HAP particles. From TEM observation and ED(Electron Diffraction) pattern the embedded HAP nanoparticles were oriented along the c-axis of COL fiber. In an aqueous system of constant [Ca$\^$2+/] and [PO$_4$$\^$3-/], quantity of soluble COL matrix was doing an important role of controlling the heterogeneous nucleation site for the formation of HAP nanocrystals. Higher concentration of COL will provide more nucleation sites for Ca$\^$2+/ and so the concentration of calcium ions for the total number of active nucleation sites will be getting relatively dilute.

• Journal of the Korea Convergence Society
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• v.11 no.5
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• pp.61-72
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• 2020

An anti-aging peptide was prepared from fish collagen hydrolysate (FCH) by ultrafiltration (MWCO; 1 kDa) and reversed-phased high performance liquid chromatography (RP-HPLC). Its anti-aging properties were evaluated based on the procollagen-synthesizing and MMP-1-inhibiting activities in Hs68 cells. A potent anti-aging peptide (fraction I-I) increased collagen synthesis by 46% and also inhibited MMP-1 secretion by 77%, compared with unpurified FCH. The amino acid sequence of fraction I-I was identified to be Gly-Arg-Arg-Gly-Asn-Lys (GRRGNK; the repeating Gly-X-Y sequence in collagen), and it had a molecular mass of 686.175 Da. It revealed that the anti-aging activity of GRRGNK was mainly due to skin protective effects. These results demonstrated that fish collagen hydrolysate may be a potential source of anti-aging peptides, which could be utilized in various field, including foods, cosmetics, and pharmaceuticals.

• Applied Biological Chemistry
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• v.36 no.4
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• pp.290-295
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• 1993

In order to utilize effectively fish skin from fish processing, characteristics of the yellowfin sole and dover sole skins were investigated. In the yellowfin sole, the crude protein content and yield of fish skin used for the preparation of gelatin were 22.3% and 11.3%, respectively and in the dover sole, 17.2% and 8.9%, respectively. In the yellowfin sole skin, the soluble and insoluble collagen occupied 66.1% and 33.9%, respectively and in the dover sole skin, 78.8% and 21.1%, respectively. No difference in the amino acid composition between soluble and insoluble collagen was detected. The sum of proline and hydroxyproline content in the collagen extracted from fish skin was lower than that of those from pork skin or bone. The molecular weight of the two major subunits from the soluble collagen in the yellowfin sole skin were found to be 143 KDa and 202 KDa. Those in the dover sole skin were 142 KDa and 207 KDa. The physico-chemical properties such as the melting point and gelling point of yellowfin sole skin gelatin were superior to those of dover sole skin gelatin.

• Journal of Nutrition and Health
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• v.42 no.6
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• pp.505-515
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• 2009

Collagen is the major matrix protein in dermis and consists of proline and lysine, which are hydroxylated by prolyl hydroxylase (PH) and lysyl hydroxylase (LH) with cofactors such as vitamin C, oxygen, iron (Fe$^{2+}$), ketoglutarate and silicon. The collagen degradation is regulated by matrix metalloproteinase-1 (MMP-1), of which is the major collagen-degrading proteinase whereas tissue inhibitors of metalloproteinase-1 (TIMP-1) bind to MMP-1 thereby inhibiting MMP-1 activity. In this study, we investigated the effects of vitamin C, silicon and iron on mRNA, protein expressions of PH, LH, MMP-1 and TIMP-1. The physiological concentrations of vitamin C (0-100 $\mu$M), silicon (0-50 $\mu$M) and iron (Fe$^{2+}$：0-50 $\mu$M) were treated to human dermal fibroblast cells (HS27 cells) for 3 or 5days. The expression level of mRNA and protein was increased in not only PH but also LH when cells were incubated with vitamin C. A similar increase in LH mRNA or protein expression occurred when cells were incubated with silicon. Our results suggest that treatment of vitamin C and silicon increased mRNA and protein expression of PH and LH in human dermal fibroblast.

• 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%.