• 제목/요약/키워드: Soluble collagen

검색결과 82건 처리시간 0.029초

숭어(Mugil cephalus) 비늘 유래 가용성 콜라겐 펩타이드가 당뇨성 흰쥐의 혈당 및 지질대사에 미치는 영향 (Effects of Soluble Collagen Peptides Extract Derived from Mugil cephalus Scale on the Blood Glucose and Lipid Metabolism in Diabetic Rats)

  • 김한수;윤호동;성종환;이영근;;김수하;최우석
    • 생명과학회지
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    • 제19권12호
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    • pp.1794-1801
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    • 2009
  • 숭어(Mugil cephalus) 비늘에서 추출한 가용성 펩타이드 추출물이 streptozotocin (STZ 55 mg/kg BW, IP injection)으로 유도된 당뇨성 Sprague Dawley계 수컷 흰쥐의 있어서, 혈당 및 혈청 지질개선효과와 당질대사 이상 등에 관여하는 효소의 활성 변동을 생리생화학적 측면에서 검토하기 위하여 본 실험을 수행하였다. 대조군인 CG군을 비롯한 STZ 당뇨 유발군(SW군), 당뇨 유발에 콜라겐 펩타이드를 섭취시킨 군(SFW군)을 5주간 실험 사육한 결과, 혈당 농도는 당뇨 유발군에 콜라겐 펩타이드를 급여함으로서 유의적인 감소 효과를 보였다. 또한 혈청 총 콜레스테롤, 동맥경화지수, LDL, LDL-콜레스테롤, 중성지방 및 인지질 농도, 유리 콜레스테롤, 콜레스테롤 에스테르 비 등은 콜라겐 펩타이드를 섭취시킨 군(SFW군)에서 농도가 저하되는 것으로 나타났다. 한편, HDL-콜레스테롤 및 총 콜레스테롤에 대한 HDL-콜레스테롤 비 등은 콜라겐펩타이드 섭취(SFW군)에 의해서 증가되는 것으로 나타났다. 혈청 중 alkaline phosphatase (ALP) 및 aminotransferase(AST, ALT)의 활성은 STZ으로 당뇨를 유도 시킨 후 콜라겐펩타이드를 섭취시킴으로서 저하되는 것으로 나타났다. 따라서 본 실험 결과 등에서 콜라겐 펩타이드 추출물이 STZ으로 유발된 당뇨성 흰쥐의 혈당조절 기능 및 지질대사 이상 등에서 오는 당뇨성 질환의 예방 및 개선에 효과가 있을 것으로 사료된다.

청상아리(Isurus oxyrinchus) 껍질 콜라겐의 물리 화학적 특성 (Characterization of Physicochemical Properties of Collagen from Shark (Isurus oxyrinchus) Skin)

  • 박순형;김태완;김선봉
    • 한국수산과학회지
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    • 제42권6호
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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.

당가자미 껍질로부터 수용성콜라겐 제조 및 이화학적 특성 (A Physicochemical Characteristics and Manufacture of Solubility Collagen Peptide from Flatfish Skin)

  • 장부식;이미진;정노희
    • 한국응용과학기술학회지
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    • 제30권3호
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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.

말쥐치피 콜라겐의 효소적 수식 및 기능성 (The enzymatic modification and functionalities of filefish skin collagen)

  • 김세권;곽동채
    • Applied Biological Chemistry
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    • 제34권3호
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    • pp.265-272
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    • 1991
  • 어류 가공시 부산물로 얻어지는 어피를 보다 효율적으로 이용할 목적으로 말쥐치피로부터 콜라겐을 추출한 후, 이에 소수성 잔기를 증가시키기 위하여 leucine alkyl ester를 도입하여 기능성 개량을 시도하였다. 말쥐치피 콜라겐 및 FSC-Leu-OCn의 콜라겐 함량, 아미노산 조성에 의한 소수성, 분자량, 용해도, 보수력, 분산성, 지방흡수력, 포말성, 유화성 등을 계면활성제인 Tween-60과 비교 검토한 결과, 어피 콜라겐에 leucine alkyl ester를 도입시킨 $FSC-Leu-OC_8$은 기능성 중 유화성 및 유화안정성이 매우 향상되어 유화제로 이용할 수 있을 것으로 본다.

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Physicochemical and histopathological parameters of broilers with dorsal cranial myopathy

  • Ana Clara Longhi Pavanello;Fernanda Jessica Mendonca;Thalita Evani Silva Oliveira;Guilherme Bau Torezan;Giovana Wingeter Di Santis;Adriana Lourenco Soares
    • Animal Bioscience
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    • 제36권6호
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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.

수식 어류껍질 젤라틴의 원료로서 연근해산 수산물껍질의 검색 (Screening for raw material of modified gelatin in marine animal skins caught in coastal offshore water in Korea)

  • 조순영;김진수
    • Applied Biological Chemistry
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    • 제39권2호
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    • pp.134-139
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    • 1996
  • 연근해산 수산물중 부산물의 양이 많은 붕장어껍질, 말쥐치껍질 및 화살오징어껍질을 대상으로 수산 연제품의 품질개선제로 사용하기 적절한 수산물껍질 젤라틴의 원료를 검색하였다. 콜라겐함량은 붕장어껍질(24.69%)이 가장 많았고, 다음으로 말쥐치껍질(20.03%)이었으며 화살오징어껍질은 12.62%에 불과하였다. 콜라겐의 조성은 어류껍질의 경우 가용성획분$(67.4%{\sim}72.3%)$이 불용성획분보다 높았으나, 화살오징어껍질의 경우 불용성획분(69.6%)이 가용성획분보다 높았고, 아미노산조성은 가용성획분 및 불용성획분 간에 차이가 없었다. 연근해산 수산물껍질의 콜라겐은 ${\alpha}$ chain과 ${\beta}$ chain으로 구성되어 있었고, ${\alpha}$ chain은 동일종이 아닌 hetero형 이었다. Imino acid 조성비, proline의 수산화정도 및 열변성온도는 붕장어껍질 콜라겐이 가장 높았고, 다음으로 말쥐치껍질 콜라겐 및 화살오징어껍질 콜라겐의 순이었고 또한 이들 껍질로부터 추출한 젤라틴의 물리적 특성도 열변성온도의 경향과 같았다.

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Application of 630-nm and 850-nm Light-emitting Diodes and Microcurrent to Accelerate Collagen and Elastin Deposition in Porcine Skin

  • Kwon, Tae-Rin;Moon, Dong Wook;Kim, Jungwook;Kim, Hyoung Jun;Lee, Seong Jae;Han, Yunhee;Dan, Hee Won;Chi, Sang Hoon;Seong, Hwan Mo;Kim, Hee Jung;Lim, Guei-Sam;Lee, Jungkwan
    • Medical Lasers
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    • 제10권2호
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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.

피부조직 콜라겐의 DSC 특성 (Differential Scanning Calorimetry of Skin Collagen)

  • 김영호;홍상필;양융
    • 한국식품과학회지
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    • 제27권4호
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    • pp.571-575
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    • 1995
  • 피부조직 콜라겐의 열안정성에 대한 기초자료를 얻고자 DSC를 이용하여 Tm(transition temperature)와 ${\Delta}H(enthalpy)$를 측정하였다. 수화시간과 수화율에 따른 불용성 콜라겐의 DSC 특성은 수화시간에 비하여 수화율이 콜라겐 구조안정성에 미치는 영향이 큰 것으로 나타났으며, 수화율이 증가할수록 Tm은 낮아지고 ${\Delta}H$는 증가하였다. 주령 및 성별에 따른 acetone dried skin의 Tm 및 ΔH는 암컷의 경우보다 수컷의 경우가 다소 높았으며, 주령이 증가할수록 Tm과 ${\Delta}H$가 서서히 증가하고 있어 열안정성은 나이와 관계가 있음을 보여주었다. Acetone dried skin의 경우와는 달리 염가용성 콜라겐의 DSC 특성값은 암컷의 경우가 수컷의 경우보다 다소 높았으며, 암컷의 Tm과 ${\Delta}H$는 주령의 증가에 따라 유의적으로 감소하는 경향을 보였다. 이러한 결과는 피부조직내에서의 콜라겐 구조는 성별 또는 주령에 따라 달리 변화되고 있음을 간접적으로 시사한 것으로 생각되었다.

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Enhancing Dermal Matrix Regeneration and Biomechanical Properties of $2^{nd}$ Degree-Burn Wounds by EGF-Impregnated Collagen Sponge Dressing

  • Cho Lee Ae-Ri
    • Archives of Pharmacal Research
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    • 제28권11호
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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.

Isolation and Characterization of Pepsin-soluble Collagens from Bones, Skins, and Tendons in Duck Feet

  • Kim, Hyun-Wook;Yeo, In-Jun;Hwang, Ko-Eun;Song, Dong-Heon;Kim, Yong-Jae;Ham, Youn-Kyung;Jeong, Tae-Jun;Choi, Yun-Sang;Kim, Cheon-Jei
    • 한국축산식품학회지
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    • 제36권5호
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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.