• Title/Summary/Keyword: low-molecular-weight collagen

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Enhancement of Skin Immune Activation Effect of Collagen Peptides Isolated from Asterias amurensis (불가사리 유래 콜라겐 펩타이드의 피부 면역 증진 효과)

  • Jeong, Hyang-Suk;Kwon, Min-Chul;Han, Jae-Gun;Ha, Ji-Hye;Jin, Ling;Kim, Jin-Chul;Kwak, Hyeong-Geun;Hwang, Bo-Young;Lee, Hyeon-Yong
    • Korean Journal of Food Science and Technology
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    • v.40 no.5
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    • pp.522-527
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    • 2008
  • Low molecular peptides were isolated from Asterias amurensis via SDS-PAGE. The peptides were separated via consecutive gel filtration as five fractions (F1-F5) according to molecular weights, based on the results of MALDI-TOF MS analysis. The molecular weight of the most active peptide was estimated as 15,000 daltons. The peptide showed cytotoxicity on normal human fibroblast cells at levels as low as 20% when 1.0 mg/mL of the samples was added. The peptide also exhibited higher levels of nitric oxide production from macrophages than the lipopolysaccaharides. It was determined that prostaglendin $E_2$ production was significantly inhibited, up to 127.8% as compared to the control. The low molecular peptide inhibited hyaluronidase activity as 535.7 ${\mu}g/mL$ of $IC_{50}$. It can be concluded that the relatively low molecular weight peptide, fucoidan, from A. amurensis has excellent cosmetic and immunomodulatory activities, which can be considered as a possible resource of new cosmetic agents for skin immunomodulation.

Study on the Degradation of Pigskin Collagen Using Irradiation Technique (방사선조사를 이용한 돈피 콜라겐의 저분자화 연구)

  • Cho, Young-Jun;Seo, Jung-Eun;Kim, Yun-Ji;Lee, Nam-Hyouk;Hong, Sang-Pil;Kim, Young-Ho
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.35 no.5
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    • pp.588-593
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    • 2006
  • This study was intended to observe possibility of which radiation technique can be used for oligopeptide production from pigskin collagen to reduce environmental pollution in processing and simplify the processing steps. Raw pigskin was ground using chopper, and then defatted in acetone cooled at $-20^{\circ}C$ freezer. Defatted dried pigskin was irradiated at 20, 40, 60, 100, 150, 200, 250, and 300 kGy using Co-60 gamma rays irradiator. With irradiation doses, the amount of soluble proteins increased, and the viscosity and turbidity of soluble proteins decreased, which could be clue of that irradiation degrade high molecular proteins directly. pH of soluble proteins from defatted pigskin increased in the sample above 150 kGy, and low molecular weight components (below 24 kDa) in SDS-PAGE increased. From gel permeation chromatography of the hydrolysates of pigskin irradiated at 300 kGy showed the major peak of 9,000, 8,200, 860, and 170 Da.

Preparation and Characterization of the Hydrolyzed Protein from Shaving Scraps of Leather Waste Containing Chromium (피혁폐기물(皮革廢棄物)인 Shaving scraps으로 부터 가수분해(加水分解) 단백질(蛋白質)의 제조(製造) 및 특성(特性))

  • Kim, Won-Ju;Cho, Ju-Sik;Lee, Hong-Jae;Heo, Jong-Soo
    • Journal of the Korea Organic Resources Recycling Association
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    • v.5 no.2
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    • pp.47-56
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    • 1997
  • To examine of possibility protein recycling of shaving scraps contained chrome generated from manufacturing process of leather, the characteristics of hydrolyzed protein that differently treated with MgO as alkaline agent were investigated. In alkaline hydrolysis of saving scraps treated with MgO, MgO had to be treated over 5.0% to maintain over pH 8.0 that is insoluble of chrome. Under the condition of alkaline treated with MgO, the solubility of chrome is low with about 60%. The average molecular weight of hydrolyzed proteins from shaving scraps treated with MgO was about 80~100 KD. The amino acid contents of that were largely collagen proteins such as glycine, alanine and proline, and acidic amino acids such as aspartic acid and glutatamic acid. The contents of Mg, Ca and Na in hydrolyzed protein were too much as liquid fertilizer, and chrome contents was 30~40 ppm that largely decreased in comparing with raw materials (40,000~42,000 ppm).

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Anti-wrinkle Activity of Low Molecular Weight Peptides Derived from the Collagen Isolated from Asterias amurensis (불가사리(Asterias amurensis) 콜라겐 유래 저분자 펩타이드의 피부주름 억제활성)

  • Kwon, Min-Chul;Kim, Cheol-Hee;Kim, Hyo-Sung;Syed, Abdul Qadir;Hwang, Bo-Yong;Lee, Hyeon-Yong
    • Korean Journal of Food Science and Technology
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    • v.39 no.6
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    • pp.625-629
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    • 2007
  • This study was carried out to investigate the anti-wrinkle effects of peptides derived from collagens isolated from Asterias amurensis, which was collected in the East Sea. The molecular weights of the peptides were between 10-50 kDa, as determined through sephadek G-75 gel. The cytotoxicities against CCD-986sk cells and HEL-299 cells were measured using the MTT assay. The cytotoxicity of all the fractions(F1: Fraction No. 4-13, 116 kDa; F2: Fraction No. 25-30, 100 kDa; F3: Fraction No. 45-55, 58 kDa; F4: Fraction No. 59-63, 43 kDa; F5: Fraction No. 79-90, 24 kDa) was less than 25%, by the addition of 1.0 mg/mL. These peptides did not show any adverse effects on human skin cells. In the presence of F1 at 1.0 mg/mL, matrix metalloproteinase-1 (MMP-1) expression of UVA-induced human normal fibroblasts was reduced to 34.8%. Overall, the results seem to suggest that peptides of approximately 20 kDa have superior anti-wrinkle effects.

Effect of Pig Skin Gelatin Hydrolysates on the Bone Mineral Density of Ovariectomized Rats (돈피 젤라틴 효소분해물이 난소 적출쥐의 골밀도에 미치는 영향)

  • Park, Jeong-Eun;Ham, Jun-Sang;Kim, Hey-Kyung;Lee, Chi-Ho;Kim, Dong-Wook;Seol, Kuk-Hwan;Oh, Mi-Hwa;Kim, Dong-Hun;Jang, Ae-Ra
    • Food Science of Animal Resources
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    • v.32 no.2
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    • pp.234-240
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    • 2012
  • This study was conducted to examine the effects of low molecular weight gelatin hydrolysates (GH, less than 3kDa), extracted from pig skin collagen on the bone metabolism of ovariectomized (OVX) rats. The rats in the experimental groups were randomly segregated into six different treatment groups such as 1) NC, the normal rat fed AIN 93 diet (basal diet) only; 2) OC, the OVX rat fed the basal diet only; 3) GH 0.1, the OVX rat fed the basal diet with 0.1% GH; 4) GH 0.8, the OVX rat fed the basal diet with 0.8% GH; 5) G 0.1, the OVX rat fed the basal diet with 0.1% gelatin; 6) G 0.8, the OVX rat fed the basal diet with 0.8% gelatin. Body weight gain in the GH 0.1, GH 0.8, and G 0.8 was significantly higher than those in the NC and OC. Feed intake of the GH 0.1 and GH 0.8 was higher than that of the NC and OC, while no significant difference was found in feed efficiency ratio (FER). BMD of the GH 0.8 was higher than that of the OC. However, gelatin hydrolysates and gelatin resulted in higher BMC level compare to the OC. Serum HDL-cholesterol of rat fed GH and gelatin was higher than that of OC (p<0.05). LDL-C of the GH 0.1 and the GH 0.8 tended to be less than that of OC. Serum alkaline phosphatase (ALP) of the GH 0.1 was lower than that of the OC. The serum of GH 0.8 showed lower osteocalcin value than the OC (p<0.05). In addition, GOT and GPT levels significantly decreased in all treatment groups. These results indicated that gelatin hydrolysates from pig skin gelatin hydrolysates enhanced BMD and serum biochemical parameters related to bone metabolism. Therefore, the gelatin hydrolysates could be used as a beneficial material to improve bone health.

The Effect of Treponema Denticola and Treponema Lecithinolyticum on Periodontal Ligament Cells (Treponema Denticola와 Treponema Lecithinolyticum이 치주인대세포에 미치는 영향)

  • Jung, Jung-Hag;Choi, Bong-Kyu;Moon, Ik-Sang;Cho, Kyoo-Sung;Chai, Jung-Kiu;Kim, Chong-Kwan
    • Journal of Periodontal and Implant Science
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    • v.29 no.2
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    • pp.311-326
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    • 1999
  • This study was investigated to observe the effect of Treponema denticola(TDC) and Treponema lecithinolyticum(TLC) on cultured human periodontal ligament cells. Several experiments were performed including MTT test for the inhibition effect of cell proliferation, LDH test for the cytotoxicity , gelatin zymography for the gelatinase activation and observation of cell morphology change using the phase-contrast microscopy. The results were as follows. 1. The effect of concentration on cell proliferation with time showed an inhibitory effect at high concentration $(150{\mu}g/well)$ for TLC and at low concentration( $9.4{\mu}gwell$ ) for TDC. 2. The effect of time on cell proliferation with concentration showed an inhibitory effect at $150{\mu}g/well$ on 2-day incubation for TLC and at $9.4{\mu}g/well$ on 2-day incubation for TDC. 3. The effect of heat-treated TDC and TLC on the inhibition of cell proliferation showed the difference in the heat-treated group compared to the non-heat treated group for TDC, whereas no difference was found for TLC. 4. The morphological changes which were observed from the phase-contrast microscopy showed the difference in the test group compared to the control group. The loss of spindle-like appearance, cell-to-cell detachment and inhibition of cell proliferation were observed. 5. There was no difference of the cytotoxicity effect between the test group and the control group in the LDH test. 6. The active form of progelatinase A with molecular weight 72kDa was activated in both TDC and TLC on the gelatin zymography. Regarding to the above results, TDC and TLC have an effect on periodontal ligament cells by playing an inhibitory role in cell proliferation and appears to activate progelatinase A which degrades type IV collagen.

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