• Applied Chemistry for Engineering
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• v.24 no.1
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• pp.62-66
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• 2013

This study was performed to investigate the physicochemical characteristics of glycoprotein extracted from carrot. We manufactured glycoprotein using natural vegetable raw materials carrots, and then analyzed it's physicochemical properties. The results showed that the nutritional composition of carrot glycoprotein (CG) consisted of 2.35% carbohydrate and 94.2% glycoprotein. There were small amounts of hydroxyproline and glycine known as characteristics of collagen peptide in the amino acid of CG, but there were large amount of glutamic acid and aspartic acid involved in the metabolism of glucose and fat. The calories of CG was 342.1 kcal/100 g and the molecular weight appeared less than 594 Da average molecular weight distribution.

• BMB Reports
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• v.40 no.4
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• pp.532-538
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• 2007

Mouse ficolin A is a plasma protein with lectin activity, and plays a role in host defense by binding carbohydrates, especially GlcNAc, on microorganisms. The ficolin A subunit consists of an N-terminal signal peptide, a collagen-like domain, and a C-terminal fibrinogen-like domain. In this study, we show that ficolin A can be synthesized and oligomerized in a cell and secreted into culture medium. We also identify a functionally relevant signal peptide of ficolin A by using MS/MS analysis to determine the N-terminal sequence of secreted ficolin A. When the signal peptide of mouse ficolin A was fused with enhanced green fluorescent protein (EGFP), EGFP was released into HEK 293 cell medium, suggesting that the signal peptide can efficiently direct ficolin A secretion. Moreover, our results suggest that the signal peptide of ficolin A has potential application for the production of useful secretory proteins.

• Journal of the Korea Academia-Industrial cooperation Society
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• v.16 no.8
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• pp.5452-5457
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• 2015

Conjugating a phytochemical, a strong antioxidant, with a functional peptide not only compensates for its stability, but also improves its solubility and anti-wrinkle effects, thereby contributing to the possibility of becoming an excellent cosmetic ingredient. Thus, in this study we examined the potential cosmetic use of a phytochemical-peptide derivative using gallic acid, a phytochemical with antioxidant, anti-inflammatory, and anti-cancer effects. To evaluate the antioxidant and wrinkle-improving efficacy of 5 synthesized gallic acids conjugated with LVH, IVH, KTTKS, YGGFM, and YGGFLRKYP respectively, we observed the expression of genes related to wrinkle improvement using DPPH radical scavenging activity and real-time PCR. As a result, all 5 derivatives had excellent free radical scavenging effects. The expression level of genes involved collagen synthesis also increased, and the secreted peptides during collagen production contributed to their antioxidant and wrinkle improving effects. These results mark the potential use of gallic acid peptide derivatives as a cosmetic ingredient for anti-oxidation and wrinkle improvement.

• Journal of Ginseng Research
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• v.36 no.1
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• pp.61-67
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• 2012

In the present study, effects of sun ginseng (SG) on the collagen synthesis and the proliferation of dermal fibroblast were investigated. Collagen synthesis was measured by assaying procollagen type I C-peptide production. In addition, the level of matrix metalloproteinase (MMP)-1 was assessed by western blot analysis. SG suppressed the MMP-1 protein level in a dose-dependent manner. In contrast, SG dose-dependently increased tissue inhibitors of MMP (TIMP)-1 production in fibroblasts. SG increased type I collagen production directly and/or indirectly by reducing MMP-1 and stimulating TIMP-1 production in human dermal fibroblasts. SG dose-dependently induced fibroblast proliferation and this, in turn, can trigger more collagen production. These results suggest that SG may be a potential pharmacological agent with anti-aging properties in cultured human skin fibroblast.

• Korean Journal of Food Science and Technology
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• v.41 no.4
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• pp.441-445
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• 2009

Recent research has revealed that hydrolyzed collagen peptides have beneficial effects in various diseases such as osteoarthritis and human rheumatoid arthritis and also play a protective role in skin by improving the activity of antioxidants. In this study, we investigated the effects of a novel mixture (AP-CPM01) containing collagen peptides and elastin peptides on photoaged hairless mice skin both in vivo and in vitro. To evaluate the effects of AP-CPM01 on UVBinduced skin wrinkle formation in vivo, the hairless mice were exposed to UVB irradiation and orally administered the AP-CPM01 at 333 mg/kg per day for 10 weeks. The effects on skin appearance and epidermal thickness were measured using bioengineering and histochemical methods. In addition, the influence of AP-CPM01 on collagen metabolism in human skin fibroblasts was also investigated. The skin of mice in the AP-CPM01 treated group had better appearance and less wrinkling than that of mice in the control group. In the human fibroblast cells, the amount of de novo procollagen synthesis was increased after AP-CPM01 treatment, reflecting that AP-CPM01 can induce de novo procollagen synthesis and reduce UVB-induced skin wrinkle formation. These results suggest that AP-CPM01 is a potent candidate for antiphotoaging functions.

• Journal of Environmental Science International
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• v.22 no.12
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• pp.1625-1631
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• 2013

In manufacturing of flatfish skin collagen peptide (FSCP) and flatfish protein hydrolysate (FPH) by reuse of dead flatfish from fish farm in Jeju island, the industrial process was optimized with the laboratory scale research and the on-field process. Segmented unit processes from raw material incoming to shipment were established to produce commercial product of FSCP and FPH. Total plate counts of FSCP were twenty five times of FPH, but food poisoning bacteria were not detected in two samples. FSCP and FPH were safe from heavy metal such as Pb(II), Cd(II) and Hg(II). The residual contents of antibiotics and disinfection matter in FSCP and FPH were not detected. The optimized process for mass production made the one-third of the running time and two times of the yield. From economic analysis, the production cost was estimated to 22,000 and 12,000 won/kg for FSCP and FPH, respectively. Therefore the product from the reuse of dead flatfish was expected to have a considerable competitive price and high added-value functional food material compared with other commercially available fish products.

• Proceedings of the SCSK Conference
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• 2003.09a
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• pp.590-600
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• 2003

The matrix metalloproteinases (MMPs) are a family of enzymes responsible for degrading connective tissue. MMPs catalyze the breakdown of collagen from the extracellular matrix, leading to wrinkle formation and accelerated skin aging. Furthermore, ultraviolet irradiation causes increased expression of certain MMPs. In the extracellular matrix turnover, MMPs are interacting with endogenous regulators named tissue inhibitors of metalloproteinases (TIMPs). Using peptide substrate assays, it has been demonstrated that TIMP-MMP complexes interact highly specifically with $K_{i}$ values of 10$^{-9}$ -10$^{-16}$ M. Therefore applications for TIMP as inhibitor of collagen degradation are suggested for cosmetic anti-aging products to prevent wrinkle formation and loss of elasticity. To date four TIMP proteins (TIMP-1, TIMP-2, TIMP-3 and TIMP-4) have been identified which show a high degree in sequence similarity. The production of human TIMP-2, a 194-residue nonglycosylated protein, was performed by fed-batch culture of Escherichia coli. TIMP-2 accumulated in the bacterial cells in an insoluble form as inclusion bodies. The inclusion bodies were solubilized and the protein refolded to yield the native TIMP-2 in the active form. The integrity of the protein was confirmed by mass analysis, Edman sequencing and gel shift experiments with authentic samples. The inhibitory activity of the refolded and purified TIMP-2 was demonstrated with MMP-1 and MMP-2 assays using synthetic fluorogenic peptide substrates.s.

• The Journal of Korean Medicine
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• v.24 no.4
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• pp.120-126
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• 2003

Object : This study was done to evaluate the inhibitory effect of Samul-tang (Siwu-tang) on collagen production by cultured murine hepatic non-parenchymal cells. Methods : Hepatic non-parenchymal cells were cultured from normal Sprague-Dawley rats and established in a primary cell culture on uncoated plastic culture plates. The Samul-tang (Siwu-tang) was treated into the cell culture media for 72 hours and the cells were harvested for analysis. Analyses were done on cell proliferation, [3H]thymidine incorporation assay and procollagen type IC-peptide. Results : The cultured cells resembled fibroblasts in shape and produced procollagen which is consistent to fibrogenesis in vivo. Proliferation of the non-parenchymal cells was inhibited slightly and the [3H]thymidine incorporation assay showed a dose-dependent decrease by Samul-tang (Siwu-tang) treatment. Production of procollagen type I C-peptide was decreased by low-concentration treatment of the Samul-tang (Siwu-tang), but increased by high-concentration treatment. Conclusion : It seemed that the cells were responding to the Samul-tang (Siwu-tang) in low-concentration, thus producing less collagen. However, when the drug was administered with high enough concentration to cause excessive stimulation of cells, it seemed that the activated cells might overly produce procollagen, the precursor of collagen, thus aggravating fibrosis of the liver. So, it is considered that the proper concentration of Samul-tang (Siwu-tang) is important when treating patients with liver cirrhosis based on the patients' status.

• Food Science of Animal Resources
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• v.34 no.2
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• pp.151-157
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• 2014

This study investigated the effects of three proteases (trypsin, pepsin and chymotrypsin) on the hydrolysis efficiency of porcine placenta and the molecular weight (Mw) distributions of the placental hydrolysates. Because placenta was made up of insoluble collagen, the placenta was gelatinized by applying thermal treatment at $90^{\circ}C$ for 1 h and used as the sample. The placental hydrolyzing activities of the enzymes at varying concentrations and incubation times were determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and gel permeation chromatography (GPC). Based on the SDS-PAGE, the best placental hydrolysis efficiency was observed in trypsin treatments where all peptide bands disappeared after 1 h of incubation as compared to 6 h of chymotrypsin. Pepsin hardly hydrolyzed the placenta as compared to the other two enzymes. The Mw distribution revealed that the trypsin produced placental peptides with Mw of 106 and 500 Da. Peptides produced by chymotrypsin exhibited broad ranges of Mw distribution (1-20 kDa), while the pepsin treatment showed Mw greater than 7 kDa. For comparisons of pre-treatments, the subcritical water processing (37.5 MPa and $200^{\circ}C$) of raw placenta improved the efficiency of tryptic digestions to a greater level than that of a preheating treatment ($90^{\circ}C$ for 1 h). Consequently, subcritical water processing followed by enzymatic digestions has the potential of an advanced collagen hydrolysis technique.

• Journal of the Korean Applied Science and Technology
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• v.31 no.3
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• pp.387-393
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• 2014

In this study were performed to investigate the physicochemical properties of flying fish roe shell extract(FRSE) extracted from flying fish roe shell. FRSE was prepared using marine flying fish roe shell, and then analyzed it's physicochemical properties. The result showed that the nutritional composition of FRSE consisted of 81.00% protein, 9.12% ash and 4.48% moisture. There were OH-proline and glycine known as characteristics of collagen peptide in the amino acid analysis of FRSE, and there were large amount of glutamic acid and aspartic acid involved in the metabolism of glucose and fat. The calories of FRSE was 347 kcal/100g and molecular weight appeared less than 1,300 Da molecular weight distribution.