• 한국응용과학기술학회지
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• 제26권4호
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• pp.457-466
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• 2009

This study is manufacturing method and analysis of feasibility about collagen peptide from fish scale. This is processed by enzyme hydrolysis, isolating and refining etc. The results of analysis of nutritional composition showed protein content of collagen peptide. In the analysis of constitutive amino acids, the ratio of contents of hydroxyproline and glycine, the characteristics of collagen peptides appeared similar and the contents of glutamic acid and aspartic acid which are involved in protein metabolism. As a result of measurement of total polyphenol content and total flavonoid, it showed that collagen peptide had more contents generally, and the effect of bioactivity of pig-skin collagen peptide appeared higher although different kinds of scale collagen peptide showed a little DPPH radical scavenging ability, total antioxidant capacity by ABTS, ACE inhibitory.

• 한국환경과학회지
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• 제25권4호
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• pp.579-588
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• 2016

본 연구에서는 홍어껍질에서 추출한 콜라겐 펩타이드 이화학적 특성과 비만 유발 쥐에 대한 투여 실험을 통해서 지방조직의 지질 감소효과를 조사하였으며, 홍어 껍질 콜라겐 펩타이드를 원료로 한 응용 제품 개발을 통하여 산업적 적용을 검토하였다. 일반성분 분석 결과 홍어 껍질 콜라겐 펩타이드는 대부분이 단백질로 이루어져 있는 고단백 저지방 물질이며, 분자량 측정 결과 약 1000 Da.의 저분자량이고, 아미노산 분석에서는 전형적인 콜라겐 단백질의 특성을 나타내었다. 비만 유발 쥐에 홍어 껍질 콜라겐 펩타이드를 500 mg/kg씩 18일간 경구 투여한 실험 결과에서 사료 섭취량과 음수량이 상당량 줄어 들었으며, 지방조직의 중성지방과 총 콜레스테롤 수치가 유의적으로 감소하였다. 홍어 껍질 콜라겐 펩타이드를 대량생산을 한 결과 제품의 최종 수율은 원료대비 약 17.23%로 상당히 높은 수율을 나타내었다. 이를 원료로 한 기능성 화장품 및 생활용품을 생산 및 출시하였다. 따라서 홍어 가공 부산물인 껍질을 재이용한 기능성 단백질 소재 개발을 통하여 건강기능식품과 화장품 분야에서의 기능성과 가격경쟁력을 갖춘 소재 개발에 기여 할 것으로 기대된다.

• 한국축산식품학회지
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• 제36권6호
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• pp.807-818
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• 2016

The effect of addition commercial fish collagen hydrolysate and encapsulated fish collagen hydrolysate on the quality characteristics of sucuk (a traditional Turkish dry-fermented sausage) was investigated. Fish collagen hydrolysates were encapsulated with maltodextrin (MD) which has two different dextrose equivalent (12DE and 19 DE), with two different types of core/coating material ratios (10% peptide : 90% MD, 20% peptide : 80% MD). Than six group of sucuk dough (control, peptide, MD1210, MD1220, MD1910, MD1920) prepared and naturally fermented. The effects of the ripening period (28 d), treatment (peptide and encapsulated peptide addition) 'ripening period ${\times}$ treatment' interaction on sucuk's pH, lactic acid contents, $a_w$ values and moisture contents were statistically significant (p<0.01). The pH, moisture and $a_w$ decrease and lactic acid concentration increses during ripening period. The highest pH was observed with peptide added group (5.41), and encapsulated peptide added groups (4.76-4.77) were lower than the control group (5.26). Lactic acid concentration was affected from treatment and all treatment groups lactic acid concentration (0.185-0.190%) were higher than the control group (0.164%). Antioxidant and Angiotensin converting enzyme inhibition activities of water soluble protein extracts were significantly (p<0.01) increased during ripening time. Antioxidant activity reached the highest level at $28^{th}$ d. There was no significant increase observed after fermentation for both activities. Antioxidant activity of encapsulated peptide added (%39.56-40.48) groups were higher than control (34.28%) and peptide added (33.99%) groups except MD1920 (38.30%). The effect of the ripening period of the sucuk samples on TBA values was found to be statistically significant (p<0.01) while treatment and 'ripening period ${\times}$ treatment' interaction were not to be significant (p<0.05). The value of hardness was the highest in the encapsulated peptide added groups (29.27, 35.83 N), and it was 20.40 N and 15.41 N in the peptide added group and the control group respectively.

• BMB Reports
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• 제36권2호
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• pp.154-158
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• 2003

Collagen is a family of proteins which consists of several genetically distinct molecular species and is intimately involved in tissue organization, function, differentiation and development. The purpose of this study was to investigate the concentration of different hydroxyproline (Hyp) fractions viz., total, free, peptide-bound, protein-bound, soluble- and insoluble-collagen hydroxyproline (Hyp) in various bovine tissues. Results showed that liver had the highest concentration of free Hyp followed by kidney, brain, spleen, lungs, muscle and heart. Liver also had the highest concentration of peptide-bound collagen Hyp followed by kidney, heart, spleen, lungs, brain and muscle. The concentration of protein-bound collagen Hyp was highest in the liver, followed by kidney, spleen, lungs, muscle, brain and heart. Total Hyp was highest in the liver, followed by kidney, spleen, brain, heart, muscle and lungs. Liver also had significantly high concentration of collagen as compared to other tissues examined (P<0.001). Spleen had the significantly higher concentration of soluble-collagen Hyp when compared to other tissues (P<0.001). This was followed by heart, muscle, lungs, brain, kidney and liver. Heart had the highest concentration of insoluble-collagen Hyp followed by lungs, kidney, liver, muscle, spleen and brain. The variation among the insoluble-collagen Hyp concentration of heart and muscle, spleen and brain was significant (P<0.001). We speculate that these differences could be due to the variation in turn over of rate of collagen metabolism in this species.

• Journal of Periodontal and Implant Science
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• 제40권1호
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• pp.11-18
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• 2010

Purpose: Significant interest has emerged in the design of cell scaffolds that incorporate peptide sequences that correspond to known signaling domains in extracellular matrix and bone morphogenetic protein. The purpose of this study was to evaluate the bone regenerative effects of the synthetic peptide in a critical-size rat calvarial defect model. Methods: Eight millimeter diameter standardized, circular, transosseus defects created on the cranium of forty rats were implanted with synthetic peptide, collagen, or both synthetic peptide and collagen. No material was was implanted the control group. The healing of each group was evaluated histologically and histomorphometrically after 2- and 8-week healing intervals. Results: Surgical implantation of the synthetic peptide and collagen resulted in enhanced local bone formation at both 2 and 8 weeks compared to the control group. When the experimental groups were compared to each other, they showed a similar pattern of bone formation. The defect closure and new bone area were significantly different in synthetic peptide and collagen group at 8 weeks. Conclusions: Concerning the advantages of biomaterials, synthetic peptide can be an effective biomaterial for damaged periodontal regeneration.

• 한국응용과학기술학회지
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• 제35권4호
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• pp.1369-1378
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• 2018

홍어 껍질 유래 콜라겐 펩타이드를 한외여과막을 이용하여 분자량의 크기를 1,000 Da 이하와 1,000 Da 이상으로 분리하고 그 효과를 비교하고자 하였다. 각각의 시료를 비만 유발 실험동물인 db/db mice에 체중당 200 mg의 콜라겐 펩타이드를 8주간 투여하였다. 본 연구의 결과는 콜라겐 펩타이드를 투여한 군에서 비만대조군에 비해 체중 증가량의 감소, 혈액 및 간조직의 활성산소 농도의 감소, 간조직의 산화적 스트레스가 완화된 것으로 나타났다. 또한 콜라겐 투여군에서 염증반응과 관련된 간조직의 핵전사인자($NF-{\kappa}B$) 및 효소(COX2, iNOS), 염증성 사이토카인(IL-6)발현이 비만대조군에 비해 유의적으로 감소하였다. 분자량의 크기에 따라 약간의 차이가 나타났지만, 전반적으로는 유의적이지 않았다. 따라서 홍어 콜라겐 펩타이드의 비만에 의해 유발된 염증반응이 억제되었는데, 이는 콜라겐의 산화적 스트레스 완화작용에 기인한 것으로 사료된다.

• BMB Reports
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• 제49권6호
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• pp.331-336
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• 2016

In murine collagen-induced arthritis (CIA), self-reactive T cells can recognize peptide antigens derived from type-II collagen (CII). Activation of T cells is an important mediator of autoimmune diseases. Thus, T cells have become a focal point of study to treat autoimmune diseases. In this study, we evaluated the efficacy of recombinant MHC class II molecules in the regulation of antigen-specific T cells by using a self peptide derived from CII (CII260-274; IAGFKGEQGPKGEPG) linked to mouseI-A^q in a murine CIA model. We found that recombinant I-A^q/CII260-274 molecules could be recognized by CII-specific T cells and inhibit the same T cells in vitro. Furthermore, the development of CIA in mice was successfully prevented by in vivo injection of recombinant I-A^q/CII260-274 molecules. Thus, treatment with recombinant soluble MHC class II molecules in complex with an immunodominant self-peptide might offer a potential therapeutic for chronic inflammation in autoimmune disease such as rheumatoid arthritis.

• 한국환경과학회지
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• 제22권11호
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• pp.1465-1471
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• 2013

To develop the protein materials by the reutilization of dead flatfish from fish farms in Jeju island, the physicochemical characteristics and the functional activities of collagen peptide extracts were investigated. Flatfish skin collagen peptide (FSCP) and flatfish protein hydrolysate (FPH) were manufactured from dead flatfish. The differences of pH, moisture and fat contents between FSCP and FPH were not significant, fat contents were analyzed less than 0.3%, and trans-fat, saturated fat and cholesterol were not detected in both samples. Protein contents of FSCP and FPH showed about 92% and 95%, respectively. In the analysis of amino acids, glycine and hydroxy proline content in FSCP was 24.22% and 6.15%, respectively, showed a typical characteristics of the collagen protein, but essential amino acids contents such as threonine, valine, methionine, isoleusine, leusine and phenylalanine were relatively higher than those of FPH. Average molecular weight of FSCP was measured as 1,102 which was almost equal value with that of tuna collagen peptide. The antioxidant activities and functional properties showed high but did not show significant difference between two samples.

• 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.

• 인간식물환경학회지
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• 제22권1호
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• pp.39-52
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• 2019

To evaluate the protective effect of collagen peptide-coated coffee extract on skin aging, cell viability was measured with a MTT assay using cultured CCD-986sk fibroblasts, and its effect on wrinkles in the skin of hairless mice induced by UVB-irradiation was examined. In addition, its effect on procollagen synthesis and anti-oxidative, and its inhibitory activity against collagenase, elastase, tyrosinase and MMP-1 were analysed. After the 30-minute topical treatment, the animals were exposed to UVB irradiation (60-100 mJ/cm²) for 4 weeks and its intensity increased during the period. Under the experimental conditions set in this study, the skin thickness of hairless mice significantly decreased (11.8-21.3%) compared to the control group. Based on these results, the prolonged oral intake of a collagen peptide mixture with coffee is expected to significantly increase the synthesis of procollagen in dermal fibroblasts, thereby contributing to the alleviation of wrinkling and lowered elasticity due to structural damage to the dermal layer caused by UV. The oral intake of collagen-coated coffee contributes to increasing collagen biosynthesis in a dose-dependent manner and alleviates the symptoms of thickened keratin caused by UV irradiation. However, it did not inhibit the enzymes involved in skin aging, whitening, wrinkle improvement, and antioxidation. Based on the these results, it can be concluded that the intake of collagen peptide-coated coffee extract can be utilized as an alternative material for the prevention or treatment of diseases associated with photoaging.