• 한국융합학회논문지
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• 제11권5호
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• pp.61-72
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• 2020

본 연구에서는 어류 유래 콜라겐 가수분해물로부터 한외여과법(MWCO; 1 kDa)과 역상액체크로마토그래피를 이용하여 항노화 활성 기능성 펩타이드를 분리, 정제하고자 하였다. 펩타이드의 분리, 정제에 따른 항노화 활성 변화는 Hs68 세포를 사용하여 procollagen 합성능과 MMP-1 저해능을 측정하여 확인하였다. 콜라겐 가수분해물과 비교하여 최종 분리, 정제된 기능성 펩타이드의 procollagen 합성과 MMP-1 저해는 각각 46%와 77% 향상되었다. 또한 기능성 펩타이드의 구조는 Gly-Arg-Arg-Gly-Asn-Lys (GRRGNK; 콜라겐의 기본 구조인 Gly-X-Y sequence와 유사)의 서열을 보였고, 분자량은 686.175 Da으로 분석되었다. 따라서 본 연구에서는 어류 콜라겐 가수분해물로부터 분리한 펩타이드가 식품, 화장품, 의약품 등의 피부노화 지연 효과를 보이는 기능성 원료로 다양하게 사용할 수 있는 가능성을 확인하였다.

• 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.

• 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.

• 한국환경과학회지
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• 제22권12호
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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.

• Journal of Applied Biological Chemistry
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• 제62권1호
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• pp.101-107
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• 2019

The objectives of this study were to evaluate the anti-aging effects and investigate the effect of simulated gastrointestinal (GI) digestion on the anti-aging properties and intestinal permeation of the potential fish collagen hydrolysates (FCH). Therefore, procollagen synthesis, matrix metalloproteinase-1 (MMP-1) production, and Caco-2 cell permeability were analyzed before and after in vitro digestion for FCHs, low-molecular weight fractions (<1 kDa), and high molecular weight fractions (>1 kDa). After being subjected to GI digestion, the level of MMP-1 inhibition was maintained, although the procollagen production was significantly (>20%) lower with all samples. Also, the digested FCHs and their <1 kDa fraction yielded 9.1 and 13.8% increased peptide transport, respectively, compared to undigested samples. Based on the effective intestinal permeation and high digestive enzyme stability, the <1 kDa fraction of FCHs is a potential bioactive material suitable for anti-aging applications in the food and cosmetics industries.

• 한국해양바이오학회지
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• 제14권1호
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• pp.9-24
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• 2022

Low-molecular weight peptides derived from fish collagen exhibit several bioactivities, including antioxidant, antiwrinkle, antimicrobial, antidiabetic, and antihypertension effects. These peptides are also involved in triglyceride suppression and memory improvement. This study aimed to investigate the optimal processing condition for preparing low-molecular weight peptides from flounder skin, and the properties of the hydrolysate. The optimal processing conditions for peptic hydrolysis were as follows: a ratio of pepsin to dried skin powder of 2% (w/w), pH of 2.0, and a temperature of 50℃. Peptic hydrolysate contains several low-molecular weight peptides below 300 Da. Gly-Pro-Hyp(GPHyp) peptide, a process control index, was detected only in peptic hydrolysate on matrix-assisted laser desorption/ionization-time-of-flight(MALDI-TOF) spectrum. 2,2'-azinobis-(3-3-ethylbenzothiazolline-6- sulfonic acid(ABTS) radical scavenging activity of the peptic hydrolysate was comparable to that of 1 mM ascorbic acid, which was used as a positive control at pH 5.5, whereas collagenase inhibition was five times higher with the peptic hydrolysate than with 1 mM ascorbic acid at pH 7.5. However, the tyrosinase inhibition ability of the peptic hydrolysate was lower than that of arbutin, which was used as a positive control. The antibacterial effect of the peptic hydrolysate against Propionibacterium acne was not observed. These results suggest that the peptic hydrolysate derived from a flounder skin is a promising antiwrinkle agent that can be used in various food and cosmetic products to prevent wrinkles caused by ultraviolet radiations.

• Journal of Microbiology and Biotechnology
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• 제34권1호
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• pp.17-28
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• 2024

Low molecular weight collagen peptide (LMWCP) is a collagen hydrolysate derived from fish. We investigated the effects of LMWCP on hair growth using human dermal papilla cells (hDPCs), human hair follicles (hHFs), patch assay, and telogenic C57BL/6 mice, while also examining the underlying mechanisms of its action. LMWCP promoted proliferation and mitochondrial potential, and the secretion of hair growth-related factors, such as EGF, HB-EGF, FGF-4, and FGF-6 in hDPCs. Patch assay showed that LMWCP increased the neogeneration of new HFs in a dose-dependent manner. This result correlated with an increase in the expression of dermal papilla (DP) signature genes such as, ALPL, SHH, FGF7, and BMP-2. LMWCP upregulated phosphorylation of glycogen synthase kinase-3β (GSK-3β) and β-catenin, and nuclear translocation of β-catenin, and it increased the expression of Wnt3a, LEF1, VEGF, ALP, and β-catenin. LMWCP promoted the growth of hHFs and increased the expression of β-catenin and VEGF. Oral administration of LMWCP to mice significantly stimulated hair growth. The expression of Wnt3a, β-catenin, PCNA, Cyclin D1, and VEGF was also elevated in the back skin of the mice. Furthermore, LMWCP increased the expression of cytokeratin and Keratin Type I and II. Collectively, these findings demonstrate that LMWCP has the potential to increase hair growth via activating the Wnt/β-catenin signaling pathway.