• 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.

• 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.

• 한국수산과학회지
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• 제49권5호
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• pp.594-599
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• 2016

Infection with HIV (Human immunodeficiency virus), over time, develops into acquired immunodeficiency syndrome (AIDS). The development of non-toxic and effective anti-HIV drugs is one of the most promising strategies for the treatment of AIDS. In this study, we investigated the anti-HIV-1 activity of gelatin hydrolysates from Alaska pollack skin. Gelatin hydrolysates were prepared using four enzymes (alcalase, flavourzyme, neutrase, and pronase E). Among these, the pronase E gelatin hydrolysate was found to inhibit HIV-1 infection in the human T cell-line MT4. It exhibited inhibitory activity on HIV-1_IIIB-induced cell lysis, reverse transcriptase activity, and viral p24 production at noncytotoxic concentrations. Moreover, it decreased the activation of matrix metalloproteinase-2 (MMP-2) in vitro. Because HIV infection-induced activation of MMP-2 can accelerate collagen resolution and collapse of the immune system, pronase E gelatin hydrolysate might prevent the activation of MMP-2 in cells, resulting in collagen stabilization and immune cell homeostasis consistent with anti-HIV activation. These results suggest that pronase E gelatin hydrolysate could potentially be incorporated into a novel therapeutic agent for HIV/AIDS patients.

• 한국식품과학회지
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• 제51권5호
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• pp.466-472
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• 2019

본 연구는 식용 어류로부터 획득한 콜라겐 중 Gly-Pro-Hyp를 주요 지표로 하는 고함량 콜라겐 트리펩타이드에 대한 피부의 광노화 억제 효과를 확인하고자 HaCaT 세포와 SKH-1 hairless 마우스를 활용한 전임상 실험을 실시하였다. HaCaT 세포는 UVB 조사 이후 Collagen 1A와 MMP-1 그리고 -13의 변화를 관찰하였으며 마우스 실험은 총 50마리의 마우스를 5군으로 구분한 다음 NOR을 제외한 모든 마우스에 UVB를 조사하고 양성대조군인 retinoic acid 혹은 실험물질인 CTP (17, 34 mg/kg)를 섭취시키며 실험하였다. CTP는 HaCaT 세포의 Collagen 1A 증가 및 MMP-1와 -13 감소에 긍정적인 영향을 미쳤을 뿐만 아니라 UVB 조사를 통해 증가된 실험동물의 피부 주름 수와 깊이 그리고 넓이를 현저히 개선시키는 효과를 나타내었다. 특히, CTP의 섭취는 UVB 조사에 따라 파괴된 피부조직 내 콜라겐의 양과 밀도를 정상적으로 회복시켰을 뿐만 아니라 Collagen 1A의 발현 증가 및 MMP1과 -13의 발현 감소를 유도함으로써 UVB 조사에 의한 주름 생성을 감소시킨 효과를 보여주었다. 따라서, 본 실험은 CTP 섭취가 콜라겐 붕괴에 관여하는 MMPs 단백질 발현을 감소시키고 이와는 반대로 Collagen 1A의 발현은 증가시킴을 확인함으로써 피부 외관의 주름 수와 넓이 혹은 깊이를 개선시키는 것에 긍정적인 영향을 미치는 것으로 판단할 수 있다.

• 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.

• 한방안이비인후피부과학회지
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• 제34권2호
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• pp.1-20
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• 2021

Objective : The object of this study was to assess the efficacy of hydrolysate from Phellinus igniarius(HPI) on anti-aging activities in vitro measurement and mini clinical study performed on 5 subjects. Methods : To evaluate skin anti-aging efficacy of HPI, 1,1-diphenyl-2-picrylhydrazyl(DPPH) radical scavenging activity, type I collagen synthesis, inhibition of nitric oxide(NO) production, inhibiton of tyrosinase, hyaluronan synthase(HAS)2, 3 mRNA expression were measured in vitro. Also, mini clinical study of skin hydration was performed on 5 subjects using HPI in distilled water(DW) and 1,3-butylene glycol diluted solution(30% in DW). Results : 1. DPPH radical scavenging activity of HPI was increased in a dose-dependant. 2. Type I collagen synthesis was increased in 50, 100 and 500㎍/㎖ of HPI. 3. NO production was not inhibited in all concentrations of HPI. 4. Tyrosinase was inhibited in 500, 1000, 2500 and 5000㎍/㎖ of HPI. 5. HAS2 mRNA expression was increased in 50, 100, 150 and 200㎍/㎖ of HPI, HAS3 mRNA expression was increased in 100, 150, and 200㎍/㎖ of HPI. 6. In the mini clinical study of 5 subjects, there was a difference in skin hydration over time for each solutions, but it was not statistically siginificant. Conclusions : HPI increased DPPH radical scavenging activity, type I collagen synthesis, and HAS2, HAS3 mRNA expression. HPI also suppressed tyrosinase. The findings of this study suggest that HPI can be used as an skin anti-aging material.

• 대한화장품학회지
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• 제47권2호
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• pp.147-153
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• 2021

콜라겐 가수 분해물(collagen hydrolysate, CH)은 피부 진피 섬유아세포를 자극하여 콜라겐과 엘라스틴 같은 세포 외 기질 합성을 촉진함으로써 피부 노화 방지에 도움을 주는 것으로 알려져 있다. 최근 피부 노화를 일으키는 다양한 요인 중 최종당화산물(advanced glycation end products, AGEs)이 주목을 받고 있음에도 불구하고, 아직까지 CH가 AGE축적에 미치는 영향은 연구된 바 없다. CH는 피부 구조단백질의 생성을 촉진하여 AGE 축적에 영향을 줄 수 있으므로, 이를 확인하기 위해 트리펩타이드25%, Gly-Pro-Hyp 4%를 함유한 CH인 저분자콜라겐펩타이드(low molecule weight collagen peptide, LMCP)를 이용하여 임상시험을 수행하였다. 피부 조직 내 AGE 축적량을 평가하기 위해 AGE reader를 사용하여 피부자가형광(skin autofluorescence, SAF) 값을 측정하였다. 0.5%와 1.0% LMCP 용액을 8 주 동안 피험자의 전박에 도포한 결과, 시험부위의 SAF값이 대조부위에 비해 유의하게 감소하였다. 추가적으로, LMCP에 의한 피부섬유아세포의 콜라겐 합성 촉진을 평가하기 위해 CCD-986sk를 이용하여 in vitro test를 수행하였다. 그 결과, 800 ㎍/mL의 LMCP는 CCD-986sk의 human pro-collagen Iα1(COL1A1) 합성을 증가시켰다. 본 연구를 통해 LMCP도포가 콜라겐 합성을 촉진하여 항당화 효과에 도움을 줄 수 있다는 것을 확인하였으며, 이는 LMCP가 노화 방지 화장품 원료로써 잠재력이 있음을 시사한다.

• 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.

• Fisheries and Aquatic Sciences
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• 제14권3호
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• pp.174-178
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• 2011

This study aimed to determine the degree of hydrolysis and angiotensin-I-converting enzyme (ACE)-inhibitory activity of Giant Jellyfish Nemopilema nomurai (jellyfish) hydrolysates. The degree of hydrolysis using six proteolytic enzymes (Alcalase, Flavozyme, Neutrase, papain, Protamex, and trypsin) ranged from 13.1-36.8% and the inhibitory activities from 20.46-79.58%. Using papain hydrolysate, we newly isolated and characterized ACE-inhibitory peptides with a molecular weight of 3,000-5,000 Da that originated from jellyfish collagen. The purified peptide (FII-b) was predicted to be produced from an alpha-2 fragment of the type IV collagen of jellyfish. The N-terminal sequence of FII-b was Asp-Pro-Gly-Leu-Glu-Gly-Ala-His-Gly- and showed 87% identity to the collagen type IV alpha-2 fragment of Rattus norvegicus and a predicted protein from Nematostella vectensis, indicating that the ACE-inhibitory peptide originated from the collagen hydrolysate and had an $IC_{50}$ value of 3.8 ${\mu}g$/mL. The primary structure of the fragment is now being studied; this peptide represents an interesting new type of ACE inhibitor and will provide knowledge of the potential applications of jellyfish components as therapies for hypertension.

• 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.