• Food Science and Biotechnology
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• 제16권4호
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• pp.549-556
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• 2007

The study was carried out to examine on the refiner discharge from Alaska pollock as a collagen resource by characterizing biochemical and functional properties of collagen. The refiner discharge from Alaska pollock surimi manufacturing was a good resource for collagen extraction according to the results of total protein, heavy metal, volatile basic nitrogen, collagen content, amino acid composition, and thermal denaturation temperature (TDT). TDT of acid soluble collagen from refiner discharge showed $20.7^{\circ}C$, which was similar to that of collagen from Alaska pollock muscle and was higher than that of collagen from Alaska pollock skin. TDT of acid-soluble collagen from refiner discharge was, however, lower than those of skin collagens from warm fish and land animal. Acid-soluble collagen from refiner discharge of Alaska pollock could be used as a functional ingredient for food and industrial applications according to the results of water and oil absorption capacities, and emulsion properties. In addition, if the thermal stability of the acid-soluble collagens is improved, collagen from refiner discharge from Alaska pollock could be more effectively used.

• 한국식품저장유통학회지
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• 제17권1호
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• pp.91-99
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• 2010

상어의 껍질과 육 조직으로부터 산 (citric acid) 가용성 콜라겐 (ASC)과 pepsin 가용성 콜라겐 (PSC)의 추출 및 탈색조건을 조사하였다. 비 콜라겐 단백질을 제거하기 위한 적정 NaOH 농도는 0.3 N이었으며 처리시간은 9시간이었다. 상어껍질의 탈색은 생 원료에 대하여 10배량의 0.48% sodium hypochlorite로 60분간 처리하는 것이 적절하였다. ASC 및 PSC의 추출시 산의 적정농도는 각각 0.3 M 및 0.1 M이었고, 추출시간은 각각 72시간 및 24시간 이었다. 산가용성 콜라겐인 ASSC (citric acid soluble shark skin collagen)와 ASMC (citric acid soluble shark muscle collagen), pepsin 가용성 콜라겐인 PSSC(pepsin and citric soluble shark skin collagen)와 PSMC (pepsin soluble shark muscle collagen)에 함유된 총 단백질 함량은 각각 88.66, 83.09, 90.33 및 84.81% (dry basis)이었으며 시판 표준 콜라겐의 88.86%와 대등하였다. Hydroxyproline의 함량으로부터 산출한 순 콜라겐 함량은 ASC에서는 25.70~70.31%, PSC에서는 32.94~83.09%이었다. 상어육과 껍질 (dry basis) 100 g으로부터 얻을 수 있는 콜라겐의 수율은 ASC는 53.85~57.22%, PSC는 20.81~23.28%이었다.

• 한국식품과학회지
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• 제27권4호
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• pp.576-581
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• 1995

피부조직에서 추출한 콜라겐의 유동특성을 검토하여 콜라겐을 효율적으로 활용할 수 있는 기초자료를 얻고자 하였다. 콜라겐의 점도는 동물의 나이와 성(sex), 콜라겐 종류에 따라 차이를 보였다. 즉, 주령에 따라서는 콜라겐의 종류에 관계없이 $6{\sim}12$주령의 것이 비교적 높게 나타났으며, 동일 주령에서는 수컷의 점도보다 암컷의 점도가, 그리고 불용성 콜라겐의 점도보다 산가용성 콜라겐의 점도가 높게 나타났다. 콜라겐 용액은 Bingham plastic 및 thixotropic 유체의 특성을 나타냈으며, 온도, pH, 에탄올 농도 및 콜라겐 농도에 따라 점도 변화가 뚜렷하게 나타났다. 즉, 콜라겐 농도를 6%까지 높일 경우 콜라겐 용액의 점조도는 직선적으로 증가하는 경향(산가용성 콜라겐 r=0.972, 불용성 콜라겐 r=0.957)을 나타냈는데, 산가용성 콜라겐의 증가속도가 불용성 콜라겐의 경우보다 높게 나타났다. 온도 증가에 따라 콜라겐 용액의 점조도는 감소하였으며 특히, 산가용성 콜라겐에서는 $30{\sim}40^{\circ}C$ 온도구간에서 점조도가 급격히 감소하였다. pH에 따라 산가용성 콜라겐의 점조도는 pH 6에서 최대치를 보였고, pH 10 부근에서 다시 증가하는 biphasic 현상을 나타냈으나, 불용성 콜라겐의 경우는 pH에 큰 영향을 받지 않았다. 에탄올 농도에 따른 산가용성 콜라겐과 불용성 콜라겐의 점조도는 에탄올 농도 $40{\sim}60%$ 수준에서 높게 나타났다.

• 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.

• Fisheries and Aquatic Sciences
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• 제24권12호
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• pp.406-414
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• 2021

The objective of this study was to investigate the yield and characteristics of collagen protein extracted from the muscle of four different species of mantis shrimp: Miyakella nepa, Harpiosquilla harpax, Erugosquilla woodmasoni, and Odontodactylus cultrifer. Mantis shrimp muscle was extracted by using a pepsin-solubilization technique, with 0.5 M acetic acid and 5% pepsin enzyme. The highest collagen yield was from M. nepa muscle (0.478 ± 0.06%), which was significantly greater (p < 0.05) than that from H. harpax, O. cultrifer, and E. woodmasoni (0.313 ± 0.03%, 0.123 ± 0.02%, and 0.015 ± 0.00%, respectively). The freeze-dried collagen appeared as thin fibers, and formed an opaque film. The pepsin-soluble collagen (PSC) from four mantis shrimp species was analyzed by gel electrophoresis. The results showed that all species of mantis shrimp contained type I collagen, consisting of β, α1, and α2 subunits with average molecular weights of 250, 145, and 118 kDa, respectively. The study of the solubility of collagen showed that, for NaCl, collagen had the highest relative solubility in 2% NaCl (80.20 ± 4.95%). In contrast, the solubility decreased at higher NaCl concentrations. However, in terms of pH, collagen had the highest relative solubility at pH 3 (91.32 ± 5.14%), and its solubility decreased at higher pH. FT-IR spectroscopy was used to compare the collagen with a model compound. Five wavenumbers in the spectrum for model collagen were identified: Amide A (3,406-3,421 cm^-1), amide B (2,916-2,940 cm^-1), amide I (1,639-1,640 cm^-1), amide II (1,539-1,570 cm^-1), and amide III (1,234-1,250 cm^-1).

• 한국식품영양과학회지
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• 제27권2호
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• pp.305-312
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• 1998

Normal tensile strength in collagen fibrils is due to intermolecular and intramolecular crosslinks which are known to be altered in aging. Pyridinoline, a mature crosslink which is stable and nonreducible, is derived from two hydroxyallysine and one hydroxylysine residues of collagen fibrils. The excess formation of pyridinoline in collagen is associated with making the tissue stiffer, less soluble and less digestible by enzymes. Lysyl oxidase is the enzyme that initiates the biosynthesis or crosslinks in collagen by catalyzing the oxidative deamination of the lysyl and hydroxylysyl residues in these molecules, and its activity is inhibited by $\beta$-aminopropionitrile(BAPN). Our previous work demonstrated that the pyridinoline content of bone collagen significantly was increased during incubation for 5 weeks at 37$^{\circ}C$ invitro, but it was diecrased by the addition of ascorbic acdi(AsA). In this study, we clarified the specific action of AsA in aging process in vitro enzymatic reaction.

• Asian-Australasian Journal of Animal Sciences
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• 제8권6호
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• pp.577-582
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• 1995

Sixty ram lambs, weighting 23.5 kg, were randomly assigned in a $2{\times}3$ factorial arrangement of two dietary energy (high; 11.7 and low; 9.0 MJ ME/kg DM) and three levels of poultry offal meal supplementation (0, 5 and 10%). Lambs were fed ad libitum for 120-day before slaughter. At slaughter, half the lambs in each dietary treatment group were randomly selected for electrical stimulation of their undressed carcasses. The M. Biceps femoris pH and temperatures were monitored at 1, 3, 5, 8 and 24 h postmortem. At 24 h postmortem, the M. biceps femoris was removed from the fight side of each carcass and steaks were obtained for determination of Warner-Bratzler shear force, collagen content and collagen solubility. The results showed that temperature and pH values during the 24-h postmortem were consistently higher (p < .01) and lover (p < .01), respectively, for M. biceps femoris from lambs fed high energy diets than for those fed on low energy diets. Muscles from high energy fed lambs had lower (p < .01) shear force values and higher (p < .01) percent soluble collagen than for low energy fed lambs; total collagen content was not significantly influenced by dietary energy level. Increased the level of poultry offal meal supplementation in the diet to 10% was associated with concomitant increases (p < .01) in muscle tenderness and percent soluble collagen. Electrical stimulation (ES) of carcasses resulted in a lower shear force values for the M. biceps femoris than in non-stimulated carcasses (Non-ES); total collagen content and percent soluble collagen were not significantly affected by ES treatment.

• 대한치과의사협회지
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• 제56권12호
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• pp.667-685
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• 2018

Objectives: Aim of this study was to evaluate bone regenerative efficacy of a chemically cross-linked porcine collagen membrane (CM) when used in combination with highly soluble biphasic calcium phosphate (BCP). Materials and methods: Physiochemical properties of the experimental collagen membrane were analyzed. Four circumferential defects with diameter of 8 mm were created in each calvarium of New Zealand white rabbits (n = 10). Defects were randomly allocated to one of following 4 groups: 1) BCP-CM (BCP (20% hydroxyapatite/80% ${\beta}$-tricalcium phosphate) covered with the prepared collagen membrane), 2) BCP (only BCP used), 3) CM (only the prepared collagen membrane used), and 4) C (control; only blood clot). After 2 weeks (n = 5) and 8 weeks (n = 5), histologic and histomorphometric analyses were performed. Results: The experimental collagen membrane exhibited dense and compact structure, relatively high tensile strength and lower degradability. Histologic analyses revealed that new bone increased rapidly at 2 weeks, while defect was preserved at 8 weeks. Histomorphometric analyses revealed that the new bone areas increased in the BCP-grafted groups over 8 weeks, with BCP-CM exhibiting greater total augmented area than that of BCP group both at 2 weeks ($27.12{\pm}3.99$ versus $21.97{\pm}2.27mm^2$) and 8 weeks ($25.75{\pm}1.82$ versus $22.48{\pm}1.10mm^2$) (P < 0.05). Conclusions: The experimental collagen membrane successfully preserved localized defect for 8 weeks despite early rapid resorption of BCP. Within the study limitations, combined use of the chemically cross-linked porcine collagen membrane and highly soluble BCP aided localized bone regeneration.

• Fisheries and Aquatic Sciences
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• 제21권4호
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• pp.7.1-7.8
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• 2018

In this study, we isolated and characterized the acid-soluble skin collagen of Pacific bluefin tuna (PBT, Thunnus orientalis). The PBT skin collagen was composed of two ${\alpha}$ chains (${\alpha}1$ and ${\alpha}2$) and one ${\beta}$ chain. The denaturation temperature of PBT collagen was low although it was rich in proline and hydroxyproline. The primary structure of PBT skin collagen was almost identical to that of calf and salmon skin collagen; however, it differed with respect to the epitope recognition of the antibody against salmon type I collagen. These results suggest that the primary structure of skin collagen was highly conserved among animal species, although partial sequences that included the epitope structure differed among collagens.

• 한국식품저장유통학회지
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• 제16권3호
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• pp.419-426
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• 2009

상어 collagens(SC)(ASSC: 산가용성 껍질 collagen, ASMC: 산가용성 육 collagen, PSSC: pepsin 가용성 껍질 collagen, PSMC: pepsin 가용성 육 collagen)의 항산화성, 항균성, tyrosinase 및 elstase 저해활성을 표품(시판 marine collagen)과 비교하였다. SC($1{\sim}5\;mg/mL$)의 전자공여능은 $14.91{\sim}17.21%$로 표품의 $4.82{\sim}5.48%$에 비하여 $3.0{\sim}3.6$배가 높았다. SC($5{\sim}80\;mg/mL$)의 SOD활성은 4.67${\sim}37.28%$로 STMC 보다 $1.9{\sim}5.9$배가 높았다. SC의 S. aureus와 S. enteritidis에 대한 최소저해농도(MIC)는 $5{\mu}g$/disc로 표품의 $200{\mu}g$/disc보다 현저하게 낮았다. E. coli에 대한 MIC는 ASSC 및 ASMC에서는 $200{\mu}g$/disc인 반면 PSSC 및 PSMC는 $100{\mu}g$/disc이었으며 표품에서는 항균활성이 없었다. S. aureus에 대한 항균력은 PSMC가, S. enteritidis에 대한 항균력은 ASMC가, E. coli에 대한 항균력은 PSMC가 가장 높았다. SC($3{\sim}5\;mg/mL$)의 tyrosinase 저해활성은 $58.95{\sim}98.16%$로 표품의 $17.67{\sim}26.25%$보다 $3.34{\sim}3.74$배가 높았다. SC의 elastase 저해활성은 농도가 0.5 mg/mL에서 1 mg/mL으로 높아짐에 따라 비례적으로 증가하였고 1 mg/mL에서의 활성도는 $53.33{\sim}80.00%$로 STMC의 50.67% 보다 높았으며 PSSC에서 가장 높은 저해활성을 나타내었다. 산 및 pepsin 가용성의 모든 상어 collagen은 STMC에 비하여 $1.1{\sim}4.0$배의 높은 활성을 나타내었다. 이상의 결과 상어 collagens은 시판 marine collagen보다 항산화성, 항균성, tyrosinase 및 elastase 저해활성이 우수하여 새로운 기능성 소재로서의 활용성이 기대된다.