• Korean journal of food and cookery science
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• v.28 no.6
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• pp.711-719
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• 2012

The collagens from squid (Todarodes pacificus) skin and Alaska pollack (Theragra chalcogramma) skin were extracted and their physicochemical properties were investigated. The yield was improved with the increase of NaOH concentration and was increased Neutrase than Alcalase in enzymatic hydrolysates. Protein and collagen contents from Alaska pollack skin were 38.3~62.7% and 13.1~28.9%, respectively. All enzymatic hydrolysates also showed high antioxidant activities as NaOH concentration decrease. Composition of their amino acids was mainly glycine and proline. The spectrum of FT-IR of the collagen showed wavenumber at $1,631cm^{-1}$, $1,549cm^{-1}$, $1,234cm^{-1}$ and $3,322cm^{-1}$ representing the regions of amide I, amide II, amide III and amide A, respectively. The decomposition temperature for the collagen was in the range of $300^{\circ}C$ and showed relatively good enough for their thermal stabilities.

• Journal of the Korean Applied Science and Technology
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• v.29 no.2
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• pp.295-301
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• 2012

The collagen-liposomes were prepared with hydrogenated phosphatidylcholine and by solvent injection method for maximum protection and stable absorption of collagen into the body. Cholesterol was added to phosphatidylcholine to increase the stability of liposome membrane. The mixture was dissolved in ethanol and propylene glycol and PBS Buffer was used to Stabilize ions. The properties collagen-liposome were analyzed by DLS, SEM and POM.

• Applied Biological Chemistry
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• v.34 no.3
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• pp.265-272
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• 1991

In order to utilize fish skin effectively, the acid-soluble collagen was extracted from the skin of filefish, Novoden modestrus, and the filefish skin collagen(FSG) was modified by papain-catalyzed incorporation of L-leucine alkyl ester(Leu-OCn). The functional properties of an enzymatically modified collagen were measured. The $FSC-Leu-OC_8$ showed very good emulsifiability and foamability and was suitable for use as a low-fat content proteinaceous surfactant.

• The Korean Journal of Vision Science
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• v.20 no.4
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• pp.561-568
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• 2018

Purpose : The size and regular array of the collagen fibers in the corneal stroma have very close correlation with transparency. Simulation was carried out to investigate the change of light transmittance according to the array structure and collagen fiber layer thickness. Methods : The collagen fibers in corneal stroma were arranged in regular hexagonal, hexagonal, square and random shapes with OptiFDTD simulation software, and the light transmittance was analyzed. In square array, the light transmittance according to the density change was confirmed by when the number of collagen fibers in the simulation space was the same and the light transmittance was examined when the number and density of collagen fibers were changed. Results : When the number of collagen fibers is the same, the density becomes smaller and the thickness of the fibrous layer becomes thicker in order of arrangement of square, regular hexagonal, random and hexagonal. As a result of measuring the light transmittance by changing the array structure, the light transmittance measured at the detector at the same position was almost similar regardless of the array structure. In the detectors D0, D1, D2 and D3, the maximum transmittance is shown in square, hexagonal and square, regular hexagonal and regular hexagonal array structure, and the minimum transmittance is hexagonal, random, hexagonal and square, and square array structure. However, the difference between the maximum transmittance and the minimum transmittance was almost the same within 1%. When the number of collagen fibers was the same, the light transmittance of the rectangular array structure decreased with increasing fiber layer thickness. And as the thickness increased, the light transmittance decreased more when the number of collagen fibers decreased. Conclusion : Even though the collagen array structure changed, the light transmittance is almost similar regardless of the arrangement structure. However, as the array structure was changed, the thickness of the collagen fiber layer changed, and as the thickness increased, the light transmittance decreased. In other words, the transparency of the corneal stroma is more closely related to the thickness of the fibrous layer than the array of collagen fibers.

• Bulletin of Food Technology
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• v.14 no.4
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• pp.60-67
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• 2001

현재, 미용식품으로 판매되고 있는 대부분의 제품은 피부를 구성하는 콜라겐과 hyaluronic acid 등이 배합되어 있으며, 이러한 것들은 피부에 윤기를 주는 것을 목적으로 한다. 그러나 이들 성분은 고분자물질이기 때문에 섭취시 고분자물 그 자체로 피부로 이행될 것으로는 생각되지 않는다. 일반적으로 콜라겐이나 hyaluronic acid는 소화효소에 의해 저분자의 아미노산이나 펩타이드, 당질로 분해되고 흡수되어 각 장기나 피부조직에서 콜라겐이나 hyaluronic acid로 재생된다고 알려져 있다. 피부조직에서의 재생은 진피 내의 피부선유아세포에서 일어난다. 따라서, 피부섬유아세포의 작용을 활성화시키는 것이 아름다운 피부를 가지는데 중요하다.

• Korean journal of food and cookery science
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• v.10 no.2
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• pp.111-120
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• 1994

본 실험은 4가지의 다른 무게를 가진 고기(0.1kg,0.5kg, 1kg, 1.5kg)를, 3가지의 다른 출력의 전자파(40%, 60%, 100%)로 조리시 나타나는 조리조건(오븐의 효율성, 대기시간, 대기시 상승온도)과 물리 화학적인변화(수분, 단백질, 지방, vit B$_1$,의 함량, 콜라겐의 용해도, 보수력, texture)를 관찰하였다. 고기의 무게가 증가할수록 전자렌지의 효율성은 낮아졌으며, 단위 무게당 조리시간은 고기의 무게가 증가할수록 길어졌다. 화학적 성분들에 있어서는 지방과 콜라겐의 용해도를 제외하고는 처리구간에 유의적인 차이를 보이지 않았다. 지방과 콜라겐의 용해도는 전자파의 출력차이에 의한 유의적인 차이는 나타나지 않았으나, 고기 무게가 증가할수록 지방의 함량의 증가와 콜라겐의 용해도는 증가하였다. Texture를 측정한 항목들에 대해서는 고기의 무게에 따른 유의적인 차이는 나타나지 않았으나 전자파의 출력에 의한 차이를 나타내었다.

• Korean Journal of Food Science and Technology
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• v.27 no.4
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• pp.571-575
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• 1995

Transition temperature$(T_m)$ and $enthalpy({\Delta}H)$ were examined by means of DSC to obtain basic information on heat stability of skin tissue collagen. From DSC properties of insoluble collagen on hydration time and moisture content, it was found that moisture content had more effect on structural stability of collagen than hydration time. As moisture content increased, $({\Delta}H)$ increased while $(T_m)$ decreased. DSC properties of acetone dried skin on the variation of age and sex showed higher heat stability in case of male rat and heat stability seemed to be connected with age, as $(T_m)$ and $({\Delta}H)$increased with age. Meanwhile, DSC properties of salt soluble collagen showed higher values in female rat than in male rat, and the $(T_m)$ and $({\Delta}H)$ decreased significantly with age in female rat. These results seemed to suggest indirectly that collagen structure varied with age or sex in the same tissue.

• Journal of the Society of Cosmetic Scientists of Korea
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• v.44 no.1
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• pp.23-29
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• 2018

In this study, sequential cross-linked collagen gels were successfully prepared with collagen, which is biomaterial, and acrylamide (AAm), which is a synthetic monomer. The elastic moduli (E) of cross-linked collagen gels were increased from 1.5 to 3.0 kPa by varying of AAm concentrations. In addition, human dermal fibroblasts were encapsulated into the porous pores introduced into the gels, and cell growth and behavior were investigated. Increasing E of the gels led to decreases in cell growth rate, while the cellular glycosaminoglycan (GAG) production level was elevated. Overall, the growth and cellular activity of skin cells were influenced by the extracellular matrix properties of the collagen gels. In conclusion, these results will be highly useful for designing reconstructive skins and various tissue engineering researches.

• Korean Journal of Food Science and Technology
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• v.43 no.4
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• pp.458-463
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• 2011

Recent studies have revealed that collagen peptide (CP) plays a protective role in skin by improving the activity of antioxidants and acts as an inducer of skin regeneration by positive feedback. In this study, we focused on the beneficial effect of reinforcing the CP skin barrier. To evaluate the skin barrier, hairless mice were exposed to UVB irradiation and acetone-treatment, with or without oral administration of CP. The effects on skin appearance, trans-epidermal water loss, epidermal thickness, and cytokine content were measured using bioengineering and histochemical methods. In the CP treated group, the skin had better appearance and less damage than that of the control. Furthermore, in HaCaT cells, the amount of serinepalmytoyl transferase (SPT) mRNA increased by about 1.6-fold after treatment (CP, 100 mg/L), reflecting that CP can induce SPT expression and reinforce the recovery of skin barrier function. These results suggest that CP is not only an anti-wrinkling agent but also a potent candidate as an epidermal moisturizer.

• 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.