• 한국식품조리과학회지
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• 제16권4호
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• pp.352-357
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• 2000

This study was conducted to investigate the effect of the lipid and collagen content and drip volume on the hardness of fish meat. Red sea bream (cultured and wild) and flounder (cultured, cultured with obosan and wild) were used for this study. Textural differences between cultured and wild meats were determined by the measurements of hardness, lipid and collagen content, and drip volume. Lipid content of the dorsal muscle was higher especially in cultured red sea bream (3.32%) than in wild one. Cultured and wild flounder contained lower content of lipid than red sea bream. The content of collagen was higher in cultured flounder fed with obosan (8.37 mg/g muscle) and wild flounder (8.02 mg/g muscle) than others. Drip volume was the highest in cultured flounder fed with obosan (8.67%). The hardness of raw meat was correlated with the contents of lipid (r= -0.7063) and collagen (r= 0.8307), significantly. Cultured fish contained more lipid and less collagen than wild one. So, the hardness of these fish meats was lower than wild one. However, cultured flounder fed with obosan showed no difference in hardness compared with wild one. In the cooked meat, there was no relationship between the hardness of fish meat and the contents of lipid and collagen. But, the drip volume was significantly related with the hardness (r= 0.6870). From these results, the factors contributing the textural difference between wild and cultured fish meat would be the lipid and collagen contents, and two ways to improve the texture of cultured fish meat could be suggested. One is to lower the lipid content by feed control, and the other is to raise the collagen content by inducing more fish movement.

• 한국조리학회지
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• 제8권1호
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• pp.95-105
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• 2002

This study was conducted to present the fundamental data on physicochemical properties of chicken foot collagen by the comparison with those from pork skin, which is present used in the factories as evaluate the usability of chicken foot in the industries of collagen production. Moisture content of chicken foot skin (CFS) was higher than that of pork skin (PS), and crude protein content was higher in PS. Content of other compositions was not different in both samples. At the evaluation of the soaking processing, effective time lapsed for soaking the skin in acid solution (acetic acid of 0.1 M) was about 12 hr for efficient extract ion of collagen, when tested by the changes of pH of the soaking solution and the increase of the weight of skins. L-Hydroxyproline of PS was slightly higher than that of CFS. Collagens were loaded in a SDS-PAGE and compared. Separated pattern of collagen of CFS was very similar to that of PS. Major collagen of CFS might be clarified as type I collagen.

• 한국축산식품학회지
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• 제41권4호
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• pp.674-686
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• 2021

This study aimed to enhance the quality of broiler breast meat by adding pig skin collagen to feed. A total of 50 Ross 308 broilers were classified according to the following feeding regime for two weeks: basal diet (NC), basal diet+0.1% fish collagen (PC), basal diet+0.1% pig skin collagen (T1), basal diet+0.5% pig skin collagen (T2), and basal diet+1.0% pig skin collagen (T3). The moisture content was the highest in the PC group, and the protein content was the lowest in the T1 group (p<0.05). The fat content was higher in the T1 and PC groups, whereas the ash content was higher in the T3 group (p<0.05). Drip loss was the highest in the NC group and the lowest in the T2 group (p<0.05). Lightness was low in groups T2 and T3, redness was low in groups T2 and PC, and yellowness was low in groups T1, T2, and PC (p<0.05). The collagen content of the chicken breast was the highest in the T3 group, and that of the skin was the highest in the T1 group (p<0.05). The texture characteristics of springiness, cohesiveness, chewiness, and hardness were the highest in the T3 group (p<0.05). In conclusion, the supplementation of a broiler diet with pig skin collagen was found to increase the collagen content of the breast meat, indicating the improved quality of the broiler breast meat.

• 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.

• 한국식품영양과학회지
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• 제26권3호
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• pp.501-506
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• 1997

As pyridinoline is one of the predominant cross-lins in a mature collagen, pyridinoline formation may be an essential step during the growth process to obtain normal mechanical strength in collagen fibrils. However, the excess formation of pyridinoline in collagen will probably make the tissue stiffer, less soluble and less digestible by enzymes. We investigated the changes of pyridinoline of bone collagen and the role of ascforbic acid(AsA) on the formation of pyridinoline. The pyridinoline content of bone collagen significantly increased during incubation for 1~5 weeks at 37$^{\circ}C$ in vitro. The addition of AsA decreased pyridinoline to half the amount found in controls with 5 week incubation. When dehydroascorbic acid(DHA) and L-2, 3-diketogulonic acid (DKG), the oxidative products of AsA, were supplemented to bone collagen solution instead of AsA, the content of pyridinoline in bone collagen was about 80% or 70% that of controls, respectively. These results suggest that pyridinoline content decreases by the addition of AsA in vitro. Furthermore, it was shown that AsA in oxidized from also affected the formation of pyridinoline.

• 생명과학회지
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• 제18권11호
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• pp.1578-1583
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• 2008

폐경을 앞둔 여성에게는 폐경을 전후하여 지속되는 골 손실 가속화 등의 문제점을 가지고 있다. 그러므로 본 연구에서는 인위적 폐경을 유발시킨 난소 절제 쥐에서의 골 손실의 유무를 결합조직 중의 collagen 함량 변화를 통하여 그 효과를 검토하였다. 그 결과 생화학적 골 대사 지표인 혈 중 ALP 활성은 난소 절제(OVX-control)로 인하여 증가하는 반면, 난소 절제 후 다시마 추출물 투여(OVX-ST50, OVX-ST200)로 혈중 ALP 활성은 감소하는 경향을 보여 골 흡수를 저하시킬 수 있는 가능성을 나타내었다. 한편 난소 절제 후 collagen 함량이 감소하였으나, 다시마 추출물 투여에 의해 피부조직과 골.연골 조직에서 collagen 함량이 증가하는 경향을 보였고, 특히 OVX-ST200군은 각 조직 모두 OVX-control에 비하여 유의적으로 증가하였다(p<0.05). Collagen의 성숙 가교물질인 pyridinoline 함량 또한 난소 절제 후 골, 연골 조직 중에서 감소하였으나 다시마 추출물을 투여한 군에서 증가하는 경향을 나타내었다. 골에서의 deoxypylidinoline 함량은 난소를 절제하지 않은 Sham군이 OVX-control군에 비해서 유의적으로 높은 값을 나타냈고(p<0.05), 난소 절제 후 다시마 추출물을 농도별로 투여한 군(OVX-ST50 및 OVX-ST200)에서 유의 적으로 높은 값을 나타내어(p<0.05), 난소 절제 시 합성이 감소되는 deoxypyridinoline 생성량을증가시켰다. 에스트로겐 감소로 인한 결합조직 중 collagen 함량 저하가 다시마 추출물 투여에 의해 증가된 본 실험 결과로 미루어 보아 다시마 중의 phytoestrogen이 에스트로겐 유사효과를 나타냄을 알 수 있었다. 이상과 같이 폐경으로 인한 장애를 감소시키기 위하여 에스트로겐의 장기간 복용에 의한 부작용을 다시마 중의 phytoestrogen이 estrogen 대체 작용을 함으로써 그 부작용을 감소시켜 줄 것으로 사료되며, 이들의 구조 및 기전에 대해서는 앞으로 연구가 더 필요 한 것으로 생각된다.

• 한국식품영양과학회지
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• 제33권2호
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• pp.324-330
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• 2004

난소 절제시술 및 폐경으로 인한 여성 호르몬인 estrogen의 감소는 지속되는 골 손실 가속화 등으로 인한 골 질환의 문제점을 가지고 있다. 그러므로 본 연구에서 흰쥐의 난소를 절제하여 인위적인 폐경을 유도하여 골손실의 정도를 결합조직 중의 collagen 함량 및 collagen성숙가교인 pyridinoline함량을 측정하여 그 효과를 검토하였다 난소 절제 후 결합조직 중의 collagen함량은 연골과 피부에서 난소를 절제하지 않은 Sham군에 비하여 낮았으며, 김 추출물 투여군에서 유의적이지는 않으나 높은 경향을 나타내었다. 골 중 collagen성숙가교인 pyrldinoline 함량은 난소절제에 의해 감소하였으나 골에서는 김 추출물 투여에 의해 난소를 절제하지 않은 Sham군과 비슷한 수준으로 증가하였고, 연골에서는 김 추출물 투여에 의해 Sham군과 비슷한 수준으로 감소하는 경향을 나타내어 pyridinoline 생성에 유익한 효과를 나타내었다. 김 추출물이 collagen합성 및 성숙가교인 pyridinoline 생성을 회복시킨 본 실험의 결과로 보아 폐경기여성에게 김 추출물의 섭취는 폐경으로 인한 골손실을 감소시켜 줄 것으로 사료되어지며, 이러한 작용을 나타낸 김의 성분 및 그 기전에 대해서는 앞으로 더 많은 연구가 필요할것으로 생각된다.

• 생명과학회지
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• 제17권7호통권87호
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• pp.931-936
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• 2007

갱년기의 여성에는 여러 폐경 증후들이 나타나는데, 특히 에스트로겐의 감소로 인한 혈중의 지질 조성의 변화 등으로 인한 심혈관계 질환과 골 손실의 증가로 인한 골다공증의 위험성이 높아 이에 대한 예방 및 치료에 대한 연구가 활발히 이루어지고 있다. 따라서 본 연구에서는 쉽게 섭취 할 수 있으며,부작용이 없는 해조류인 청각 추출물을 난소제거술을 통한 갱년기 유도 흰쥐에 투여하여 결합조직 중의 collagen과 pyridinoline함량, 혈 중 ALP활성 변화를 통해 갱년기 장애 질환의 개선효과를 알아보았다. 청각 추출물이 골 노화에 미치는 영향을 실험 한 결과 난소 절제에 의한 골 손실에 의해 결합조직의 collagen 함량이 감소하였으나, 청각 추출물의 투여로 인해 증가하는 경향을 보였다. 따라서 청각 추출물이 에스트로겐 감소로 인해 저하되는 collagen 합성능을 회복 시켜 유익한 효과를 가지는 것으로 추측된다. 또한 골 및 연골조직에서 collagen 성숙가교인 pyridinoline 함량을 HPLC에 의해 측정한 결과, 연골 중 pyridinoline함량은 난소절제에 의해 감소되었으나 청각 추출물 투여로 인해 난소를 절제하지 않은 SHAM군과 비슷한 수준으로 증가하여 pyridinoline 생성에 유익한 효과를 나타내었다. 이상의 결과로부터 갱년기 장애 시 유발되는 골 노화에 청각 추출물이 유효한 효과를 나타낼 것으로 기대된다.

• Journal of Animal Science and Technology
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• 제65권3호
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• pp.511-518
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• 2023

This study examined the association between functional sequence variants (FSVs) of myosin heavy chain 3 (MYH3) genotypes and collagen content in a Landrace and Jeju native pig (JNP) crossbred population. Four muscles (Musculus longissimus dorsi, Musculus semimembranosus, Musculus triceps brachii, and Musculus biceps femoris) were used for the analysis of meat collagen content, and the same animals were genotyped for the FSVs of the MYH3 gene by using PCR-RFLP (polymerase chain reaction-restriction fragment length polymorphism). Three FSVs of MYH3 genotypes were identified and had genotype frequencies of 0.358, 0.551, and 0.091 for QQ, Qq, and qq, respectively. QQ animals for the FSVs of the MYH3 genotypes showed higher collagen content in their M. longissimus dorsi (p < 0.001), M. semimembranosus (p < 0.001), M. triceps brachii (p < 0.001), and M. biceps femoris (p < 0.001) than qq homozygous animals. After the validation of this result in other independent populations, the FSVs of MYH3 genotypes can be a valuable genetic marker for improving collagen content in porcine muscles and can also be applied to increase the amount of collagen for biomedical purposes.

• 대한치과의사협회지
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• 제13권6호
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• pp.563-567
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• 1975

This present investigation was concerned with the content of collagen and minerals of incisor and molar dentin in rats of differednt ages. The results obtained were summarized as follows. 1. There was no remarked change in the content of collagen-hydroxyproline of incisor and molar dentin according to days after delivery. 2. The Ca content in incisor dentin rose from approximately 15.4% of the dry weight in 7 days after delivery to 21.1% in 22 days while that in molar dentin from 17.6% in 7 days to 19.7% in 22 days. 3. The P content in molar dentin rose from 8.5% in 7 days after delivery to 11.65% in 22 days. while in incisor rose from 8.05% in 7 days to 11.85 in 22 day after delivery.