• Korean journal of food and cookery science
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• v.16 no.4
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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.

• Culinary science and hospitality research
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• v.8 no.1
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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.

• Food Science of Animal Resources
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• v.41 no.4
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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.

• Journal of the Korean Applied Science and Technology
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• v.26 no.4
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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.

• Journal of the Korean Society of Food Science and Nutrition
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• v.26 no.3
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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.

• Journal of Life Science
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• v.18 no.11
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• pp.1578-1583
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• 2008

The purpose of this study was to investigate the effects of sea tangle (ST) extracts on formation of collagen and collagen cross-link in ovariectomized rats. From day 3 until 42 after the ovariectomy, Sprague-Dawley female rats were randomly assigned to the following groups: sham-operated rats(Sham), ovariectomized control rats (OVX-control), ovariectomized rats supplemented with ST at 50 mg/kg bw/day (OVX-ST50), 200 mg/kg bw/day (OVX-ST200). The ethanol extraxcr of ST was orally administrated at 1 ml/day. The change of collagen content was investigated in bone, cartilage and skin of ovariectomized rats. Effects of ST extract on the amount of collagen was examined by measuring the hydroxyproline, which is a specific amino acid existing in collagen. The ovariectomy resulted in a decrease in the levels of collagen content in bone and cartilage tissues. However, the supplementation with the sea tangle extract prevented the decrease in the collagen level in bone and cartilage tissues. Pyridinoline is pyridinium cross-link formed in the mature form of collagen from lysine and hydroxylysine residues. Although the pyridinoline content in bone collagen declined after ovariectomy, it was recovered to a normal level of Sham group by the supplementation with the ST extracts. In addition, the deoxypyridinoline content in bone collagen, which was reduced after ovariectomy was enhanced to normal level by the supplementation with the ST extract. These results was consistent with the conclusions based on estrogenic activities of ST.

• Journal of the Korean Society of Food Science and Nutrition
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• v.33 no.2
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• pp.324-330
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• 2004

The purpose of this study was to investigate the effects of Porphyra tenera (PT) extracts on formation of collagen cross-link in ovariectomized rats. From day 3 until 42 after the ovariectomy, Sprague-Dawley female rats were randomly assigned to the following groups : sham-operated rats (Sham), ovariectomized control rats (OVX-control), ovariectomized rats supplemented with PT at 50 mg/kg bw/day (OVX-PT5O), 200 mg/kgbw/day (OVX-PT200). The PT ethanol extracts were orally administrated 1 mL per day. Body weight gain, food intake and food efficiency ratio were significantly different among the groups. The change of collagen content was studied in lung, bone, cartilage and skin of ovariectomized rats. The effects of PT extracts on the amount of collagen were examined by measuring the hydroxyproline, which is a specific amino acid existing in collagen. Pyridinoline is pyridinium cross-link formed in the mature form of collagen from lysine and hydroxylysine residues. Pyridinoline content was analyzed by HPLC. Pyridinoline content in bone collagen was decreased by ovariectomy but supplementation with the PT extracts was similarly increased to Sham. These results suggest that the PT supplementation could decrease bone loss in postmenopausal women.

• Journal of Life Science
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• v.17 no.7 s.87
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• pp.931-936
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• 2007

The aim of this study was to evaluate the effects of Codium Fragile(CF) extract on the collagen content and collagen cross-link content of the connective tissues, alkaline phosphatase activity and calcium levels of serum in ovariectomized estrogen-deficient rats. Three groups were surgically ovariectomized. The fourth group was sham operated. Sprague-Dawley female rats were randomly assigned to the following groups : sham-oper-ated rats(Sham), ovariectomized control rats (OVX-CON), ovariectomized rats supplemented with CF at 50 mg/kg body wt and 200 mg/kg body wt, respectively The CF were orally administrated at 1mLa day. The ovariectomy caused a decreasing in collagen content in bone, cartilage, skin and lung tissues. However CF groups, supplementation with Codium Fragile extract, increased in collagen contentin bone and cartilage tissues than OVX-CON group. Fyridinoline content in cartilage collagen was de-creased by ovariectomy but supplementation with the CF extracts was similarly increased to Sham. Alkaline phosphatase activity on serum of CF groups decreased than OVX-CON group. These results suggest that CF supplementation prevents post-menopausal bone loss, thus it may be used possibly to improve the quality of life in menopausal women.

• Journal of Animal Science and Technology
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• v.65 no.3
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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.

• The Journal of the Korean dental association
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• v.13 no.6
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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.