• Journal of Life Science
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• v.16 no.7 s.80
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• pp.1219-1224
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• 2006

Osteoporosis is one of the major health problem affecting postmenopausal women. Estrogen deficiency results in an increase in bone turnover, lead to bone resorption and an increase risk of fracture. The aim of this study was to evaluate the effects of Capsosiphon fulvecense extract (SCF) on the collagen content of the connective tissues and alkaline phosphatase activity of serum in ovariectomized estrogen-deficient rats. Three groups were surgically ovariectomized (OVX). The fourth group was sham operated. Sprague-Dawley female rats were randomly assigned to the following groups : sham-operated rats (Sham), ovariectomized control rats (OVX-control), ovariectomized rats supplemented with CsF at 50mg/kg body wt (OVX-CSF50) and ovariectomized rats supplemented with CsF at 200mg/kg body wt (OVX-CSF200). The Capsosiphon fulvecense extracts were orally administrated at 1mL per day. The ovariectomy caused a decreasing in the levels of collagen content in bone, cartilage, skin and lung tissues. However CSF groups, supplementation with Capsosiphon fulvecense extract, were increased the level of collagen content in bone, cartilage, skin and lung tissues than OVX-control group. Alkaline phosphatase activity also were increased and calcium levels were decreased than OVX-control on serum. These results suggest that Capsosiphon fulvecense supplementation prevents postmenopausal bone loss, thus it may be used possibly to improve the quality of life in menopausal women.

• Food Science of Animal Resources
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• v.35 no.4
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• pp.431-440
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• 2015

Chicken bone is not adequately utilized despite its high nutritional value and protein content. Although not a common raw material, chicken bone can be used in many different ways besides manufacturing of collagen products. In this study, a multi-step procedure was optimized to isolate chicken bone collagen for higher yield and quality for manufacture of collagen products. The chemical composition of chicken bone was 2.9% nitrogen corresponding to about 15.6% protein, 9.5% fat, 14.7% mineral and 57.5% moisture. The lowest amount of protein loss was aimed along with the separation of the highest amount of visible impurities, non-collagen proteins, minerals and fats. Treatments under optimum conditions removed 57.1% of fats and 87.5% of minerals with respect to their initial concentrations. Meanwhile, 18.6% of protein and 14.9% of hydroxyproline were lost, suggesting that a selective separation of non-collagen components and isolation of collagen were achieved. A significant part of impurities were selectively removed and over 80% of the original collagen was preserved during the treatments.

• Asian-Australasian Journal of Animal Sciences
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• v.19 no.7
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• pp.1059-1064
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• 2006

Six muscles were seamed out randomly from Hanwoo carcasses (n = 12) of each quality grade (quality grades 1, 2 and 3). Samples were analysed for their total and soluble collagen contents, IMCT (intramuscular connective tissue) and Warner-Bratzler shear force (WBSF). Simple correlation (n = 21) was determined for WBSF among major muscles. For LT (longissimus thoracis), total collagen content was significantly higher (p<0.05) for quality grade 3 than those for quality grades 1 and 2. For semitendinosus (ST), semimembranosus (SM), psoas major (PM) and serratus ventralis (SV), total collagen content of quality grade 1 was lowest (p<0.05) of all quality grades. IMCT shear force for gluteus medius (GM) decreased (p<0.05) with better quality grade, and those for other muscles, with the exception of GM, were higher (p<0.05) for quality grade 3 than for quality grades 1 and 2. WBSF values showed GM and LT to be decreased (p<0.05) with better quality grade, and PM to be higher (p<0.05) for quality grade 3 than those for quality grades 1 and 2. SM, ST and SV from quality grade 1 had lower (p<0.05) WBSF value than those from quality grades 2 and 3. Total collagen content of ST was highest (p<0.05) of all muscles, whereas that of PM was lowest (p<0.05). Soluble collagen contents of LT and SV from quality grades 1 and 2 were, in general, higher (p<0.05) than other muscles, but that of SM was lowest (p<0.05). ST and SM had higher (p<0.05) WBSF values for three quality grades when compared to other muscles, whereas PM was lowest (p<0.05). LT had the strongest simple correlation with SV (r = 0.78) and GM (r = 0.77), and SM had the strongest correlation with ST (r = 0.73) and LT (r = 0.73). Also, PM had the strongest correlation with SV (r = 0.62).

• 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.

• Food Science of Animal Resources
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• v.39 no.2
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• pp.345-353
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• 2019

Various commercial collagen mixtures aimed at improving the quality of meat products are available, but the optimal composition is unclear. This study aimed to compare the functional properties, including physicochemical characteristics and lipid oxidative stability, of loin ham marinated with three commercial collagen mixtures sold as food additives. The addition of collagen mixtures led to significant increases in the moisture content, water holding capacity (WHC), cooking yield, and instrumental tenderness, regardless of the type of collagen mixture. In particular, meat samples containing collagen mixture C showed the highest (p<0.05) WHC and tenderness among all groups. Furthermore, collagen mixture B induced increases (p<0.05) in pH values in both raw and cooked samples. The $a^*$ values of samples with collagen mixtures were lower (p<0.05) than those of samples without collagen mixtures. All collagen mixtures effectively improved oxidative stability during 7 days of storage at $4^{\circ}C$. The samples containing collagen mixture B had the lowest lipid oxidation (p<0.05) among groups. These results indicated that collagen mixture C could be used in injection brine to enhance the quality characteristics of meat products, particularly the WHC and tenderness. Collagen mixture A could be used for meat products with high fat contents based on its ability to improve lipid oxidative stability during long-term storage.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.41 no.6
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• pp.427-434
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• 2008

Processing of collagen from yellowfin tuna (Thunnus albacares) abdominal skins was optimized by response surface methodology and central composite design. The values of independent variables at optimal conditions were NaOH concentration: 0.5 N, NaOH treatment time: 36.2 hr, pepsin concentration: 1:4.9 ratio (0.245%, w/v), and digestion time: 48.1 hr, respectively. The collagen content estimated under optimal conditions was 33.1%, and the actual experimental collagen content was 32.3%. Physicochemical properties of collagen from yellowfin tuna abdominal skin were investigated by amino acids analysis, SDS-PAGE, FT-IR, viscosity and denaturation temperature. Amino acids content of the collagen was 21.0%. SDS-PAGE pattern of the collagen showed two different $\alpha$-chain (${\alpha}_1$- and ${\alpha}_2$- chain), $\beta$-component and $\gamma$-component. The spectrum of FT-IR of the collagen showed wavenumber at 3,434, 1,650, 1,542 and $1,235\;cm^{-1}$ representing the regions of amide A, I, II and III, respectively. Relative viscosity of the collagen decreased continuously on heating up to $32^{\circ}C$, and the rate of decrease was retarded in the temperature range of $35-50^{\circ}C$. Denaturation temperature (Td) of the collagen solution (0.06%, w/v) was $31^{\circ}C$ and was lower than calf skin collagen ($35^{\circ}C$).

• Journal of Life Science
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• v.15 no.6 s.73
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• pp.1022-1027
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• 2005

The aim of this study was to evaluate effects of mulberry cultivars extracts on the collagen content of the connective tissues in ovariectomized rats. From day 2 until day 37 after ovariectomy, Sprague-Dawley female rats were randomly assigned to the following groups : sham-operated rats (Sham), ovariectomized control rats (OVX-control), and ovariectomized rats supplemented with $80\%$ ethyl alcohol extracts from various kinds of Tajikistan mulberry, Korea mulberry and China mulberry at 200 mg/kg bw/day, respectively. The mulberry extracts were orally administrated at 1 mL per day. The OVX rats were significantly heavier than the sham-operated rats were at all time points, but supplementation with the mulberry extracts tended to gain weight less than OVX-control did. The ovariectomy caused a decreasing in the levels of collagen content in bone and cartilage tissues. However, supplementation with mulberry extracts prevented the decrease in the collagen level in bone and cartilage tissues. Therefore, it may be used to possibly improve the quality of life in menopausal women.

• Journal of the East Asian Society of Dietary Life
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• v.23 no.6
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• pp.760-767
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• 2013

This study investigated the quality of noodles containing different amounts of collagen powder. Noodles were prepared at ratios of 1, 3, 5 and 7% collagen power based on flour weight. The water binding capacity of the collagen powder was higher than that of flour. The rate of weight increase and volume increase of the noodles as well as the pH and turbidity of the soups were significantly increased with increasing amounts of collagen powder. The noodles showed decreased L and a values, and increased b values with increasing collagen powder in the flour composite. Hardness, springiness and chewiness of cooked noodles increased significantly with the increase in collagen powder content. cohesiveness and brittleness decreased with increasing amounts of added collagen powder. DPPH radical scavenging activity was improved significantly the addition of the collagen powder. Finally sensory evaluation results indicated that the noodles containing 1, 3% collagen powder had higher quality as compared to the other samples. Overall the results suggest that collagen powder is effective for improving the appearance and texture of noodles.

• Food Science and Biotechnology
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• v.16 no.4
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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.

• Journal of Periodontal and Implant Science
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• v.5 no.1
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• pp.14.2-14.2
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• 1975