• 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.28 no.6
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• pp.1332-1338
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• 1999

Intermolecular collagen cross links stabilize collagen fibrils and are necessary for normal tensile strength in collagen fibrils. Once the fibrils are aligned, hydroxyllysine, hydroxylysine derived aldehyde modified enzymatically, reacts with hydroxylysine to form the dehydrodihydroxylysinonorleucine (DHLNL), an immature crosslink. Pyridinoline, one of matured cross links is presumably formed nonenzymatically through condensation of DHLNL and hydroxylysine residue. It is widely distributed in hard connective tissues such as cartilage, bone and tendon. L ascorbic acid(AsA) is well known to be required for the enzymatic hydroxylation of proline and lysine in collagen fibrils. The purpose of this study is to clarify the role of AsA on the biosynthesis of DHLNL in vitro. We examined the effect of AsA on the formation of hydroxylysine and DHLNL in collagen. Pyridinoline and DHLNL were measured as a function of time. The contents of DHLNL was increased, reached maximum within 2 hr and was held until 24 hr, then it decreased slowly. On the contrary, pyridinoline increased gradually after 24 hr and continued to increase for 2 weeks. Moreover, the contents of DHLNL remarkably decreased at 60 min after incubation, the contents of DHLNL was decreased by addition of AsA or dehydroascorbic acid(DHA). These results suggest that the supplementation of AsA causes decrease in DHLNL formation and pyridinoline formed by nonenzymatic reaction of DHLNL.

• 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.

• Journal of Environmental Science International
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• v.22 no.11
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• pp.1465-1471
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• 2013

To develop the protein materials by the reutilization of dead flatfish from fish farms in Jeju island, the physicochemical characteristics and the functional activities of collagen peptide extracts were investigated. Flatfish skin collagen peptide (FSCP) and flatfish protein hydrolysate (FPH) were manufactured from dead flatfish. The differences of pH, moisture and fat contents between FSCP and FPH were not significant, fat contents were analyzed less than 0.3%, and trans-fat, saturated fat and cholesterol were not detected in both samples. Protein contents of FSCP and FPH showed about 92% and 95%, respectively. In the analysis of amino acids, glycine and hydroxy proline content in FSCP was 24.22% and 6.15%, respectively, showed a typical characteristics of the collagen protein, but essential amino acids contents such as threonine, valine, methionine, isoleusine, leusine and phenylalanine were relatively higher than those of FPH. Average molecular weight of FSCP was measured as 1,102 which was almost equal value with that of tuna collagen peptide. The antioxidant activities and functional properties showed high but did not show significant difference between two samples.

• Journal of Animal Science and Technology
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• v.65 no.2
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• pp.311-323
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• 2023

Beef consumers valued meat quality traits such as texture, tenderness, juiciness, flavor, and meat color that determining consumers' purchasing decision. Most research on meat quality has focused on marbling, a key characteristic related to meat eating quality. However, other important traits such as meat texture, tenderness, and color have not much studied in cattle. Among these traits, meat tenderness and texture of cattle are among the most important factors affecting quality evaluation of consumers. Collagen is the main component of connective tissues.It greatly affects meat tenderness. The objective of this study was to determine significant variants and candidate genes associated with collagen contents trait (total collagen) through genome-wide association studies (GWAS). Phenotypic and genomic data from 135 Hanwoo were used. The BLUPF90 family program and GRAMMAR method for GWAS were applied in this study. A total of 73 potential single nucleotide polymorphisms (SNPs) showed significant associations with collagen content. They were located in or near 108 candidate genes. TMEM135 and ME3 genes were identified to have the most significant SNPs associated with collagen contents trait. Data indicated that these genes were related to collagen. Biological processes and pathways for the prediction of biological functions of candidate genes were confirmed. We found that candidate genes were involved in positive regulation of CREB transcription factor activity and actin cytoskeleton related to tenderness and texture of beef. Three genes (CRTC3, MYO1C and MYLK4) belonging to these biological functions were related to tenderness. These results provide a basis for improving genomic characteristics of Hanwoo for the production of tender beef. Furthermore, they could be used they could be used as an index to select desired traits for consumers.

• 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.

• The Korean Journal of Food And Nutrition
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• v.28 no.4
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• pp.710-716
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• 2015

This experiment was carried out to find the quality characteristics of yanggaeng added antioxidant rich collagen powder in the color, sugar contents, texture, radical scavenging activity and electronic nose detected flavor. L value and a value kept decreased as the more collagen powder was added in the yanggaeng while b value was increased significantly at the same time. Sugar contents was increased significantly from $43^{\circ}$Brix in the control to 48% in the 10% treatment (p<0.05). Hardness in the 10% treatment of collagen powder increased biggest among the treatments but springiness decreased when hardness increased. And adhesiveness, cohesiveness, gumminess and chewiness were also increased with more the collagen powder in the treatments, therefore 10% treatment showed biggest result significantly. Radical scavenging activity kept increased with higher addition of collagen powder and it resulted 60% of radical scavenging activity in the 10% treatment. In the flavor test under electronic nose experiment, 10% of collagen powder treatment was believed it flavored most for it was found in the furthest from the AIR location. Control was found also in the nearest from the AIR, which meant it has least flavor than any other treatment. Also 2.5% and 5% of collagen powder added treatments showed little differences of flavor from control, which meant 5% of treatment was believed idea condition in the treatments. With the above experimental results, 5% of collagen powder treatment in the yanggaeng manufacturing was chosed as the best mixture ratio in the test.

• 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).

• Journal of the Korean Society of Clothing and Textiles
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• v.23 no.6
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• pp.800-808
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• 1999

The demand for PU coated synthetic leather is increasing as a high fashion material. But it has some faults of water vapor permeability surface tacky property and static electricity. Therefore the purpose of this study was the produce of PU coated fabric added collagen with hydrophilic property and soft touch. In the PU coated fabric water vapor permeability water vaper absorption and frictional electronic voltage were investigated surface bending and compression properties were also examined by the use of KES-FB System. The followings were the results of this study. 1. There was no Cr in the collagen so that Cr was not treated in the collagen. 2. The surface and cross sectional layer of PU coated fabric with collagen were highly developed by micro porous structure. 3. The water vapor permeability of PU coated fabric was increased as collagen concentration increased. 4. The water vapor absorption of PU coated fabric was increased as collagen concentration increased. 5. The frictional electronic voltage of PU coated fabric was decreased in accordance with the increase of collagen concentration. Especially it effectively decreased by the use of only 5% collagen concentration. 6,. The bending and compression properties of PU coated fabric were increased in accordance with the increase of collagen concentration so that it became stiff. 7. The Value of MIU, SMD was decreased in accordance with the increase of collagen concentration so that the PU coated fabric became smooth.

• Asian-Australasian Journal of Animal Sciences
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• v.14 no.11
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• pp.1638-1644
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• 2001

The objective of this research was to evaluate alternative treatments for the best extraction condition for collagen from chicken feet. Various properties such as chemical composition, amino acid, pH, swelling percentage, yield and pure collagen, collagen loss, color (Hunter L, a and b) and electrophoresis of collagen from chicken feet treated by 5% acids (acetic acid, citric acid. hydrochloric acid and lactic acid) and soaking times (12, 24, 36 and 48 h) were evaluated. The crude protein, fat, ash and moisture contents of chicken feet was 17.42, 12.04, 5.98 and 62.05%, respectively. Amino acid composition of collagen from chicken feet indicated that the protein of collagen was markedly hydrolized by the hydrochloric acid treatment. The result of electrophoresis also supported this phenomenon. Both the swelling percentage of lactic acid and citric acid treatments were significantly higher than that of acetic acid and HC1 treatment. The pH of the acid treatments ranged from 2.43-3.62. According to the result of yield, pure collagen and loss of collagen, the best condition of extracting collagen from chicken feet was soaked in 5% lactic acid for 36 h. However, a brighter yellow color of collagen from all treatments was observed with a longer soaking time.