By using the wastes fish skin of sturgeon processed as a raw material, a macromolecule biomaterial of collagen was extracted. Acid-soluble collagen(ASC) and pepsin-soluble collagen(PSC) were successfully isolated from...By using the wastes fish skin of sturgeon processed as a raw material, a macromolecule biomaterial of collagen was extracted. Acid-soluble collagen(ASC) and pepsin-soluble collagen(PSC) were successfully isolated from the skin of hybrid sturgeon with two extraction methods. The yields of ASC and PSC based on the wet weight of skin were 5.73 ± 0.11% and 10.26 ± 0.39%, respectively. The denaturation and melting points of ASC(26.83 ℃ and 110.49 ℃) and PSC(26.54 ℃ and 102.99 ℃) were assessed by Circular dichroism(CD) and Differential scanning calorimetry(DSC). ASC and PSC appeared to be dense sheet-like film linked by random-coiled filaments under scanning electron microscopy(SEM). Sodium dodecyl sulfate-polyacrylamide gel electrophoresis(SDS-PAGE) and Fourier transform infrared spectroscopy(FTIR) confirmed that both the ASC and PSC were Type I collagen and maintained a complete triple helix structure. These results indicated that both ASC and PSC possessed good biological activity and could be widely used in medical biomaterials and other fields.展开更多
The biochemical composition of the turbot skin was investigated. The moisture level of the skin was found to be 51.4%. Based on dry matter content, there were relatively high protein(82.1%) and lipid(13.1%) concentrat...The biochemical composition of the turbot skin was investigated. The moisture level of the skin was found to be 51.4%. Based on dry matter content, there were relatively high protein(82.1%) and lipid(13.1%) concentrations in the turbot skin. Mineral element analysis revealed that the turbot skin had high Ca content(2069.0 mg kg^-1), and the concentrations of toxic heavy metals Hg and Pb were less than 0.005 mg kg^-1, which indicates that the turbot skin is a safe resource for collagen production. The sodium dodecyl sulfate-polyacrylamide gel electrophoresis(SDS-PAGE) analysis showed that acid-soluble collagen(ASC) extracted from the turbot skin was type-I collagen. The imino acid content of the ASC was 241.6 per 1000 amino acids, which suggests a relatively high denaturation temperature. The Fourier transform infrared(FTIR) spectra of ASC reflected a highly stable structure, and the measured denaturation temperature of ASC was 29.5℃, which is higher than those from many temperate fishes. ASC was the most soluble at pH 4.0, and when the pH values were below or above 4.0, the solubility decreased rapidly. The ASC exhibited a relatively high solubility when NaCl concentration was lower than 2%. These results show that turbo skin can be employed as a source for producing collagen with high quality.展开更多
Acid-soluble collagen (ASC) and pepsin-solubilized collagen (PSC) were prepared from the waste freshwater carp fish scales. The results of SDS-PAGE showed that purified collagens were composed of at least two differen...Acid-soluble collagen (ASC) and pepsin-solubilized collagen (PSC) were prepared from the waste freshwater carp fish scales. The results of SDS-PAGE showed that purified collagens were composed of at least two different chains which were in accordance with the type I collagen with α chain composition of (α1)2α2. Compared with the carp fish ordinary muscle type I collagen , porcine dermis type I collagen and other seawater fish collagens, freshwater carp fish scales collagen contained relative high half-cystine (Cys-s), but lower denaturation temperature(Td) than the porcine dermis type I collagen. These collagens had evident absorption at 230 nm by UV-Vis spectra. The spectrum X-ray diffraction showed that the collagen remained single-helix and tri-helix configuration with the minimum values of the repeat spacings (d) of about 4.48 ? and 11.87 ?. Therefore, to make more effective use of limited-resources, carp fish scales can be a potential resource for the extraction of type I collagen or gelatin.展开更多
Acid-soluble collagen(ASC) and pepsin-soluble collagen(PSC) from the spine(ASC-SP and PSC-SP) and skull(ASC-SK and PSC-SK) of the skipjack tuna, Katsuwonus pelamis, were successfully isolated and characterized. The yi...Acid-soluble collagen(ASC) and pepsin-soluble collagen(PSC) from the spine(ASC-SP and PSC-SP) and skull(ASC-SK and PSC-SK) of the skipjack tuna, Katsuwonus pelamis, were successfully isolated and characterized. The yields of ASC-SP, PSC-SP, ASC-SK and PSC-SK were(2.47 ± 0.39)%,(5.62 ± 0.82)%,(3.57 ± 0.40)%, and(6.71 ± 0.81)%, respectively, on the basis of dry weight. The four collagens contained Gly(330.2-339.1 residues/1 000 residues) as the major amino acid, and their imino acid contents were between 168.8 and 178.2 residues/1 000 residues. Amino acid composition, SDS-PAGE, and FTIR investigations confirmed that ASC-SP and ASC-SK were mainly composed of type I collagen, and had higher contents of high-molecular weight cross-links than those of PSC-SK and PSC-SP. The FTIR investigation also certified all the collagens had triple helical structure. The denaturation temperatures of ASC-SK, PSC-SK, ASC-SP, and PSC-SP were 17.8, 16.6, 17.6, and 16.5 °C, respectively. All isolated collagens were soluble at acidic pH(1-5) and lost their solubilities when the NaCl concentration was above 2%(W/V). The isolated collagens from the spines and skulls of skipjack tuna could serve as an alternative source of collagens for further application in food, cosmetic, biomedical, and pharmaceutical industries.展开更多
研究了以酸法提取鲤鱼鳞胶原蛋白过程中温度、时间、乙酸浓度的影响,并以SAS对影响因素进行了回归分析,得到了鲤鱼鳞胶原蛋白提取的最佳条件,温度18℃、提取时间38 h、乙酸浓度为1.3 m ol/L,在提取之前,采用Na2CO3处理对胶原蛋白提取有...研究了以酸法提取鲤鱼鳞胶原蛋白过程中温度、时间、乙酸浓度的影响,并以SAS对影响因素进行了回归分析,得到了鲤鱼鳞胶原蛋白提取的最佳条件,温度18℃、提取时间38 h、乙酸浓度为1.3 m ol/L,在提取之前,采用Na2CO3处理对胶原蛋白提取有较大的提高。为淡水鱼综合加工利用提供理论依据。展开更多
基金Funded by the National Natural Science Foundation of China(No.51173143)
文摘By using the wastes fish skin of sturgeon processed as a raw material, a macromolecule biomaterial of collagen was extracted. Acid-soluble collagen(ASC) and pepsin-soluble collagen(PSC) were successfully isolated from the skin of hybrid sturgeon with two extraction methods. The yields of ASC and PSC based on the wet weight of skin were 5.73 ± 0.11% and 10.26 ± 0.39%, respectively. The denaturation and melting points of ASC(26.83 ℃ and 110.49 ℃) and PSC(26.54 ℃ and 102.99 ℃) were assessed by Circular dichroism(CD) and Differential scanning calorimetry(DSC). ASC and PSC appeared to be dense sheet-like film linked by random-coiled filaments under scanning electron microscopy(SEM). Sodium dodecyl sulfate-polyacrylamide gel electrophoresis(SDS-PAGE) and Fourier transform infrared spectroscopy(FTIR) confirmed that both the ASC and PSC were Type I collagen and maintained a complete triple helix structure. These results indicated that both ASC and PSC possessed good biological activity and could be widely used in medical biomaterials and other fields.
基金supported by the Major Special Science and Technology Projects in Shandong Province (No. 2015 ZDZX05003)the Fundamental Research Funds for the Central Universities (Nos. 201564018, 201513048)
文摘The biochemical composition of the turbot skin was investigated. The moisture level of the skin was found to be 51.4%. Based on dry matter content, there were relatively high protein(82.1%) and lipid(13.1%) concentrations in the turbot skin. Mineral element analysis revealed that the turbot skin had high Ca content(2069.0 mg kg^-1), and the concentrations of toxic heavy metals Hg and Pb were less than 0.005 mg kg^-1, which indicates that the turbot skin is a safe resource for collagen production. The sodium dodecyl sulfate-polyacrylamide gel electrophoresis(SDS-PAGE) analysis showed that acid-soluble collagen(ASC) extracted from the turbot skin was type-I collagen. The imino acid content of the ASC was 241.6 per 1000 amino acids, which suggests a relatively high denaturation temperature. The Fourier transform infrared(FTIR) spectra of ASC reflected a highly stable structure, and the measured denaturation temperature of ASC was 29.5℃, which is higher than those from many temperate fishes. ASC was the most soluble at pH 4.0, and when the pH values were below or above 4.0, the solubility decreased rapidly. The ASC exhibited a relatively high solubility when NaCl concentration was lower than 2%. These results show that turbo skin can be employed as a source for producing collagen with high quality.
文摘Acid-soluble collagen (ASC) and pepsin-solubilized collagen (PSC) were prepared from the waste freshwater carp fish scales. The results of SDS-PAGE showed that purified collagens were composed of at least two different chains which were in accordance with the type I collagen with α chain composition of (α1)2α2. Compared with the carp fish ordinary muscle type I collagen , porcine dermis type I collagen and other seawater fish collagens, freshwater carp fish scales collagen contained relative high half-cystine (Cys-s), but lower denaturation temperature(Td) than the porcine dermis type I collagen. These collagens had evident absorption at 230 nm by UV-Vis spectra. The spectrum X-ray diffraction showed that the collagen remained single-helix and tri-helix configuration with the minimum values of the repeat spacings (d) of about 4.48 ? and 11.87 ?. Therefore, to make more effective use of limited-resources, carp fish scales can be a potential resource for the extraction of type I collagen or gelatin.
基金supported by the National Natural Science Foundation of China(No.31001109)the Public Projects of Zhejiang Province(No.2014C33034)the Special Program for the Science and Technology Plan of Zhejiang Province(Nos.2009C03017-2,2011C02003)
文摘Acid-soluble collagen(ASC) and pepsin-soluble collagen(PSC) from the spine(ASC-SP and PSC-SP) and skull(ASC-SK and PSC-SK) of the skipjack tuna, Katsuwonus pelamis, were successfully isolated and characterized. The yields of ASC-SP, PSC-SP, ASC-SK and PSC-SK were(2.47 ± 0.39)%,(5.62 ± 0.82)%,(3.57 ± 0.40)%, and(6.71 ± 0.81)%, respectively, on the basis of dry weight. The four collagens contained Gly(330.2-339.1 residues/1 000 residues) as the major amino acid, and their imino acid contents were between 168.8 and 178.2 residues/1 000 residues. Amino acid composition, SDS-PAGE, and FTIR investigations confirmed that ASC-SP and ASC-SK were mainly composed of type I collagen, and had higher contents of high-molecular weight cross-links than those of PSC-SK and PSC-SP. The FTIR investigation also certified all the collagens had triple helical structure. The denaturation temperatures of ASC-SK, PSC-SK, ASC-SP, and PSC-SP were 17.8, 16.6, 17.6, and 16.5 °C, respectively. All isolated collagens were soluble at acidic pH(1-5) and lost their solubilities when the NaCl concentration was above 2%(W/V). The isolated collagens from the spines and skulls of skipjack tuna could serve as an alternative source of collagens for further application in food, cosmetic, biomedical, and pharmaceutical industries.
