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
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 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.
文摘利用酸溶法和酶溶法分离纯化绿鳍马面鲀(Navodon septentrionalis)鱼皮酸溶性胶原蛋白(ASC)和酶溶性胶原蛋白(PSC),并对所得的ASC和PSC的氨基酸组成、亚基组成、红外光谱(FTIR)、黏度和热变性温度,以及溶解度等性质进行系统分析。研究结果表明:马面鲀鱼皮酸溶性胶原蛋白(ASC)和酶溶性胶原蛋白(PSC)的得率分别为0.87%±0.15%和9.52%±0.41%(按鱼皮干重计算)。ASC和PSC中含有的主要氨基酸为甘氨酸(Gly),含量分别为323.3残基/1000残基和321.7残基/1000残基;二者中所含的亚氨基酸含量分别为191.1/1000残基和183.4/1000残基。氨基酸组成分析、SDS-PAGE和FTIR证实马面鲀鱼皮酸溶性胶原蛋白(ASC)为I型胶原蛋白,且其SDS-PAGE图中的亚基组成(α1-肽链和α2-肽链)、氨基酸序列,以及胶原蛋白构型与PSC明显不同。ASC和PSC的热变性温度(Td)分别为21.5℃和18.9℃,显著低于哺乳动物来源的胶原蛋白。ASC和PSC的最大溶解度出现在p H 2—3时,当Na Cl的浓度低于2%时,二者的溶解度就开始急剧下降。此外,冻干的胶原蛋白显示出疏松多孔的超微结构。综上,相对于哺乳动物类胶原蛋白,马面鲀鱼皮ASC和PSC的亚氨基酸含量和热变性温度较低,结构稳定性差,易于降解,可作为胶原蛋白肽的制备原料进行开发利用。
