Ovine bones are the major by-products after slaughtered. The present study was conducted to extract and characterize acid soluble collagens （ASC） and pepsin soluble collagens （PSC） from ovine bones （Ujumuqin shee...Ovine bones are the major by-products after slaughtered. The present study was conducted to extract and characterize acid soluble collagens （ASC） and pepsin soluble collagens （PSC） from ovine bones （Ujumuqin sheep）. Ovine bones collagen were identified by sodium dodecyl sulfate-polyacrylamide gel electrophoresis （SDS-PAGE） and liquid chromatography-tan- dem mass spectrometry （LC-MS/MS） as type I collagen. The results of Fourier transform infrared （FTIR） spectra analysis testified the existence of triple superhelical structure in both ASC and PSC, showing pepsin did not disrupt the triple helical structure of ovine bones collagen. Glycine, accounting for one-third of total amino acids, was the major amino acid for ovine bones collagen. Higher imino acid content was responsible for higher thermal denaturation temperature of ovine bones collagen compared to fish collagens. The isoelectric point of ASC was lower than PSC due to the higher content of acidic amino acids. Therefore, this study provides the potential reference for collagen extraction and application of ovine bones by-procduct.展开更多
采用Osborne分级提取法,分离玉米清蛋白、球蛋白、醇溶蛋白和谷蛋白,测定4种蛋白的氨基酸组成、亚基分子量、蛋白变性温度和微观结构。结果表明,清蛋白赖氨酸含量最高,为5.581 g/100 g,醇溶蛋白和谷蛋白含有较多谷氨酸和亮氨酸。SDS-PAG...采用Osborne分级提取法,分离玉米清蛋白、球蛋白、醇溶蛋白和谷蛋白,测定4种蛋白的氨基酸组成、亚基分子量、蛋白变性温度和微观结构。结果表明,清蛋白赖氨酸含量最高,为5.581 g/100 g,醇溶蛋白和谷蛋白含有较多谷氨酸和亮氨酸。SDS-PAGE图中清蛋白有7条谱带,分子量范围在20~80 k Da,球蛋白有4条谱带,分子量范围在20~70 k Da,醇溶蛋白的分子量分布在两个区域,即14~25 k Da和30~50 k Da,谷蛋白分子量分布在30~50 k Da。清蛋白、球蛋白、醇溶蛋白和谷蛋白热变性温度分别为95.96℃,78.85℃,99.53℃和104.33℃。扫描电镜观测发现清蛋白呈薄片状,表面平整光滑;球蛋白呈现蜂窝状,表面孔洞均匀微小;醇溶蛋白呈大小不一球状,表面有凹陷;谷蛋白呈现鳞片状,表面孔洞大小不一。展开更多
Acid-soluble collagen was extracted from the skins of surf smelt and characterized. The yield of collagen was high about 24.0% on a dry weight basis. By SDS-polyacrylamide gel electrophoresis and CM-Toyopearl 650 M co...Acid-soluble collagen was extracted from the skins of surf smelt and characterized. The yield of collagen was high about 24.0% on a dry weight basis. By SDS-polyacrylamide gel electrophoresis and CM-Toyopearl 650 M column chromatography, this collagen is a heterotrimer with a chain composition of α1α2α3. The denaturation temperature was 32.5℃, about 4.5℃ lower than that from porcine skin. Attenuated total reflectance-fourier transform infrared analysis showed that the percentage of secondary structural components in this collagen were 11% α-helix, 34% β-sheet, 19% β-turn, and 21% others. It suggests that the triple helical structure is present in the acid-soluble collagen from the skins of the surf smelt in comparison to that from the skin of porcine.展开更多
Pepsin-soluble collagen was prepared from bullfrog skin and partially characterized. This study revealed interesting differences, such as molecular weight, amino acid composition, denaturation temperature (Td), in the...Pepsin-soluble collagen was prepared from bullfrog skin and partially characterized. This study revealed interesting differences, such as molecular weight, amino acid composition, denaturation temperature (Td), in the frog skin collagen when compared to the known vertebrate collagens. This study gives hints that bullfrog skin can be a potential, safe alternative source of collagen from cattle for use in various fields.展开更多
基金funded by the emarked fund for China Agriculture Research System (CARS-39)the National Agricultural Science and Technology Innovation Program
文摘Ovine bones are the major by-products after slaughtered. The present study was conducted to extract and characterize acid soluble collagens （ASC） and pepsin soluble collagens （PSC） from ovine bones （Ujumuqin sheep）. Ovine bones collagen were identified by sodium dodecyl sulfate-polyacrylamide gel electrophoresis （SDS-PAGE） and liquid chromatography-tan- dem mass spectrometry （LC-MS/MS） as type I collagen. The results of Fourier transform infrared （FTIR） spectra analysis testified the existence of triple superhelical structure in both ASC and PSC, showing pepsin did not disrupt the triple helical structure of ovine bones collagen. Glycine, accounting for one-third of total amino acids, was the major amino acid for ovine bones collagen. Higher imino acid content was responsible for higher thermal denaturation temperature of ovine bones collagen compared to fish collagens. The isoelectric point of ASC was lower than PSC due to the higher content of acidic amino acids. Therefore, this study provides the potential reference for collagen extraction and application of ovine bones by-procduct.
文摘采用Osborne分级提取法,分离玉米清蛋白、球蛋白、醇溶蛋白和谷蛋白,测定4种蛋白的氨基酸组成、亚基分子量、蛋白变性温度和微观结构。结果表明,清蛋白赖氨酸含量最高,为5.581 g/100 g,醇溶蛋白和谷蛋白含有较多谷氨酸和亮氨酸。SDS-PAGE图中清蛋白有7条谱带,分子量范围在20~80 k Da,球蛋白有4条谱带,分子量范围在20~70 k Da,醇溶蛋白的分子量分布在两个区域,即14~25 k Da和30~50 k Da,谷蛋白分子量分布在30~50 k Da。清蛋白、球蛋白、醇溶蛋白和谷蛋白热变性温度分别为95.96℃,78.85℃,99.53℃和104.33℃。扫描电镜观测发现清蛋白呈薄片状,表面平整光滑;球蛋白呈现蜂窝状,表面孔洞均匀微小;醇溶蛋白呈大小不一球状,表面有凹陷;谷蛋白呈现鳞片状,表面孔洞大小不一。
文摘Acid-soluble collagen was extracted from the skins of surf smelt and characterized. The yield of collagen was high about 24.0% on a dry weight basis. By SDS-polyacrylamide gel electrophoresis and CM-Toyopearl 650 M column chromatography, this collagen is a heterotrimer with a chain composition of α1α2α3. The denaturation temperature was 32.5℃, about 4.5℃ lower than that from porcine skin. Attenuated total reflectance-fourier transform infrared analysis showed that the percentage of secondary structural components in this collagen were 11% α-helix, 34% β-sheet, 19% β-turn, and 21% others. It suggests that the triple helical structure is present in the acid-soluble collagen from the skins of the surf smelt in comparison to that from the skin of porcine.
文摘Pepsin-soluble collagen was prepared from bullfrog skin and partially characterized. This study revealed interesting differences, such as molecular weight, amino acid composition, denaturation temperature (Td), in the frog skin collagen when compared to the known vertebrate collagens. This study gives hints that bullfrog skin can be a potential, safe alternative source of collagen from cattle for use in various fields.
