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
Characteristics and antioxidant activities of pepsin-soluble collagen （PSC） from yellow goosefish （Lophius litulon） skins were investigated. PSC was characterized as a type I collagen, and its imino acid content w...Characteristics and antioxidant activities of pepsin-soluble collagen （PSC） from yellow goosefish （Lophius litulon） skins were investigated. PSC was characterized as a type I collagen, and its imino acid content was 193 residues/1 000 residues. PSC＇s denaturation temperature was -17.56℃ and Fourier transform infrared spectra confirmed the presence of triple helices. Solubility analysis showed good solubility at acidic pH （1-6） or low NaCl concentrations （≤2%）. PSC showed scavenging activity against hydroxyl radicals and superoxide anions in a concentration-dependent manner. Furthermore, PSC could protect D-galactose-induced skin aging by significantly controlling malondialdehyde formation and improving the activity of superoxide dismutase, glutathione peroxidase, catalase, glutathione, and hydroxyproline. PSC may be a promising antioxidant in appropriate applications.展开更多
To make more effective use of underutilized resources, pepsin-solubilized collagen (PSC) was successfully extracted from the skin of black carp (Mylopharyngdon piceus) with a yield of 45.7% based on dry weight. The PS...To make more effective use of underutilized resources, pepsin-solubilized collagen (PSC) was successfully extracted from the skin of black carp (Mylopharyngdon piceus) with a yield of 45.7% based on dry weight. The PSC comprising two identical α1-chains and one α2-chain with no disulfide bond was characterized as type I, and it contained 195 imino acid residues vs. 1000 amino acid residues. The collagen showed an absorption edge around 218 nm, which was lower than the maximum absorption wavelength of other PSC. The denaturation temperature of PSC was 25.6°C, which was lower than that of porcine collagen by approximately 11°C. The isoelectric point (pI) was estimated to be 8.23, and the collagen was soluble at an acidic pH as well as below 40 g/L NaCl. It is thought that the high yield and stability of PSC from the skin of black carp warrant its application as a new source of collagen for industrial purposes.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
针对加工副产物鲍鱼外套膜利用率低的现象,对鲍鱼腹足和外套膜胶原蛋白相关性质进行比较研究,以期为鲍鱼的综合加工提供一定的理论依据。本研究以皱纹盘鲍为原料分别提取得到腹足酶促溶性胶原蛋白(pepsin-soluble collagen of abalone a...针对加工副产物鲍鱼外套膜利用率低的现象,对鲍鱼腹足和外套膜胶原蛋白相关性质进行比较研究,以期为鲍鱼的综合加工提供一定的理论依据。本研究以皱纹盘鲍为原料分别提取得到腹足酶促溶性胶原蛋白(pepsin-soluble collagen of abalone adductor,PSC1)和外套膜酶促溶性胶原蛋白(pepsin-soluble collagen of abalone mantle,PSC2),对PSC1和PSC2相关特性进行比较分析,并利用PSC1制备得到兔抗鲍鱼胶原蛋白多克隆抗体。SDS-PAGE显示,PSC1和PSC2分子组成均为(α1)3,且α1的分子量为140 ku,与水产无脊椎动物Ⅰ型胶原蛋白特征相似。对PSC1进行肽指纹图谱分析,获得6个肽段、含75个氨基酸残基,与盘鲍螺的胶原蛋白前肽α链和欧洲鲍螺的纤维状胶原一致性分别达100%和88%,证明纯化的PSC1为胶原蛋白。氨基酸组成分析表明,PSC1和PSC2的组成基本一致,但脯氨酸和羟脯氨酸含量均低于牛酸溶性胶原蛋白。圆二色谱分析结果显示,PSC1和PSC2溶液均在220和197 nm分别有一正、负峰,具有典型胶原蛋白三股螺旋结构特征。FTIR光谱分析结果提示PSC1和PSC2具有相似的三螺旋结构。利用兔抗皱纹盘鲍PSC1多克隆抗体对皱纹盘鲍、尼罗罗非鱼、鲤和仿刺参胶原蛋白进行免疫印迹分析发现,该抗体只与皱纹盘鲍PSC1和PSC2的α、β和γ链产生反应,表明该抗体具有良好的特异性。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 International S&T Cooperation Program of China(No.2015DFA30980)the Zhejiang Provincial Natural Science Foundation of China(No.LQ14C170001)the Special Program for the Science and Technology Plan of Zhejiang Province(No.2011C02003)
文摘Characteristics and antioxidant activities of pepsin-soluble collagen （PSC） from yellow goosefish （Lophius litulon） skins were investigated. PSC was characterized as a type I collagen, and its imino acid content was 193 residues/1 000 residues. PSC＇s denaturation temperature was -17.56℃ and Fourier transform infrared spectra confirmed the presence of triple helices. Solubility analysis showed good solubility at acidic pH （1-6） or low NaCl concentrations （≤2%）. PSC showed scavenging activity against hydroxyl radicals and superoxide anions in a concentration-dependent manner. Furthermore, PSC could protect D-galactose-induced skin aging by significantly controlling malondialdehyde formation and improving the activity of superoxide dismutase, glutathione peroxidase, catalase, glutathione, and hydroxyproline. PSC may be a promising antioxidant in appropriate applications.
文摘To make more effective use of underutilized resources, pepsin-solubilized collagen (PSC) was successfully extracted from the skin of black carp (Mylopharyngdon piceus) with a yield of 45.7% based on dry weight. The PSC comprising two identical α1-chains and one α2-chain with no disulfide bond was characterized as type I, and it contained 195 imino acid residues vs. 1000 amino acid residues. The collagen showed an absorption edge around 218 nm, which was lower than the maximum absorption wavelength of other PSC. The denaturation temperature of PSC was 25.6°C, which was lower than that of porcine collagen by approximately 11°C. The isoelectric point (pI) was estimated to be 8.23, and the collagen was soluble at an acidic pH as well as below 40 g/L NaCl. It is thought that the high yield and stability of PSC from the skin of black carp warrant its application as a new source of collagen for industrial purposes.
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.
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。
