共查询到18条相似文献，搜索用时 250 毫秒
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鲈鱼骨酸溶性和酶溶性胶原的性质比较 总被引：1，自引：0，他引：1
《河北渔业》2015,(10)
以鲈鱼骨为原料提取得到酸溶性胶原(ASC)和酶溶性胶原(PSC),对ASC和PSC的性质进行比较。粘度测定结果表明,ASC的变性温度25~30℃,PSC的变性温度为30~35℃;电泳结果表明,ASC和PSC都属于Ⅰ型胶原且纯度比较高;氨基酸分析结果显示,羟脯氨酸和脯氨酸含量ASC均低于PSC,氨基酸检测结果与粘度检测结果相一致。 相似文献
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交联方法对草鱼皮胶原蛋白海绵生物学性能的影响 总被引：1，自引：0，他引：1
为探讨不同交联方法对草鱼皮胶原蛋白海绵材料性能的影响,实验以草鱼鱼皮为原料,提取、纯化胶原蛋白并制备胶原海绵材料.在此基础上,分别用紫外交联、热交联、戊二醛交联以及EDC/NHS交联方法处理胶原海绵,通过测定材料的交联度、热变性温度、拉伸强度和体外抗酶降解性能,比较了不同方法的交联效果.结果发现,提取所得的草鱼皮胶原蛋白为典型的Ⅰ型胶原;经不同方法交联处理后,海绵材料交联度依次为戊二醛(72.0％) ＞EDC/NHS(32.5％)＞热交联(29.9％)＞紫外交联(15.6％);与对照胶原材料相比,戊二醛处理后,胶原材料的热变性峰值温度(67.4℃)、最大拉伸强度(125.6 kPa)和体外抗酶降解性能均有显著提升(P＜0.05);EDC/NHS处理后,胶原材料的热变性焓显著提升(6.86 J/g),同时材料的拉伸强度(98.6 kPa)和体外抗酶降解性能也得到适度增加(P＜0.05).紫外交联和热交联对草鱼皮胶原材料性能的改善作用比较有限,并可能导致胶原分子的部分变性.红外光谱的分析结果表明,戊二醛处理可导致草鱼皮胶原三螺旋分子内产生新的共价键交联从而使材料性能改善,而EDC/NHS处理主要导致胶原分子间产生新的氢键交联并可提高胶原材料的稳定性.研究表明,戊二醛和EDC/NHS交联能有效提高胶原海绵材料的性能,而热交联和紫外交联对材料性能的改善作用非常有限. 相似文献
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鲢鱼鳞片胶原蛋白的提取 总被引：1，自引：0，他引：1
利用酸和酶提取法,从淡水鲢鱼鳞片中提取酸溶性和酶溶性胶原蛋白.经紫外光谱分析显示,所提取的胶原蛋白与I型胶原蛋白标准品接近.氨基酸组成分析表明,ASC和PSC是典型的Ⅰ型胶原蛋白. 相似文献
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皱纹盘鲍酶促溶性胶原蛋白的性质研究及抗体制备 总被引：1，自引：1，他引：0
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。 相似文献
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鲤鱼鱼鳞胶原蛋白ASC与PSC的比较 总被引：1，自引：0，他引：1
以鲤鱼鱼鳞为原料,研究了酸法和酶法提取的鱼鳞胶原蛋白ASC和PSC的异同.经过SDS-凝胶电泳和氨基酸分析可以看出,2种蛋白在分子构型、氨基酸组成等方面的差异并不明显,经过蛋白酶K有限酶解后的图谱证明了这一点.但从差热分析,以及蛋白质受热的分解变化来看,二者之间在热稳定性方面存在一定的差异.推测差距产生的原因与蛋白质制备过程中,胃蛋白酶的作用有关,胶原蛋白两端的非螺旋区域受到酶的作用而分解,非螺旋区域对三螺旋的稳定性起着重要作用,非螺旋区域的分解大大降低了PSC对热的耐受性. 相似文献
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为了探究养殖花鳗鲡(Anguilla marmorata)鱼皮胶原蛋白的特性,利用胃蛋白酶结合酸抽提法提取花鳗鲡鱼皮胶原蛋白,SDS-PAGE电泳法展示胶原蛋白的电泳图谱,氨基酸分析仪测定胶原蛋白的氨基酸组成,分析胶原蛋白分子的紫外和红外光谱特征,用浊度实验和流变黏弹性实验探究胶原蛋白分子的体外自组装动力学特性。结果显示,花鳗鲡鱼皮胶原蛋白属于Ⅰ型胶原蛋白,氨基酸组成中甘氨酸、脯氨酸与羟脯氨酸三者的比值为8∶3∶2,胶原蛋白分子的最大紫外吸收峰出现在222.6 nm处,热变性温度28℃,红外光谱图和扫描电镜扫描结果图均表明经胃蛋白酶及酸溶得到的胶原蛋白保持了胶原原有的结构。胶原蛋白分子的体外自组装动力学曲线是含有迟滞期、成长期和稳定期的三阶段曲线。以上结果表明花鳗鲡鱼皮胶原具有接近淡水鱼皮胶原的特征。 相似文献
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仿刺参胶原蛋白的提取及理化性质 总被引：9，自引：0，他引：9
对仿刺参（Stichopus japonicus）胶原蛋白的提取及理化性质进行了研究。结果表明，低温提取可得到胃蛋白酶促溶且去除端肽(telopeptide)的酸溶性胶原蛋白（PSC）。紫外-可见扫描测得PSC的最大吸收峰位于220 nm；氨基酸分析发现，在1 000个总氨基酸残基中，甘氨酸为329个，羟脯氨酸为66个，羟脯氨酸与脯氨酸之比为0.69，酪氨酸、苯丙氨酸及组氨酸的含量较低，可能不含胱氨酸，这些特性均符合Ⅰ型胶原的特征。差示量热扫描法（DSC）测定仿刺参PSC的热稳定性温度（Ts）为57 ℃，低于牛皮Ⅰ型胶原5 ℃；苯酚-硫酸及次甲基蓝法测得PSC的总糖及粘多糖含量分别为0.61％及0.48％；经DEAE52纯化后，可得到除去粘多糖的蛋白纯品。SDS-PAGE显示，本研究所提取的仿刺参PSC不含杂蛋白，主要成分为胶原β及α链，含少量γ链；其中α链类似于脊椎动物Ⅰ型胶原α1链，PSC分子组成为（α1）3。 相似文献
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多棘海盘车体壁胶原蛋白的研究 总被引：1，自引：0，他引：1
采用两种不同的方法从海盘车体壁中提取出酸溶性胶原蛋白（ＡＳＣ）和胃蛋白酶促溶的胶原蛋白（ＰＳＣ）,得率分别为１０．９０％、６１．４３％。将ＡＳＣ、ＰＳＣ的氨基酸组成、理化性质与脊椎动物及其它无脊椎动物胶原蛋白进行比较,结果表明,ＡＳＣ、ＰＳＣ是典型的胶原蛋白。在此基础上对ＡＳＣ、ＰＳＣ进行了ＳＤＳ－ＰＡＧＥ电泳,进一步表明制品的纯度较高,并且它们在分子大小、构型及性质上没有显著差异。 相似文献
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Acid-solubilized collagen (ASC) and pepsin-solubilized collagen (PSC) from golden pompano skins were extracted and characterized. The molecular weight of ASC was about 130 kDa for α1 and 115 kDa for α2, which were slightly higher than those of PSC. Similar amino acid composition and Fourier transform infrared (FTIR) spectra were observed in both collagens, but slight differences were found in the peptide maps of collagen digested by V8 protease and trypsin. The denaturation temperatures (Tds) of ASC and PSC calculated from the reduced viscosity were 31.8 and 30.0°C, while the transition temperature (Tm) of ASC and PSC analyzed by DSC were 33.0 and 32.0°C, respectively. ASC has a lag phase, a growth phase, and a plateau phase in the turbidity–time curve, while PSC does not have similar phenomenon. It was found that the fibril gel of ASC could be formed at 25°C, leading to improved thermal stability. 相似文献
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Wanticha Savedboworn Soottawat Benjakul Sittichoke Sinthusamran Hideki Kishimura 《Journal Of Aquatic Food Product Technology》2017,26(3):248-257
Acid soluble collagen (ASC) and pepsin soluble collagen (PSC) were isolated from rohu skin with the yield of 64.2 and 6.8% (dry weight basis), respectively. Both collagens had glycine as the major amino acid with imino acid content of 196–202 residues/1,000 residues and were characterized as type I collagen with molecular composition of (α1)2α2-heterotrimer. Fourier transform infrared spectra of both collagens were similar, with no shift in wavenumber of all amide bands. The Tmax value of ASC and PSC was 36.40 and 35.48°C, respectively. The zero surface net charge of ASC and PSC was found at pH 5.9 and 5.3, respectively. 相似文献
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Chodsana Sriket Wonnop Visessanguan Hideki Kishimura Kenji Hara Asami Yoshida 《Journal Of Aquatic Food Product Technology》2013,22(2):137-145
Chemical compositions and thermal properties of cultured freshwater prawn meat (FPM) were studied. FPM contained 83.2% protein (dry basis), 62.7% of which was myofibrillar protein. Pepsin-soluble collagen (PSC) and insoluble collagen (ISC) contents were 0.63 and 0.32%, respectively. Both collagens were similar to type V collagen from porcine placenta. Glutamic acid/glutamine, arginine, aspartic acid/?asparagine, and lysine were abundant amino acids in FPM. Glycine, proline, hydroxyproline, and aspartic acid/?asparagine were predominant in both collagens. FPM exhibited thermal transition temperatures (Tmax) of 48.3 and 64.7°C, whereas Tmax of PSC and ISC were 43.0 and 46.0°C, respectively. Textural changes in FPM during post-mortem storage on ice are plausibly dependent upon its compositional and thermal properties. 相似文献
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Isolation and characterization of collagens from the skin of giant grouper (Epinephelus lanceolatus)
Cheng-Hong Hsieh Chyuan-Yuan Shiau Yi-Cheng Su Yi-Han Liu 《Journal Of Aquatic Food Product Technology》2013,22(1):93-104
ABSTRACTAcid-solubilized collagen (ASC) and pepsin-solubilized collagen (PSC) were extracted from the skin of giant groupers (Epinephelus lanceolatus) with yields of 39.51 and 19.12%, respectively. ASC and PSC consisted of two different α chains (α1 and α2) and were characterized to be type I collagen with no disulfide bond. The imino acid contents of the ASC and PSC from giant grouper skin were 189 and 181 per 1,000 residues, respectively. The maximum endothermic temperatures (Tmax) of ASC and PSC measured by differential scanning calorimetry (DSC) were 31.71 and 31.33°C, respectively. The denaturation temperatures of ASC and PSC measured by viscometry were 29.84 and 29.05°C, respectively. The maximum solubility in 0.5 M acetic acid was observed at pH 5 and pH 6 for ASC and PSC, respectively. A sharp decrease in solubility was observed for both ASC and PSC in the presence of NaCl above 3% (w/v). 相似文献
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Masashi Ando Yoko Nakagishi Keiko Yoshida Masashi Nakao Takayuki Nakagawa Yasuo Makinodan Yasuyuki Tsukamasa Ken-Ichi Kawasaki 《Fisheries Science》2006,72(5):1104-1108
Pyridinoline (Pyr), one of the mature crosslinks of collagen, was determined in muscular collagen of three species of fish.
The amounts of muscular Pyr in red sea bream, yellowtail, and tiger puffer were 3.4, 8.8, and 50.3 mmol/mol collagen, respectively,
indicating that the Pyr concentration in muscular collagen differs greatly among fish species. The Pyr concentration in tiger
puffer muscular collagen was the greatest, but it was only one-fourth that in rabbit muscle. As in mammalian skin collagen,
Pyr was not detected in skin collagen of red sea bream and yellowtail. However, tiger puffer skin contained Pyr (3.75 mmol/mol
collagen). The presence of Pyr would have a relationship to some features of tiger puffer skin, such as mechanical strength
and thickness. Pyr concentrations in acid-soluble collagen (ASC), pepsin-solubilized collagen (PSC), and insoluble collagen
(ISC) in muscles of three species of fish were determined. Pyr was found in ISC > PSC > ASC, from the highest to the lowest
concentration, and the concentration in ISC was 45–200 times that in ASC. Therefore, Pyr crosslinks that are formed between
collagen molecules would have a close relationship to collagen solubility. 相似文献
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Carmen G. Sotelo María Blanco Comesaña Patricia Ramos Ariza Ricardo I. Pérez-Martín 《Journal Of Aquatic Food Product Technology》2013,22(3):388-399
ABSTRACTSkin collagen of six discarded fish species was analyzed and compared. Acid soluble collagen (ASC) was extracted; a characteristic sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) profile for type I collagen was obtained, except for Chimaera mostrosa. Contents of collagen calculated from HPro (31.85% average) were higher than those determined from ASC extracts (17.75% average), with Galeus spp. being the species with the higher percentage. Amino acid analysis revealed the typical composition of collagen, with very few differences among species. Specific profiles were obtained after protease digestion. Denaturation temperature of ASC correlated well with imino and hydroxyproline contents.Results demonstrate the feasibility of using the obtained collagens in different industrial applications. 相似文献
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The changes in collagen content and its solubility in sea bream muscle were studied for variable storage times following the death of the fish, and these variables were related to the evolution of physical parameters important for consumer acceptance: firmness and water-holding capacity (WHC). The results show that the collagen content in muscle diminished slightly over storage time and that this variable was directly related to firmness but inversely related to the water-holding capacity. With regard to collagen solubility, a decline was detected in acid-soluble collagen (ASC) in the first few post mortem hours, perhaps related to the end of rigor mortis that occurs at these stages. Pepsin-soluble collagen (PSC) increased, while insoluble collagen (ISC) decreased from 96 h, coinciding with a loss of firmness. This softening can be explained as a result of specific collagenases acting on the insoluble fraction of the collagen. 相似文献