鱼鳞胶原蛋白研究

采用酸性和酶提取法从鱼鳞中提取酸溶性和酶促溶性Ⅰ型胶原蛋白，经ＳＤＳ－ＰＡＧＥ电泳显示，所提取的胶原蛋白电泳区带与Ⅰ型标准品相同。氨基酸分析表明，ＡＳＣ和ＰＳＣ是典型的胶原蛋白，热稳定性测定ＡＳＣ的Ｔｄ为３２．３℃，ＰＳＣ的Ｔｄ为２７．８℃。     

闽南_台湾浅滩渔场六种主要中上层鱼类的脂肪酸研究

研究了蓝圆Ｓｈｅｎ、金色小沙丁鱼、颌圆Ｓｈｅｎ、鲐鱼、竹Ｊｉａ鱼、羽鳃鲐肌油中的脂肪酸组成及含量变化。结果表明：鱼油中都含有Ｃ１２－Ｃ２２系列脂肪酸。饱和脂肪酸（ＳＦＡ）占总脂肪酸（ＴＦＡ）的３５．２４％￣３８．６０％，单不饱和脂肪酸（ＭＵＦＡ）占２３．５９％￣３０．０７％，多不饱和脂肪酸（ＰＵＦＡ）占３３．０６％￣４０．３３％，ＥＰＡ占２．３５％￣３．６２％，ＤＨＡ占１７．９５％￣２４．４９％。     

条纹石鮨摄食强度与代谢及能量收支间的关系

设日摄食率为０．４％、１．５％、４．０％三种水平，分别测定条纹石鱼旨Ｍｏｒｏｎｅｓａｘａｔｉｌｉｓ幼鱼的代谢及能量的收支情况。处于饱食（日摄食率４．０％）及维持状态（日摄食率１．５％）下，该鱼代谢率增加的峰值分别于摄食后３ｈ及７ｈ内出现，为静止时代谢水平的２．１０倍和２．４６倍，ＳＤＡ（特殊动力作用）持续时间均为２１ｈ，ＳＤＡ总耗能量分别占摄入能的１３％和３５．８％。条纹石鱼旨在饱食时的转化效率Ｋ（湿重）为２０．８５％。三种摄食水平下条纹石鱼旨的能量收支方程分别为：饱食状态（日摄食率４．０％）时，１００Ｃ＝８．４Ｆ＋７．８Ｕ＋１３．０ＳＤＡ＋３６．９（Ｒｓ＋Ｒａ）＋３３．９Ｇ；维持状态（日摄食率１．５％）时，１００Ｃ＝７．８Ｆ＋４．１Ｕ＋３５．８ＳＤＡ＋５２．３（Ｒｓ＋Ｒａ），其中Ｇ＝０；减重状态（日摄食率０．４％）时，（Ｆ＋Ｕ＋Ｒ）／（Ｃ＋Ｐ１）＝６７．３％，其中Ｃ＋Ｐ１＝１４．４Ｃ＋８５．６Ｐ１，Ｆ＋Ｕ＋Ｒ＝１．８Ｆ＋８．１Ｕ＋５７．４Ｒ。     

聚甘露糖醛酸对中国对虾免疫相关酶活性和溶菌溶血活性的影响

在中国对虾的血清、肌肉和肝胰提取液中有酸性磷酸酶（ＡＣＰ）、碱性磷酸酶（ＡＬＰ）、过氧化物酶（ＰＯＤ），其中，ＡＣＰ和ＡＬＰ在肝脏中的活性最高。采用１．０％的聚甘露糖醛多糖作为免疫药物，对中国对虾进行注射刺激后，发现血清中的溶菌和溶血活性有显著提高；肝胰腺中的ＡＣＰ和ＡＬＰ活性也有明显增加，在７２ｈ，ＡＣＰ活性由对照组的３．２１Ｕ．１００ｍＬ＾－１提高到９．６９Ｕ．１００ｍｌ＾－１，ＡＬＰ活性由４     

生长猪不同赖氨酸/消化能水平日粮饲养效果对比试验报告

生长猪饲喂Ａ、Ｂ、Ｃ ３种日粮，Ａ、Ｂ、Ｃ的消化能均为１２．７ＭＪ／ｋｇ，赖氨酸含量分别为０．７０％、０．７５％、０．８０％，Ａ、Ｂ、Ｃ赖氨酸／消化能比分别为０．５５ｇ／ＭＪ、０．５９ｇ／ＭＪ、０．６３ｇ／ＭＪ。结果表明，饲养４周时，头均增重Ｂ＞Ｃ＞Ａ，Ｄ、Ａ间差异显著（Ｐ＜０．０５），料重比Ａ＞Ｃ＞Ｂ，Ｄ、Ａ间差异显著（Ｐ＞０．０５）；饲养８周时，头均增重Ｂ＞Ｃ＞Ａ，３组间差异不显著（Ｐ＜０．０５），料重比Ａ＞Ｃ＞Ｂ，Ｂ、Ａ间差异显著（Ｐ＜０．０５），３组间每千克增重饲料成本比较Ａ＞Ｃ＞Ｂ，综上所述Ｂ粮为最优。     

褐藻多糖类化合物对卵磷脂氧化的抑制作用

褐藻多糖类化合物在乳化体系中对卵磷脂（ＰＣ）氧化具抑制作用，通过测定卵磷脂氢过氧化物（ＰＣ－ＯＯＨ）含量，确定各化合物的抗氧化能力。结果表明：在自由基引发剂（ＡＡＰＨ）作用下，褐藻多糖类化合物（褐藻胶ＡＬＧ、磺化褐藻胶ＳＡＬＧ、甘糖酯ＰＧＭＳ、藻酸双酯钠ＰＳＳ，５０μｍｏｌ／Ｌ）对ＰＣ氧化的抑制作用均比ＶＣ（６０μｍｏｌ／Ｌ）好，但不如ＶＥ（３０μｍｏｌ／Ｌ）的效果好；抑制顺序是：ＶＥ＞ＳＡＬＧ＞ＰＧＭＳ＞ＰＳＳ＞ＡＬＧ＞ＶＣ。     

盐度对杂交鳢幼鱼生长及血液免疫指标的影响

在３５ｄ的试验周期内,研究了不同盐度（２、４、６、８）对杂交鳢（斑鳢♀×乌鳢♂）幼鱼生长及血液红细胞数量（ＲＢＣ）、白细胞数量（ＷＢＣ）、溶菌酶（ＬＺＭ）含量、超氧化物歧化酶活性（ＳＯＤ）和过氧化氢酶（ＣＡＴ）活性等免疫因子的影响。结果显示,随着盐度的升高,杂交鳢增重率分别为６７．８１％、６８．２６％、７１．１４％、３２．９６％和１４．２６％,存活率分别为１００％、１００％、１００％、１００％和９３．３％。盐度２、４组增重率和对照组差异不显著,盐度６、８组增重率和对照组差异显著（Ｐ＜０．０５）。随着盐度的升高,血液红细胞数量呈下降的趋势,对照组和其他组差异显著（Ｐ＜０．０５）,而白细胞数量先急剧上升后又恢复到对照组水平,盐度６组达到最高。血液中溶菌酶浓度随着盐度变化出现波动,盐度６组达到最高,且与对照组差异显著（Ｐ＜０．０５）,盐度８组溶菌酶浓度有所回降,但仍显著高于对照组（Ｐ＜０．０５）。超氧化物歧化酶活性变化趋势与溶菌酶浓度变化趋势相似,各组超氧化物歧化酶活性均高于对照组且差异显著（Ｐ＜０．０５）。当盐度升至６时,超氧化物歧化酶活力升至最高。过氧化氢酶活性随着盐度的增加逐步升高,盐度８组达到最高,且各组与对照组差异显著（Ｐ＜０．０５）。     

应用Dot_ELISA技术检测草鱼出血病病毒的研究

报道了斑点免疫吸附ＥＬＩＳＡ（Ｄｏｔ－ＥＬＩＳＡ）快速检测草鱼出血病病毒（ＧＣＨＶ）的方法以及对提纯病毒、染毒细胞内病毒和病鱼组织的检测结果，并对该方法的灵敏度与ＳＰＡ－ＣｏＡ和常规ＥＬＩＳＡ法进行了系统的比较。结果表明，Ｄｏｔ－ＥＬＩＳＡ检出ＧＣＨＶ的最低含量为３ｐｇ，该灵敏度比ＳＰＡ－ＣｏＡ和常规ＥＬＩＳＡ法分别提高１０倍和２０倍，而且快速易行，是目前检测ＧＣＨＶ最为有效的方法，并可在草鱼出血病临床诊断和病毒疫苗质量鉴定等方面得到应用。     

中华绒螯蟹线粒体DNA l2S rRNA基因片段的序列研究

首次进行了中华绒螯蟹（ Ｅｒｉｏｃｈｅｉｒ ｓｉｎｅｎｓｉｓ）线粒体 ＤＮＡ １２ＳｒＲＮＡ的序列分析。参考果蝇、蚤状溞序列对中华绒螯蟹线粒体ＤＮＡ １２ＳｒＲＮＡ基因片段做了引物设计、ＰＣＲ扩增及序列测定，结果得到 ４５７ ｂｐ的碱基序列，其Ａ、Ｔ、Ｇ、Ｃ含量分别为 １５９ｂｐ（３４．７９％）、１７７ｂｐ（３８．７３％）、５１ｂｐ（１１．１６％）、７０ｂｐ（ １５． ３２％），与果蝇、蚤状溞的相同基因片段的序列含量基本相似。     

长吻鮠碱性磷酸酶的分子量及氨基酸组成

长吻鮠碱性磷酸酶的分子量及氨基酸组成陈定福，唐云明（西南师范大学生物系，重庆６３０７１５）关键词长吻．肝脏，碱性磷酸酶，分子量，氨基酸组成ＭＯＬＥＣＵＬＡＲＷＥＩＧＨＴＡＮＤＡＭＩＮＯＡＣＩＤＣＯＭＰＯＳＩＴＩＯＮＯＦＡＬＫＡＬＩＮＥＰＨＯＳＰＨＡＴ...     

Isolation and characterization of collagens from the skin of giant grouper (Epinephelus lanceolatus)

ABSTRACT

Acid-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 (T_max) 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).     

草鱼鱼鳞胶原蛋白的提取及其部分生物学性能

以草鱼鱼鳞为原料, 分别提取鱼鳞中的酸溶性胶原蛋白(ASC)和酶溶性胶原蛋白(PSC), 着重开展了其包括热稳定性、体外酶降解性以及胶原海绵材料特性在内的相关研究, 并与哺乳动物来源的猪皮胶原(PC)相比较。实验结果表明, 制备所得的3种胶原蛋白均为典型的Ⅰ型胶原并具有完整的三螺旋结构; PC的热变性温度(41.6 ℃)明显高于ASC(34.8 ℃)和PSC(35.2 ℃); 3种胶原蛋白的体外酶降解性能受水解酶的种类、胶原蛋白提取方法、胶原蛋白来源、胶原蛋白受热历史以及蛋白的自组装程度影响。胶原蛋白酶、胰蛋白酶和木瓜蛋白酶对淡水鱼胶原均具有不同程度的降解能力, 但胶原蛋白酶的降解能力最强; 相同条件下, 3种胶原蛋白体外酶降解率依次为ASC>PSC>PC; 经热变性处理后胶原蛋白的体外酶降解率明显提高而经体外自组装处理后其体外酶降解率均出现不同程度的降低; 3种胶原样品冻干后得到的胶原海绵材料具有不同的机械性能和组织结构, ASC和PSC海绵是一种多孔但拉伸承受力较弱的海绵材料, 而PC则与之相反。     

Characteristics of Collagen from Rohu (Labeo rohita) Skin

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 T_max 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.     

Characteristics and Select Functional Properties of Collagen from Golden Pompano (Trachinotus ovatus) Skins

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 (T_m) 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.     

鲤鱼鱼鳞胶原蛋白ASC与PSC的比较

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.     

Pyridinoline concentrations in muscular and skin collagen of fish and relationship between collagen solubility and pyridinoline concentration in fish muscular collagen

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.     

Changes in muscle collagen content during <Emphasis Type="Italic">post mortem</Emphasis> storage of farmed sea bream (<Emphasis Type="Italic">Sparus aurata</Emphasis>): influence on textural properties

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.     

Isolation and Characterization of Pepsin-Soluble Collagen from the Skin of Peru Squid (Dosidicus gigas)

Pepsin-soluble collagen (PSC) was isolated from Peru squid (Dosidicus gigas) skin and physicochemical properties of the PSC were determined. The PSC exhibited a maximum absorbance at 220 nm. Sodium dodecyl sulfate polyacrylamide gel electrophoresis suggested the collagen containing α1 and α2 chain was classified as type I collagen. Amino acid composition indicated that the collagen had lower amino acid content than that of mammalian collagen. Denaturation temperature (T_d) of the PSC was 26.8°C. The PSC had relatively high solubility in alkaline condition or NaCl concentrations below 2%. Fourier transform infrared spectroscopy investigations showed the existence of helical arrangements of collagen. The lyophilized collagen had a uniform and regular network structure. These results suggested that Peru squid skin was a potential source of collagen for further research and application.     

Characterization of Acid-Soluble Collagen From Bone of Pacific Cod (Gadus macrocephalus)

Acid-soluble collagen (ASC) was isolated from Pacific cod (Gadus macrocephalus) bone. The ASC was rich in glycine. The amount of imino acid was lower than that of calf skin collagen, as was the transition temperature (48.6°C). Electrophoresis revealed two different α chains (α₁ and α₂), β-component, and γ-component. Fourier transform infrared spectroscopy measurement showed that ASC was in triple-helix structure. ASC had a solubility greater than 90% in a very acidic pH range (pH 1–4), and the solubility decreased with increasing NaCl concentrations up to 3%. Lyophilized ASC had a network ultrastructure with lace-like fibers, similar to calf skin collagen sponge.