Citrobacter freundii休止细胞催化合成L-多巴

以在L-酪氨酸诱导下高效表达酪氨酸酚解酶的菌株Citrobacter freundii 48003-3的休止细胞为生物催化剂,以邻苯二酚、丙酮酸钠、醋酸铵为前体,选择性合成L-DOPA。研究了反应温度、pH和前体浓度等对合成L-DOPA的影响。最优反应条件下,反应12h,L-DOPA的量可达到9．5g／L。     

利用固定在角叉菜凝胶中的中间埃希氏菌细胞合成L-多巴

将中间埃希氏菌(Escherichia intermedia)细胞用包埋方法固定在角叉菜凝胶中,应用于从邻苯二酚、丙酮酸和氨酶促合成L-多巴。含75mg细胞/克凝胶的制剂保留原酶活性的60～65％。通过对三种底物抑制作用进行观察。看到底物浓度对游离细胞和固定化细胞合成L-多巴初速度的影响几乎相似,在分批反应器中,20小时得到7.8克/升以上的L-多巴(产率是0.39克/升小时)。在初速度条件和分批反应器中,固定在角叉菜凝胶中的细胞合成的L-多巴比固定在聚丙烯酰胺凝胶中的细胞要高。     

L-酪氨酸苄酯的合成及其影响因素研究

以L-酪氨酸和苯甲醇为原料合成一种新型的L-酪氨酸衍生物——L-酪氨酸苄酯。首先用苯甲醇与氯化亚砜反应生成氯化亚硫酸酯,合成物再与L-酪氨酸发生酯化反应得到L-酪氨酸苄酯,其结构经质谱(MS)分析法确证。在此基础上研究了影响该合成工艺的主要因素,即原料配比、反应温度、反应时间、pH值。结果显示合成L-酪氨酸苄酯的较佳工艺条件为:物料摩尔比mol(SOCl2)∶mol(L-酪氨酸)=1.3∶1.0,室温下反应3h,120℃下反应2h,后处理溶液pH为7.5。本工艺适宜于工业化大规模生产。     

Citrobacter freundii休止细胞催化合成L-多巴

以在L 酪氨酸诱导下高效表达酪氨酸酚解酶的菌株Citrobacterfreundii 4 80 0 3 3的休止细胞为生物催化剂 ,以邻苯二酚、丙酮酸钠、醋酸铵为前体 ,选择性合成L DOPA。研究了反应温度、pH和前体浓度等对合成L DOPA的影响。最优反应条件下 ,反应 1 2h ,L DOPA的量可达到 9 5g/L。     

2-氰基-D,L-苯丙氨酸盐酸盐的合成

合成了非天然氨基酸２－氰基－Ｄ,Ｌ－苯丙氨酸盐以及四个中间体,其结构分别通过红外光谱、核磁共振、元素分析、熔点测试等手段得到确证。     

虫酰肼对甜菜夜蛾多巴脱羧酶和酪氨酸羟化酶的抑制作用

虫酰肼模拟昆虫蜕皮激素的作用干扰新表皮的形成。为了探讨虫酰肼对昆虫新表皮形成的影响是否与抑制表皮形成相关酶的活性有关, 本研究应用高效液相色谱-荧光检测法（HPLC-RP）, 测定了甜菜夜蛾Spodoptera exigua 5龄幼虫用虫酰肼处理不同时间（24, 48和72 h）后多巴脱羧酶和酪氨酸羟化酶的活性。结果表明： 用LC₁₁ （28.41 μmol/L）和LC₃₃ （85.23 μmol/L）两个亚致死剂量的虫酰肼处理5龄幼虫后, 多巴脱羧酶和酪氨酸羟化酶的活性均受到明显抑制, 高浓度的抑制作用大于低浓度的抑制作用。随着处理时间的延长, 同一剂量的抑制作用逐渐增强。进一步测定虫酰肼处理24, 48和72 h后5龄幼虫血淋巴、 脂肪体、 中肠、 表皮和头部的多巴脱羧酶和酪氨酸羟化酶的活性, 可看出虫酰肼对幼虫不同组织的多巴脱羧酶和酪氨酸羟化酶的活性也具有相似的抑制作用。结果提示, 虫酰肼对甜菜夜蛾幼虫多巴脱羧酶和酪氨酸羟化酶活性具有明显抑制作用, 幼虫新表皮形成受阻可能与虫酰肼抑制多巴脱羧酶和酪氨酸羟化酶的活性有关。     

L-酪氨酸纯化工艺的优化

采用一步法对不同来源的L-酪氨酸粗品进行了分离纯化。通过对碱溶pH值、分解胱氨酸的温度、分解时间和中和pH值等条件的优化,提高了L-酪氨酸产品的纯度。试制产品主要质量指标均达到日本味之素(AJI92)和中国药典(CP2000)标准。同时,工艺的简化、活性炭的回收利用以及滤液的循环使用,均大幅降低了生产成本。     

异柱五加叶中齐墩果烷型皂苷的研究(英文)

利用柱色谱从异柱五加 (Acanthopanax sieboldianus forma albeofolium Yook) 叶的甲醇提取液中分离出四个齐墩果烷型皂苷类化合物.通过波谱方法(1H NMR、13C NMR、2D NMR和FAB-MS)鉴定它们分别为kalopanax-saponin B (1)、acanthopanax saponin CP3(2)、kalopanax-saponin A (3) 和sieboldianoside A (4).     

Electropolymerized films formed from the amphiphilic decyl esters of D- and L-tyrosine compared to L-tyrosine using the electrochemical quartz crystal microbalance

Using the electrochemical quartz crystal microbalance (EQCM), we compared thin films formed on Pt by electropolymerization of l-tyrosine to that of the amphiphilic monomers, decyl esters of d- and l-tyrosine (DEDT and DELT). Mass build-up and film properties were determined as a function of monomer concentration via frequency, f, motional resistance, R, and charge passage, Q, measurements. Films were found to occur by a combination of monomer electropolymerization and adsorption for DEDT and DELT, but only by electropolymerization for l-tyrosine. This difference in film formation process for the monomers is reflected in the net mass build-up for each film, as represented by calculated df/dQ values. For the adsorbing monomers DEDT and DELT, films possessed concentration dependent df/dQ values, more than 100-fold greater than that for l-tyrosine film formation under equivalent electropolymerization conditions. During the entire film growth process, all three films exhibited no significant energy dissipation properties (DeltaR invariant). Concentration dependent adsorption of significant levels of unpolymerized but self-assembled DEDT and DELT monomers account for the subsequent time dependent mass loss observed from the films maintained in buffer in the absence of monomer. Contact angle measurements demonstrated a pH dependent increase in the surface hydrophilicity of films electropolymerized from the DEDT, DELT, and l-tyrosine monomers but not films formed from phenol and 3-nitrophenol monomers. This behavior is consistent with the monomers' known changes in titration/charge state properties with increasing pH. This study provided insight into the film formation, stability, and surface hydrophilicity resulting from electropolymerization of these related tyrosine based monomers. This information is critical to assessing the utility these films may have in the development of new biomaterials and as biological macromolecule or cell immobilization strategies in biosensors.     

电渗析技术用于猪毛水解液脱酸的研究

利用上海华凯科技贸易公司制作的HF系列离子交换膜为隔膜的电渗析器对猪毛水解液进行电渗析脱酸,研究了脱酸过程中浓缩室、淡化室酸度变化及电流效率     

Purification and some properties of L-tyrosine carboxy-lyase from barley roots

L-Tyrosine carboxy-lyase (E. C. 4. 1. 1. 25) was extracted fromthe roots of barley seedlings and purified approximately 25fold. Optimum pH for the enzyme activity was found to be 7.3.The Km value for L-tyrosine was calulated as 4.5?10^–4M.D-Isomer did not react with the enzyme. L-DOPA, m-tyrosine ando-tyrosine were decarboxylated to some extent. Pyridoxal phosphateactivated the enzyme 4 fold. Caffeic acid and p-coumaric acidare competitive inhibitors. Ki values were 4.5?10^–5M forcaffeic acid and 1.6?10^–4M for p-coumaric acid. L-DOPAand m-tyrosine had an inhibitory effect on the decarboxylationof L-tyrosine. Hydroxylamine, semicarbazide, p-CMB, Fe⁺⁺, Cu⁺⁺,and Hg⁺⁺ inhibited the decarboxylation of tyrosine. Enzyme activitywas also found in extracts from Triticum aestivum, Zea maysand Cytisus scoparius. (Received November 30, 1973; )     

Structural basis for discrimination of L-phenylalanine from L-tyrosine by phenylalanyl-tRNA synthetase

Aminoacyl-tRNA synthetases (aaRSs) exert control over the faithful transfer of amino acids onto cognate tRNAs. Since chemical structures of various amino acids closely resemble each other, it is difficult to discriminate between them. Editing activity has been evolved by certain aaRSs to resolve the problem. In this study, we determined the crystal structures of complexes of T. thermophilus phenylalanyl-tRNA synthetase (PheRS) with L-tyrosine, p-chloro-phenylalanine, and a nonhydrolyzable tyrosyl-adenylate analog. The structures demonstrate plasticity of the synthetic site capable of binding substrates larger than phenylalanine and provide a structural basis for the proofreading mechanism. The editing site is localized at the B3/B4 interface, 35 A from the synthetic site. Glubeta334 plays a crucial role in the specific recognition of the Tyr moiety in the editing site. The tyrosyl-adenylate analog binds exclusively in the synthetic site. Both structural data and tyrosine-dependent ATP hydrolysis enhanced by tRNA(Phe) provide evidence for a preferential posttransfer editing pathway in the phenylalanine-specific system.     

Life history,morphology and crossability of Chondrus ocellatus forma ocellatus and C. ocellatus forma crispoides (Gigartinales,Rhodophyta) from the north-western Pacific

The morphology, life histories and crossability in culture are described for the marine red algae Chondrus ocellatus Holmes forma ocellatus from Japan, China and Korea and C. ocellatus f. crispoides Mikami (Gigartinaceae, Rhodophyta) from Japan. In culture, all isolates of both formae showed a Polysiphonia-type life history typical of the family Gigartinaceae. Plants of C. ocellatus f. ocellatus from Korea and China and some strains from Japan formed gametangia under long-day conditions (LD) at 15°C; however, two other Japanese strains required short-day conditions (SD) at 15°C for gametogenesis, indicating a photoperiodic response. Plants of C. ocellatus f. crispoides did not require SD for gamete formation. In all strains, tetrasporophytes of both formae produced tetrasporangia under LD. Isolates of C. ocellatus f. ocellatus from Japan, China and Korea were found to be completely sexually compatible regardless of photoperiodic characteristics, and the responses to daylength shown by progeny of LD and SD strains suggested Mendelian inheritance of a daylength factor. Chondrus ocellatus f. ocellatus was sexually incompatible with C. nipponicus Yendo, a morphologically similar species from Japan, but C. ocellatus f. crispoides was partially interfertile with both C. ocellatus f. ocellatus and C. nipponicus, indicating that the three entities are closely related. In view of the apparently higher breeding compatibility between C. nipponicus and C. ocellatus f. crispoides, and the fact that these two entities are more similar morphologically and reproductively, it is proposed, provisionally, to refer C. ocellatus forma crispoides to C. nipponicus.