Electrocatalytic Reduction of CO2 to Ethylene by Molecular Cu‐Complex Immobilized on Graphitized Mesoporous Carbon

The electrochemical reduction of carbon dioxide (CO₂) to hydrocarbons is a challenging task because of the issues in controlling the efficiency and selectivity of the products. Among the various transition metals, copper has attracted attention as it yields more reduced and C2 products even while using mononuclear copper center as catalysts. In addition, it is found that reversible formation of copper nanoparticle acts as the real catalytically active site for the conversion of CO₂ to reduced products. Here, it is demonstrated that the dinuclear molecular copper complex immobilized over graphitized mesoporous carbon can act as catalysts for the conversion of CO₂ to hydrocarbons (methane and ethylene) up to 60%. Interestingly, high selectivity toward C2 product (40% faradaic efficiency) is achieved by a molecular complex based hybrid material from CO₂ in 0.1 m KCl. In addition, the role of local pH, porous structure, and carbon support in limiting the mass transport to achieve the highly reduced products is demonstrated. Although the spectroscopic analysis of the catalysts exhibits molecular nature of the complex after 2 h bulk electrolysis, morphological study reveals that the newly generated copper cluster is the real active site during the catalytic reactions.     

纵览衣物清洗剂技术

随着生活水平的提高，人们对自身生活质量的要求越来越高，从而促进了衣物清洗剂技术的发展。本文从这个角度阐述了衣物清洗剂从肥皂、洗衣粉到多功能环保型产品的发展过程。     

Immobilization of an endopectinlyase on γ-alumina: Study of factors influencing the biocatalytic matrix stability

Endopectinlyase (EC 4.2.2.10) from Aspergillus japonicus was immobilized on to γ-alumina. Adsorption performed at pH 5·0 and a subsequent cross-linking phase using 0·1% glutaraldehyde were the chosen immobilization conditions. The comparison between the main biochemical parameters of the immobilized and free form of the enzyme showed that the immobilization procedure used did not affect the enzyme biochemical properties. The interactions between the carrier and the enzyme are essentially secondary bonding. In fact they depend on the pH and on the presence of phosphate ions in the medium. A tentative chemical model of the biocatalytic matrix thus obtained is proposed.     

Kinetic behaviour of muscle LDH immobilized in nylon tubing

Immobilization was carried out of the lactate dehydrogenase (LDH) from rabbit muscle (EC 1.1.1.27), cross-linked through the bifunctional reactive glutar-aldehyde on to nylon tubing (1 m long, 53cm² internal surface area). Immobilized LDH inactivation kinetics are of first order (t_1/2 = 3·6 years, k = 5·4,e^?4 day^?1 to 5°C). The smaller effect of pH on activity than in the case of LDH in solution can be explained on the basis of limitation to proton diffusion towards the support. A limiting effect to free external diffusion of the substrate towards and products from the support was also observed, an effect which seems to determine the effective kinetic behaviour of immobilized LDH. The apparent optimum temperature is centred around 40°C, observing a clear inactivation (thermal denaturation) above this temperature. In the temperature range studied (10–40°C), the co-existence was seen of a kinetic control accompanied by another control, involving diffusional transport of substrates and products, on the global activity of the immobilized enzyme. This makes the Arrhenius profiles curvilinear. Both graphic and statistical non-linear regression analysis of the kinetic data—rate, v, versus substrate concentration [S]—carried out under conditions in which the diffusional limitations can be considered negligible (high recirculation flow rate), permitted investigation of the intrinsic kinetic behaviour of immobilized LDH. In this sense, it can be deduced that the rate equation to which these data seem to be fitted is of the polynomial quotient type in [S] of minimum degree 2:2. Although the diffusional limitations have a marked effect on the type of global kinetics shown by immobilized LDH, temperature was not found to affect its v[S] behaviour. The experimental evidence obtained thus indicates that the rate equation in the 10-40°C temperature range continues to be a rational equation of at least degree 2:2 in [S].     

醋酸甲酯在Cs_(1.5)PW/SiO_2催化剂上的水解反应

通过改变阳离子的种类与配比,制备了一系列SiO2负载的磷钨酸盐催化剂,考察了制备方法对催化剂性能的影响,采用傅里叶变换红外光谱、X射线衍射、X射线荧光光谱、环境扫描电子显微镜等方法对催化剂进行了表征,并考察了该系列催化剂对醋酸甲酯水解反应的活性。实验结果表明,Cs1.5PW/SiO2催化剂的活性最好,当Cs1.5PW负载量(质量分数)为30%时,Cs1.5PW的Keggin结构保持完好,没有硅钨酸阴离子形成,Cs1.5PW在SiO2载体上高度分散;在反应温度55℃、反应时间2h的条件下,醋酸甲酯的转化率为35.79%,约为均相磷钨酸催化剂的1.3倍。该催化剂重复使用4次后,醋酸甲酯的转化率稳定在25%;80℃下反应2h,与NKC-9磺酸树脂催化剂相比,醋酸甲酯的转化率提高了5.17%。     

酶法提取树莓汁的研究

本试验以澳洲红、早红、美国22三个品种树莓为原料，通过不同的酶处理方法来制原果汁，优选适于制汁的品种和酶处理方法。     

General rate equations and their applications for cyclic reaction networks: multi-cycle systems

The network reduction technique and the Bodenstein approximation of quasi-stationary behavior of reaction intermediates were systematically applied to derive general yield ratio and rate equations for multi-cycle reaction networks in homogeneous catalysis. Dual-cycle reaction networks connected by a linear pathway, multi-cycle networks stemming from the same intermediate, and single-cycle with arbitrary number of pathways between two intermediates were considered. The general yield ratio and rate equations derived in this study are applicable for most enzymatic reactions and for homogeneous catalytic reactions. Examples of homogeneous catalysis were used to illustrate the application of the general yield ratio and rate equations for network elucidation.     

Screening of supports for the immobilization of pectinmethylesterase from acerola (Malpighia glabra L)

A partially purified extract of pectinmethylesterase (PME) from acerola fruit was immobilized on various supports: glass, celite, chrysotile, agarose, concanavalin A Sepharose 4B, egg shell, polyacrylamide and gelatin. In addition, reticulation with glutaraldehyde was assessed, as well as the use of gelatin in the presence of celite, glass and silica. The highest immobilization yields were obtained when the pectinmethylesterase was immobilized in concanavalin A Sepharose 4B (81.7%) and in gelatin‐water (78.0%). Copyright © 2004 Society of Chemical Industry     

固载于SBA-15分子筛中的同双核金属配合物催化剂

合成了3种同双核金属配合物[M2LCl3]Cl(L代表配体三亚乙基四胺,M代表Co,Cu,Cr),采用微波加热法合成了SBA-15分子筛,采用浸渍法将3种同双核金属配合物分别固载在表面官能化的SBA-15分子筛(SBA-15-NH2分子筛)中制得负载型催化剂。傅里叶变换红外光谱、X射线衍射、紫外可见光谱和热分析表征结果表明,同双核金属配合物被固载后,其结构仍保持完整。以环己烷氧化反应为探针反应,考察了[Co2LCl3]Cl/SBA-15-NH2,[Cu2LCl3]Cl/SBA-15-NH2,[Cr2LCl3]Cl/SBA-15-NH2催化剂的活性,环己烷转化率分别为11.0%,49.5%,57.9%;对于[Cr2LCl3]Cl/SBA-15-NH2催化剂,当分别以乙睛、丙酮和冰醋酸为溶剂时,环己烷转化率分别为57.9%,52.1%,34.2%,3次重复实验的环己烷转化率分别为57.9%,47.8%,46.5%,表明该催化剂具有较好的活性和重复使用性。     

γ-癸内酯的酶法拆分研究

研究了脂肪酶对γ-癸内酯(GDL)对映催化选择性水解反应,考察了各种因素对酶促水解拆分过程的影响。试验结果表明,水解产物-大量的酸会抑制脂肪酶的活性,采用高浓度的磷酸盐缓冲液可有效地稳定系统的酸碱度,使酶促反应顺利进行。在磷酸缓冲溶液体系中缓冲液pH=7.8,底物浓度为0.6mol/L,反应时间2.5小时,反应温度43℃为γ-癸内酯酶促水解拆分的最佳工艺条件。