离子膜法技术在氨基酸制备中的应用探讨

介绍了离子交换膜分离技术原理及其在氨基酸制备中的应用工艺 ,设计提出了新型反馈离子交换膜分离工艺 ,取代传统的老工艺 ,实现了工业化大生产。     

氨基酸制备中的萃取技术

总结了氨基酸制备中的三大萃取技术:离子交换反应萃取,液膜分离萃取和反相胶团萃取及其在毛发水解氨基酸萃取分离方面的应用。     

膜分离技术在寡糖制备与分离中的应用*

寡糖是多糖经过降解后得到的小分子活性物质,具有抗氧化、抗肿瘤、抗病毒和免疫调节等多种生物活性,是功能食品开发领域研究的热点。目前,寡糖的分离和制备主要采用离子交换色谱、凝胶渗透色谱以及两者联用的方法,分离时间长、制备成本高,难以实现寡糖的规模化分离和制备。膜分离技术(membrane separation technology,MST)是一种利用膜的选择性渗透作用,实现两组分或者多组分分离的技术,具有操作简单、分离效果好、高效节能等优点,特别是能够直接放大应用于规模化的分离工程,因此在寡糖等小分子的分离和制备等方面具有巨大的应用潜力。系统总结了膜分离技术在寡糖分离与制备领域的最新进展,综述了用于分离和制备寡糖的膜分离技术分类、分离工艺及其应用现状,并对目前膜分离技术用于大规模分离和制备寡糖过程中面临的挑战进行了讨论。     

低聚木糖分离纯化的研究进展

综述了低聚木糖分离纯化的研究进展。低聚木糖是一种非消化性寡糖 ,能选择性增殖肠道内双歧杆菌 ,可广泛应用于食品工业和饲料工业。低聚木糖的分离纯化技术主要包括层析分离技术 (包括凝胶过滤层析、离子交换层析和吸附层析 )和膜分离技术 (包括超滤、纳滤和反渗透 )。低聚木糖的提纯主要采用膜分离技术和层析分离技术 ,低聚木糖单一组分的分离主要采用凝胶过滤层析和吸附层析     

中空纤维膜过滤技术在单抗生产中的应用

作为生物药物的”重磅炸弹”,大规模动物细胞培养生产治疗用单克隆抗体（以下简称单抗）已成为生物制药发展的主导。Mabselect SuRe亲和层析结合Capto Adhere复合离子交换两步层析工艺已经成为抗体生产工艺的亮点,而中空纤维膜过滤技术是一种快速高效的膜分离技术,具有容尘量高、温和低剪切力、操作灵活、成本低、易于放大等优点．因此广泛应用于重组蛋白、疫苗等生物制药领域。通过将中空纤维膜过滤技术和下游两步层析工艺相结合,可以成功的迎接几十甚至上百公斤单抗生产所面临的挑战。     

最新专利文摘

CN1903703:一种富氢气源提纯氢气的工艺方法本发明公开了一种富氢气源提纯氢气的工艺方法,解决现有采用膜分离和/或变压吸附工艺提纯氢气存在的对原料气成分要求严格、应用范围不广、工艺复杂、装置占地大的技术问题,包括如下工序:a·原料气压缩;b·脱碳脱水;c·膜分离;d·催化     

电渗析分离提纯谷氨酸工艺研究

<正> 一概述目前味情行业较普遍采用的谷氨酸提炼工艺为等电点离子交换法。其流程为: 发酵液pH3.2等电点结晶→母液第一次离子交换除按→母液第二次离子交换浓缩→结晶谷氨酸。由于采取二次离子交换耗酸耗碱量较大。采用电渗析分离提纯谷氨酸工艺,代替母液第一离子交换除铵旧工艺则能节约酸碱提高得率,降低成本,其工艺流程如图1:     

猪脑组织总神经节苷脂提取纯化工艺的研究

本文较详细地研究论述了神经节苷脂（Ｇｌｓ）的提取纯化工艺。从猪脑组织中用萃取法获得Ｇｌｓ后,用多孔型弱碱性离子交换树脂３３５和强碱性离子交换树脂７１７对其进行分离纯化,并对工艺过程及产品品质进行了分析和比较研究,实验证明：３３５离子交换层析分离Ｇｌｓ,得率６５．９ｍｇ／１００ｇ湿组织,纯度８０．３％;７１７离子交换层析分离Ｇｌｓ,得率７７．４ｍｇ／１００ｇ湿组织,纯度７６．９％;从工艺过程及产品品质而言,采用多孔型弱碱性离子交换树脂分离提取Ｇｌｓ,具有一定的经济价值。     

白腐真菌吸附铅的研究

含重金属废水的传统处理方法有化学沉淀法、离子交换法、吸附法、电解法和膜分离法等,它们虽然也能达到一定的净化效果,但因过程繁琐并易造成二次污染而不够理想,尤其是金属离子浓度较低时,往往操作费用和原材料成本相对过高。近年来采用生物吸附法去除废水中的重金属...     

膜分离技术在硫酸软骨素分离方面的应用

介绍了硫酸软骨素的生产工艺 ,应用膜分离技术对现有工艺进行了改进 ,使硫酸软骨素纯度达 95 .2 % ,收率提高3% ,并且简化了操作     

离子交换法分离D-天冬氨酸和L-丙氨酸

对离子交换法分离D-天冬氨酸和L-丙氨酸的工艺条件进行了研究。综合考虑树脂对D-天冬氨酸和L-丙氨酸的吸附容量及相对选择系数,选择了一种适合该体系分离的树脂—XH-1,并对吸附条件及洗脱条件进行了研究,确定了最佳工艺条件,为今后工业应用提供一定的依据。     

Selective protein separations using Formed-In-Place anion exchange membranes.

Anion exchange membranes prepared by adsorption of polymers on Formed-In-Place microfiltration substrates were formed and ion-exchange separations of solutions containing two proteins were determined by ion exchange membrane sequential separation procedures, similar to affinity membrane separation procedures. Representative ion exchange separation processes utilizing adsorbed poly(ethylene imine) (PEI) as the ion exchange membrane for the separation of the components of solutions containing two proteins, bovine serum albumin (BSA) and lysozyme and ovalbumin and lysozyme, are described. The stability of the PEI adsorbed layer, binding characteristics of the BSA to the membrane and purification properties of the procedure were determined.     

Large scale protein separations: engineering aspects of chromatography

The engineering considerations common to large scale chromatographic purification of proteins are reviewed. A discussion of the industrial chromatography fundamentals is followed by aspects which affect the scale of separation. The separation column geometry, the effect of the main operational parameters on separation performance, and the physical characteristics of column packing are treated. Throughout, the emphasis is on ion exchange and size exclusion techniques which together constitute the major portion of commercial chromatographic protein purifications. In all cases, the state of current technology is examined and areas in need of further development are noted.

The physico-chemical advances now underway in chromatographic separation of biopolymers would ensure a substantially enhanced role for these techniques in industrial production of products of new biotechnology.     

Recombinant human insulin.

Insulin is a well-characterized peptide that can be produced by recombinant DNA technology for human therapeutic use. A brief overview of insulin production from both traditional mammalian pancreatic extraction and recombinant bacterial and yeast systems is presented, and detection techniques, including electrophoresis, are reviewed. Analytical systems for insulin separation are principally based on reversed-phase chromatography, which resolves the deamidation product(s) (desamido insulin) of insulin, proinsulin, and insulin. Process-scale separation is a multistep process and includes ion exchange, reversed-phase, and size exclusion chromatography. Advantages and/or disadvantages of various separation approaches, as described by the numerous literature references on insulin purification, are presented.     

离子交换法与氨基酸的分离纯化

离子交换法广泛用于氨基酸的分离纯化。文章综述了离子交换法与氨基酸的分离纯化,包括分离纯化单一氨基酸及对氨基酸混合物进行分组分离纯化。     

Understanding the interaction of proteins to ion exchange chromatographic supports: A surface energetics approach

Ion exchange chromatography is one of the most widely used chromatographic technique for the separation and purification of important biological molecules. Due to its wide applicability in separation processes, a targeted approach is required to suggest the effective binding conditions during ion exchange chromatography. A surface energetics approach was used to study the interaction of proteins to different types of ion exchange chromatographic beads. The basic parameters used in this approach are derived from the contact angle, streaming potential, and zeta potential values. The interaction of few model proteins to different anionic and cationic exchanger, with different backbone chemistry, that is, agarose and methacrylate, was performed. Generally, under binding conditions, it was observed that proteins having negative surface charges showed strong to lose interaction (20 kT for Hannilase to 0.5 kT for IgG) with different anionic exchangers (having different positive surface charges). On the contrary, anionic exchangers showed almost no interaction (0–0.1 kT) with the positively charged proteins. An inverse behavior was observed for the interaction of proteins to cationic exchangers. The outcome from these theoretical calculations can predict the binding behavior of different proteins under real ion exchange chromatographic conditions. This will ultimately propose a better bioprocess design for protein separation.     

Kinetics of ion exchange process for separation of glutamic acid

Kinetics of the separation of L-glutamic acid (GLU) by ion exchange has been studied with strongly acidic H⁺-type cation exchange resin Amberlite IR-122. Since glutamic acid is a trivalent ampholyte and dissociates according to three equilibrium reactions, separation of G⁺ ions by a cation exchange process is accompanied by the dominant reversible reaction, i.e. G⁺+H⁺ ? G⁰. Accompanying reversible reaction has an effect on the ion exchange rate, and decreases the performance of the process comparing with the ideal case that the exchanging ions retain their identity. The analysis was performed first with the ion exchange column, DIC (L/D=0.52); and then with the ion exchange column, IC (L/D=10.9). The data were collected with model glutamic acid solutions for both DIC and IC columns/reactors. IC experimental results were then compared with that of DIC and the effect of scale up on ion exchange process was investigated. The experimental results have provided an adequate basis for the design calculations, and the design parameters were determined. Rate coefficients for the liquid phase mass transfer controlled cation exchange process were calculated and interrelated with a plot of j _Mfactor versus Reynolds number.     

Removal of lipopolysaccharides from protein-lipopolysaccharide complexes by nonflammable solvents

During the recovery of recombinant proteins from gram negative bacteria, many of the methods used to extract proteins from cells release lipopolysaccharides (LPS, endotoxin) along with the protein of interest. In many instances, LPS will co-purify with the target protein due to specific or non-specific protein-LPS interactions. We have investigated the ability of alkanediols to effect the separation of LPS from protein-LPS complexes while the complexes are immobilized on ion exchange chromatographic resins. Proteins were complexed with fluorescently labeled LPS and bound to ion exchange resin. Alkanediol washes of the resins were preformed and the proteins eluted. Column eluates were monitored for LPS and protein by fluorescence and UV spectroscopy, respectively. Alkanediols were effective agents for dissociating LPS from protein-LPS complexes. The efficiency of LPS removal increased with increasing alkanediol chain length. The 1,2-alkanediol isomers were more effective than terminal alkanediol isomers in the separation of LPS from protein-LPS complexes, while the separation of LPS from protein-LPS complexes was more efficient on cation exchangers than on anion exchangers. In addition, it was noted during these investigations that the 1,2-alkanediols increased the retention time of the proteins on the ion exchange resins. Alkanediols provide a safer alternative to the use of other organics such as alcohols or acetonitrile for the separation of LPS from protein due to their lower toxicity and decreased inflammability. In addition, they are less costly than many of the detergents that have been used for similar purposes.