影响低电压电泳芯片分离的主要因素

运用简化的低电压电泳芯片的运动梯度场的分离和控制模型 ,对低电压芯片的各参数与分离度、分离效率的关系进行了讨论     

车身电泳流痕问题的解决

通过一次电泳流痕问题,从材料、工艺、工装及产品结构方面综合研究车身电泳流痕的解决方案。     

电泳废水处理技术研究进展综述

电泳废水成分复杂,需要不同的工艺对其进行处理,使其满足相关的排放标准。针对目前国内电泳废水的处理情况,介绍了厌氧折流板反应器-序批式活性污泥法、铁碳微电解处理法、Fenton工艺处理法、膜处理法及絮凝-生化处理法,及相关的研究进展。探讨了不同处理技术的优缺点,为企业选择合适的废水处理方法提供技术参考,实现经济效益与环境效益的双丰收。     

Study of hydroxycinnamic acids and malvidin 3-monoglucoside derivatives using capillary zone electrophoresis and ultra-performance liquid chromatography

Model solutions (pH = 3.5, 12% ethanol) of malvidin 3-O-glucoside (Mv3glc), the most common free anthocyanin in grapes and red wines from Vitis vinifera, and three free hydroxycinnamic acids present in wines (caffeic, ferulic and p-coumaric acids) were studied.     

制备型电泳法分离腺苷酸混合物

考察了制备型电泳法分离小分子生物物质的可行性及影响因素.在填充排阻凝胶的色谱柱两端各连接一个电极室以放置电极,在色谱柱上外加电场,进行单磷酸腺苷酸(AMP)和二磷酸腺苷酸(ADP)混合物的分离.以pH值 4.6的乙酸钠-乙酸缓冲溶液为流动相,考察分离介质、电场方向、电场大小和断电时间对分离度和样品回收率的影响.结果表明,具有很大孔径的排阻凝胶有利于样品的分离;电泳方向与液体流动方向一致时,电场越大,分离度越好,但收率越低;电泳方向与流体流动方向相反时,通电时间不能过长(否则样品不能出峰),分离度差,但收率高;在样品到达电极前停止通电,可以将AMP与ADP分离,而且减少了电解对样品的破坏.建立的制备电泳系统可用于离子型小分子生物物质的制备分离.     

Identification of four low molecular and water‐soluble proteins from grape (Vitis vinifera L.) seeds

Profiles of soluble proteins isolated from mature seeds of grape (Vitis vinifera L.) pomace were studied using two‐dimensional polyacrylamide gel electrophoresis (2D‐PAGE) coupled with matrix‐assisted laser desorption/ionisation time‐of‐flight mass spectrometry (MALDI–TOF–MS). Two‐dimensional gels stained with Coomassie brilliant blue revealed more than fifty protein spots. Four abundant protein spots showing low molecular weight (Mr) and wide isoelectric point (pI) were analysed by MALDI–TOF–MS, resulting in their identification. Taken together, these results suggest that identified proteins may be linked to seed development and metabolism, but more instructive is that they have some potential functions for future food application. These results provide some insights into conversion of grape processing wastes into useful products or even as raw material for other industries.     

Purification and structural characterisation of lipid transfer protein from red wine and grapes

Lipid transfer proteins (LTP) play a major role in plant defence and are of particular interest due to their known ability to cause allergic reactions. These proteins are expressed in grapes and also remain detectable after vinification, especially in red wine. However, it remains unknown whether the protein undergoes any changes during the vinification process. Here, we present a purification method for LTPs from Dornfelder grapes and wine. By liquid-chromatography–mass spectroscopy (LC–MS/MS) we identified LTPs from two different species (Vitis vinifera and Vitis aestivalis). Additionally, the purified LTPs were characterised using spectrometric methods, confirming their high purity and structural stability during vinification. We conclude that LTPs are resistant to the alcohol content (13.5 vol%), acidic milieu of wine and other ingredients present during the vinification process, indicating that the allergenic potential of grape LTP is not diminished by the vinification process.     

The effect of enzyme systems and processing on the hydrolysis of peanut (Arachis hypogaea L.) protein

In vitro protein digestion studies were carried out on raw and roasted peanut flour as the starting material in the production of peanut protein hydrolysate. Peanut flour was hydrolyzed with alcalase and alternately in a sequential digestion with pepsin-pancreatin, both for up to 24 h. The degree of hydrolysis (DH) at different times of hydrolysis was determined using the trinitrobenzenesulfonic acid (TNBS) method. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) was used to indicate destruction of native protein units in the enzymatic digests.Hydrolysis with alcalase was very rapid for the first 6 h after which a plateau was reached, whereas that with pepsin–pancreatin was more gradual reaching a plateau after 12 h of hydrolysis. Raw peanut hydrolyzed with alcalase and pepsin–pancreatin had 23% and 21% DH after 24 h respectively, whilst roasted peanut hydrolyzed with alcalase had 21% DH, with the pepsin–pancreatin hydrolysate recording the highest value of 25% after 24 h of hydrolysis.SDS-PAGE results showed that raw peanut samples behaved differently from the roasted samples; increasing hydrolysis time reduced larger peanut protein subunits, with only peptides of <20 kDa visible after hydrolysis for raw peanut, and virtually no distinct visible bands for the roasted peanut after 3 h of hydrolysis.     

Characterisation of the S-Carboxymethyl Extract of Wool Using Small Format Alkaline Urea-PAGE/SDS-PAGE Followed by Silver Staining

Abstract

Alkaline urea-PAGE/SDS-PAGE, when used in a novel format which was significantly smaller than that employed by earlier workers, and when followed by silver staining, resulted in the detection of excellently resolved protein components from S-carboxymethyl reductive extracts of very small wool samples, even samples as small as an individual wool fibre. The silver stained two-dimensional gel patterns exhibited significant improvements compared to the fluorograph gel patterns of earlier workers based on the presence of radiolabel incorporated within the S-carboxymethyl moiety. The silver staining resulted in the visualisation of numerous protein components, and in the region of the gel pattern expected to contain the high-sulfur protein fraction, there appeared more major components than the number of high-sulfur protein components usually displayed in fluorograph patterns. The relative amount of the high-sulfur protein fraction in the final silver stained gel pattern could be boosted, if desired, if the gel was loaded not with the whole wool extract but with the filtrate resulting from the passage of the whole extract through a centrifugal ultrafilter.