TRAJAN Scientific and Medical

Ringwood, Australia

TRAJAN Scientific and Medical

Ringwood, Australia
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Candish E.,University of Tasmania | Wirth H.-J.,Trajan Scientific and Medical | Gooley A.A.,University of Tasmania | Shellie R.A.,University of Tasmania | Hilder E.F.,University of Tasmania
Journal of Chromatography A | Year: 2015

While polymer monoliths are widely described for solid phase extraction (SPE), appropriate characterization is rarely provided to unravel the links between physical characteristics and observed advantages and disadvantages. Two known approaches to fabricate large surface area polymer monoliths with a bimodal pore structure were investigated. The first incorporated a high percentage of divinyl benzene (PDVB) and the second explored hypercrosslinking of pre-formed monoliths. Adsorption of probe analytes; anisole, benzoic acid, cinnamic acid, ibuprofen and cortisone were investigated using frontal analysis and the SPE performance was compared with particulate adsorbents. Frontal analysis of anisole described maximum adsorption capacities of 164mgg-1 and 298mgg-1 for hypercrosslinked and PDVB adsorbents, respectively. The solvated state specific surface area was calculated to be 341 and 518m2g-1 respectively. BET revealed a hypercrosslinked surface area of 817m2g-1, 2.5 times greater than in the solvated state. The PDVB BET surface area was 531m2g-1, similar to the solvated state. Micropores of 1nm provided the enhanced surface area for hypercrosslinked adsorbents. PDVB displayed a pore size distribution of 1-6nm. Frontal analysis demonstrated the micropores present size exclusion for the larger probes. Recovery of anisole was determined by SPE using 0.4 and 1.0mLmin-1. Recovery for PDVB remained constant at 90%±0.103 regardless of the extraction flow rate suggesting extraction performance is independent of flow rate. A more efficient sample purification of saccharin in urine was yielded by PDVB due to selective permeation of the small pores. © 2015 Elsevier B.V.

PubMed | University of South Australia, University of Tasmania, Trajan Scientific and Medical and ARC Technologies
Type: | Journal: Journal of chromatography. A | Year: 2016

A membrane evaporation concentrator for continuous flow conditions is introduced. The membrane evaporation concentrator provides nearly 30-fold concentration in less than 60min whilst maintaining solute integrity under different sub-ambient pressure conditions and mild temperatures. To better understand the performance of the concentrator, a theoretical model was developed using caffeine as a model analyte, and used to predict the concentration performance of three target analytes at different conditions. An exponential relationship exists between temperature and concentration factor. By using the model it was determined that a 10-fold concentration (0.5) can be performed at 56.720.07C and at a flow rate of 10Lmin

Villani C.,University of Rome La Sapienza | D'Acquarica I.,University of Rome La Sapienza | Gasparrini F.,University of Rome La Sapienza | Ritchi H.,Trajan Scientific and Medical | And 4 more authors.
LC-GC Europe | Year: 2014

There is a need for chiral stationary phases (CSPs) designed for high performance liquid chromatography (HPLC) to switch to enantioselective applications using ultrahigh-performance liquid chromatography (UHPLC). Although important goals have been achieved to rapidly separate achiral compounds, enantioselective LC remains solidly attached to 3-μm and 5-μm totally porous particles and pressure values in the HPLC domain. This article describes strategies aimed at immobilizing or coating well-established chiral selectors onto sub-2-μm silica particles, and aims to illustrate the potential of enantioselective UHPLC (eUHPLC) in terms of high speed, throughput and resolution. © 2014, Advanstar Communications Inc. All rights reserved.

Williams K.L.,BKG Group | Gooley A.A.,TRAJAN Scientific and Medical | Wilkins M.R.,University of New South Wales | Packer N.H.,Research Frontiers
Journal of Proteomics | Year: 2014

This is the story of the experience of a multidisciplinary group at Macquarie University in Sydney as we participated in, and impacted upon, major currents that washed through protein science as the field of Proteomics emerged. The large scale analysis of proteins became possible. This is not a history of the field. Instead we have tried to encapsulate the stimulating personal ride we had transiting from conventional academe, to a Major National Research Facility, to the formation of Proteomics company Proteome Systems Ltd. There were lots of blind alleys, wrong directions, but we also got some things right and our efforts, along with those of many other groups around the world, did change the face of protein science. While the transformation is by no means yet complete, protein science is very different from the field in the 1990s.This article is part of a Special Issue entitled: 20. years of Proteomics in memory of Viatliano Pallini. Guest Editors: Luca Bini, Juan J. Calvete, Natacha Turck, Denis Hochstrasser and Jean-Charles Sanchez. © 2014 Elsevier B.V.

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