Albrektsenhirsch0674

In a continuous powder blending process machine vision is utilized as a Process Analytical Technology (PAT) tool. While near-infrared (NIR) and Raman spectroscopy are reliable methods in this field, measurements become challenging when concentrations below 2 w/w% are quantified. TEW-7197 However, an active pharmaceutical ingredient (API) with an intense color might be quantified in even lower quantities by images recorded with a digital camera. Riboflavin (RI) was used as a model API with orange color, its Limit of Detection was found to be 0.015 w/w% and the Limit of Quantification was 0.046 w/w% using a calibration based on the pixel value of images. A calibration for in-line measurement of RI concentration was prepared in the range of 0.2-0.45 w/w%, validation with UV/VIS spectrometry showed great accuracy with a relative error of 2.53 %. The developed method was then utilized for a residence time distribution (RTD) measurement in order to characterize the dynamics of the blending process. Lastly, the technique was applied in real-time feedback control of a continuous powder blending process. Machine vision based direct or indirect API concentration determination is a promising and fast method with a great potential for monitoring and control of continuous pharmaceutical processes.A synchronous fluorescence spectroscopy (SFS) nanoprobe is developed for the determination of vancomycin in exhaled breath condensate (EBC) samples. The synthesized nanoprobe is copper nanoclusters (Cu NCs) and its SFS peak is located at 405 nm with Δλ = 80. The affinity of Cu NCs to complex formation with vancomycin results in blocking non-radiative e-/h+ recombination defect sites on the surface of NCs and consequently enhancing the SFS signal intensity. Central composite design and response surface methodology is used for the optimization of reaction conditions. Under the optimized conditions, a linear relationship is found between the SFS intensity and the concentration of vancomycin in the range of 0.1-8 μg/mL. The validated method is applied for the determination of vancomycin in EBC of newborns receiving vancomycin treatment.Low extraction efficiency (60-81%) of okadaic acid (OA) and dinophysistoxin 1 (DTX1) was obtained for 4 out of 5 shellfish species from Washington State (WA), USA, during application of a standard extraction method for determination of lipophilic marine biotoxins by LC-MS/MS as recommended by the European Union Reference Laboratory for Marine Biotoxins (EURLMB). OA and total OA including esters, DTX1, DTX2, and total DTX including esters, azaspiracid 1, 2, and 3 (AZA1, AZA2, and AZA3), pectenotoxin 2 (PTX2), and yessotoxin (YTX) were the toxins examined. Matrix-matched standards prepared from the same control samples used for spike-and-recovery tests were employed to evaluate toxin extraction efficiency and sample clean-up procedures. We adjusted the EURLMB extraction method by either using an acidified methanol extraction or pre-cooking shellfish homogenates at 70 °C for 20 min before EURLMB extraction. Extraction efficiency was improved markedly for OA and DTX1 with both modified methods and for YTX with the pre-cooking step included. However, recoveries were lower for YTX using the acidified methanol extraction and for PTX2 in non-mussel samples with the pre-cooking step. A hexane wash was applied to clean water-diluted non-hydrolyzed samples and a hexane wash was combined with solid-phase extraction for cleaning hydrolyzed samples. Improved sample clean-up, combined with LC-MS/MS adjustments, enabled quantification of U.S. Food and Drug Administration-regulated toxins in five shellfish species from WA with acceptable accuracy using non-matrix matched calibration standards.Among the bioactive compounds present in extra-virgin olive oil, polar lipids and free fatty acids are minor compounds with well-known nutritional values and have been studied for traceability and adulteration investigations as well. In the present paper, the simultaneous characterization of polar lipids and free fatty acids in a pool of fifteen EVOO samples was achieved by means of reversed phase C18 analysis coupled to negative polarity high-resolution mass spectrometry. A total of 24 polar lipids, comprising 19 phospholipids and 5 sulfolipids, and 27 free fatty acids were tentatively identified, including several odd-chain and very long-chain fatty acids at trace levels. Moreover, a one-month study of lipid degradation on simulated storage conditions was carried out thanks to the set-up of a dedicated approach for degradation product analysis which was implemented of Compound Discoverer software. By virtue of the customized data processing workflow, more than forty compounds were tentatively identified, including compounds deriving from hydrolysis and oxidation reactions. Finally, by analysis of peak area trends, phosphoester hydrolyses of polar heads of phospholipids emerged as the fastest reactions, followed by glycerol ester hydrolyses and oxidative processes.The adsorption process of bovine serum albumin (BSA), ovalbumin (OVA) and human immunoglobulin G (IgG) on agarose ion-exchange media Q Sepharose FF and two dextran-grafted agarose media including Q Sepharose XL and Capto Q were studied using low field nuclear magnetic resonance (NMR). The T2 relaxation time was found directly proportional to the pore size and diminished after protein adsorbed, therefore, a theoretical model describing the relationship between protein binding amount and T2 relaxation signals was established. The model parameters, a, which reflects the contact area between the adsorbed protein and media surface, and the δ, which defined as the ratio of the protein volume to the pore volume after adsorption, were found to describe the pore occupation states of proteins in media with different pore structures very well. For small proteins, such as BSA and OVA, monolayer adsorption occurred on Q Sepharose FF, which has no dextran chains. Therefore, the adsorbed protein only occupied 49.05% of the pore volume for BSA and 25.51% for OVA, and contact area of each protein on the media were also low, suggesting mostly monolayer adsorption occurred. In the contrast, their adsorption to Q Sepharose XL and Capto Q with dextran chains tended to form multilayer adsorption, thus higher contact area was obtained and the pore volumes were almost 100% occupied. For large protein, such as IgG, the adsorption to all these three media was similar and about 30% of the pore volume were occupied, probably due to the similar restriction for IgG to entering the media pore. Results of this study will help to elucidate the relationship between protein adsorption and pore size variation, which present the significance of low field NMR in understanding protein adsorption mechanism.