Publications by authors named "Simon Crelier"

Contaminants deriving from human activities represent a constantly growing threat to our environment and have a direct impact on plant and animal health. To alleviate this ecological imbalance, biocatalysis offers a green and sustainable alternative to conventional chemical processes. Due to their broad specificity, laccases are enzymes possessing excellent potential for synthetic biotransformations in various fields as well as for the degradation of organic contaminants.

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Three institutes of the Universities of Applied Sciences that are active in Chemistry and Life Sciences present a selection of their activities in the field of environmental sciences. These projects include analytical monitoring, removal of micropollutants, waste reduction and valorization.

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Phenolic compounds such as catechol represent a particular type of micropollutant whose high stability prevents rapid decay and metabolization in the environment. We successfully cloned a catechol 2,3-dioxygenase (C2,3O) from Pseudomonas putida mt-2 and expressed it in Escherichia coli BER2566. The biomass isolated from shake-flask fermentations was used to partially purify the enzyme.

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This article provides an overview of activities in the fields of continuous processes, flow chemistry and microreactors at the Universities of Applied Sciences in Switzerland.

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Medium-chain-length polyhydroxyalkanoates (mcl-PHAs) are biobased and biodegradable alternatives to petrol-derived polymers, whose break-through has been prevented by high production cost. Therefore we investigated whether wastes from the food industry (nine types of fruit pomace including apricots, cherries and grapes, and waste frying oil) could replace the costly sugars and fatty acids typically used as carbon substrates for the bacterial fermentations. A selection of enzyme preparations was tested for converting the residual polysaccharides from the pomaces into fermentable monosaccharides.

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The biological properties of a protein critically depend on its conformation, which can vary as a result of changes in conditions such as pH or following the addition of various substances. Being able to reliably assess the quality of protein structures under various conditions is therefore of crucial importance. Infrared (IR) spectroscopy of the Amide I band of proteins is a powerful method for the determination of protein conformations and further allows the analysis of continuously flowing solutions of the target molecule.

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A micro-reactor coupled to a microfluidic system and an online UV/VIS spectrometer is described. The enzymatic reaction studied is the hydrolysis of the N-benzoyl-L-tyrosine ethyl ester (BTEE) to N-benzoyl-L-tyrosine (BT) and ethanol, catalyzed by chymotrypsin. The production is online monitored with UV spectroscopy at 256 nm.

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Manothermosonication (MTS) treatments, the simultaneous application of heat and ultrasound under moderate pressure, of milk during 12 s at 20 kHz ultrasound amplitude, 2 kg pressure, and 40 degrees C allowed elaboration of yoghurts with rheological properties superior to those of control yoghurts elaborated with untreated milk. Measurements performed on intact samples (compression tests, relaxation tests, and texture profile analysis) and on slowly stirred samples (flow curves, apparent viscosity, yield stress, and viscoelastic properties) showed that MTS yoghurts had stronger structures, which resulted in higher values of almost all of the many relevant rheological parameters. Homogenization of fat globules brought about by MTS treatments is not responsible for the superior properties of MTS yoghurts, because the control yoghurt was also elaborated with homogenized milk.

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