Differentiation of volatile aroma components in organically and conventionally produced apples by stir bar sorptive extraction combined with gas chromatography and EI/CI TOF mass spectrometry

Volatile aroma components and contents of organically and conventionally produced apples of the cultivars Elstar, Jonagold, Jonagored and Braeburn were studied. In three cultivars investigated, the aroma contents of organically produced apples were significantly lower (Elstar 16%, Jonagold 29%, Jonagored 68%). For Braeburn, no statistically significant difference was observed. In particular, the main aroma components were present at much lower concentrations in organically produced apples. In all apple cultivars, these were hexanal, trans-2-hexenal, 2-methylbutylacetate and hexylacetate. twenty-three aroma components were identified in total, in different relative ratios in the different apple cultivars: saturated esters, saturated and unsaturated aldehydes and alcohols. Some components identified in the conventionally produced cultivars were not present in the organically produced cultivars at all. The aroma components were extracted from juice freshly prepared from the apples by stir bar sorptive extraction (SBSE) technique and characterised by FID gas chromatography and EI/CI TOF mass spectrometry.     

Two-step binding of green mamba toxin to muscarinic acetylcholine receptor

The mechanism of binding of toxin MT2 from venom of green mamba Dendroaspis angusticeps to muscarinic acetylcholine receptors from rat cerebral cortex was investigated by studying the kinetics of the toxin-receptor interaction. The muscarinic antagonist N-methyl-[3H]scopolamine was used as a 'reporter' ligand. Evidence for a mechanism of toxin-receptor interaction comprising at least two steps was obtained. Such a mechanism increases the potency of the toxin. The first step was fast with no competition between the toxin and the antagonist. The second step was slow with formation of a more stable toxin-receptor complex and inhibition of the antagonist binding. It is proposed that the snake toxin is a muscarinic agonist of slow action.     

Production of biosensors with exchangeable enzyme-containing threads

We introduce a simple method for the construction of biosensors, based on coiling an enzyme-containing, thread-shaped material around a cylindrical signal transducer in the form of winding stairs with a variable length of step and so forming a variable biocatalytic membrane on the sensor surface, which can be easily modified for particular purposes. In the model system, we immobilized glucose oxidase (GO) on a nylon thread, formatted from a sheaf of numerous minor filaments and used as a biorecognition element integrated with a Clark-type oxygen sensor. The immobilized enzyme was evenly distributed throughout the thread, and the activity of the enzyme could be measured in units of length. Appropriate pieces of the enzyme-containing thread with a certain amount of GO could be cut for a definite biosensor or bioreactor. The enzyme amount and substrate diffusion parameters, which together control the sensor's working range and sensitivity, could be changed simultaneously with the change of the length of the thread. Besides glucose oxidase, experiments with other enzymes have confirmed the applicability of the proposed technological solution. Thus, the thread-type matrixes enable one to construct sensors with a required range of work, sensitivity, and selectivity, which can be easily customized within seconds.     

Modulation of [3H]quinpirole binding to dopaminergic receptors by adenosine A2A receptors

Alteration of ligand binding to dopamine D2 receptors through activation of adenosine A2A receptors in rat striatal membranes has been studied by means of kinetic analysis. The binding of dopaminergic agonist [3H]quinpirole to rat striatal membranes was characterized by the constants Kd = 1.50+/-0.09 nM and Bmax = 115+/-2 fmol/mg of protein. The kinetic analyses revealed that the binding had at least two consecutive and kinetically distinguishable steps, the fast equilibrium of complex formation between receptor and agonist (KA = 5.9+/-1.7 nM), followed by a slow isomerization equilibrium (Ki = 0.06). Activation of adenosine A2A receptors by CGS 21680 caused enhancement of the rate [3H]quinpirole binding, altering mainly the formation of the receptor-ligand complexes (KA) as well as the isomerization rate of this complexes (ki), while the deisomerization rate (k[-i]) and the apparent dissociation rate remained unchanged.