Validation of Methods for Determination of Metabolic Rate in the Edholm Scale and ISO 8996

The aim of this study was to validate the Edholm scale (Edholm, 1966) and the ISO 8996 standard (International Organization for Standardization [ISO], 1990) by comparing the metabolic rates estimated for both methods with the actual measured metabolic rate (MMeas) in 6 manual material handling tasks simulated under laboratory conditions. The metabolic rate was calculated from oxygen consumption V˙ O2 (19 participants) according to Standard No. ISO 8996 (ISO, 1990). Additionally, the participants estimated perceived exertion using the Borg scale. The metabolic rates derived from the Edholm scale (MEdh) overestimated 5 of 6 activities by 34–50% (< =.05). The metabolic rates derived from ISO 8996 (MISO) overestimated all activities by 7–38% (< =.05)

ALD/MLD fabrication of luminescent Eu-organic hybrid thin films using different aromatic carboxylic acid components with N and O donors

The research leading to these results has received funding from the European Research Council under the European Union's Seventh Framework Programme (FP/2007-2013) / ERC Grant Agreement n. 339478. Acronym LAYERENG-HYBMAT. | openaire: EC/FP7/339478/EU/LAYERENG-HYBMATAtomic/molecular layer deposition (ALD/MLD) processes based on Eu(thd)3 and three different aromatic organic acids with O and N donors as precursors are systematically investigated for the growth of Eu-based inorganic-organic thin-film phosphors. For all the acid precursors evaluated, i.e. 1,4-dicarboxylic, 3,5-pyridinedicarboxylic and 2,6-pyridinedicarboxylic acids, conditions are found to produce high-quality hybrid thin films through self-saturating gas-solid reactions as expected for an ideal ALD/MLD process. The resultant Eu-organic thin films show intense red photoluminescence. The luminescence characteristics depend on the manner the organic ligands are bound to Eu3+; this is discussed based on FTIR, XPS, UV-vis and fluorescence spectroscopy data measured for the films.Peer reviewe

High activity catechol 1,2-dioxygenase from Stenotrophomonas maltophilia strain KB2 as a useful tool in cis,cis-muconic acid production

This is the first report of a catechol 1,2-dioxygenase from Stenotrophomonas maltophilia strain KB2 with high activity against catechol and its methyl derivatives. This enzyme was maximally active at pH 8.0 and 40 °C and the half-life of the enzyme at this temperature was 3 h. Kinetic studies showed that the value of K(m) and V(max) was 12.8 μM and 1,218.8 U/mg of protein, respectively. During our studies on kinetic properties of the catechol 1,2-dioxygenase we observed substrate inhibition at >80 μM. The nucleotide sequence of the gene encoding the S. maltophilia strain KB2 catechol 1,2-dioxygenase has high identity with other catA genes from members of the genus Pseudomonas. The deduced 314-residue sequence of the enzyme corresponds to a protein of molecular mass 34.5 kDa. This enzyme was inhibited by competitive inhibitors (phenol derivatives) only by ca. 30 %. High tolerance against condition changes is desirable in industrial processes. Our data suggest that this enzyme could be of use as a tool in production of cis,cis-muconic acid and its derivatives