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Multiple Substrates (multiple + substrate)
Selected AbstractsTurnover of labile and recalcitrant soil carbon differ in response to nitrate and ammonium deposition in an ombrotrophic peatlandGLOBAL CHANGE BIOLOGY, Issue 8 2010PAULINE M. CURREY Abstract The effects of 4 years of simulated nitrogen deposition, as nitrate (NO3,) and ammonium (NH4+), on microbial carbon turnover were studied in an ombrotrophic peatland. We investigated the mineralization of simple forms of carbon using MicroRespÔ measurements (a multiple substrate induced respiration technique) and the activities of four soil enzymes involved in the decomposition of more complex forms of carbon or in nutrient acquisition: N -acetyl-glucosaminidase (NAG), cellobiohydrolase (CBH), acid phosphatase (AP), and phenol oxidase (PO). The potential mineralization of labile forms of carbon was significantly enhanced at the higher N additions, especially with NH4+ amendments, while potential enzyme activities involved in breakdown of more complex forms of carbon or nutrient acquisition decreased slightly (NAG and CBH) or remained unchanged (AP and PO) with N amendments. This study also showed the importance of distinguishing between NO3, and NH4+ amendments, as their impact often differed. It is possible that the limited response on potential extracellular enzyme activity is due to other factors, such as limited exposure to the added N in the deeper soil or continued suboptimal functioning of the enzymes due to the low pH, possibly via the inhibitory effect of low phenol oxidase activity. [source] Differentiation-dependent association of phosphorylated extracellular signal-regulated kinase with the chromatin of osteoblast-related genesJOURNAL OF BONE AND MINERAL RESEARCH, Issue 1 2010Yan Li Abstract The ERK/MAP kinase pathway is an important regulator of gene expression and differentiation in postmitotic cells. To understand how this pathway controls gene expression in bone, we examined the subnuclear localization of P-ERK in differentiating osteoblasts. Induction of differentiation was accompanied by increased ERK phosphorylation and expression of osteoblast-related genes, including osteocalcin (Bglap2) and bone sialoprotein (Ibsp). Confocal immunofluorescence microscopy revealed that P-ERK colocalized with the RUNX2 transcription factor in the nuclei of differentiating cells. Interestingly, a portion of this nuclear P-ERK was directly bound to the proximal promoter regions of Bglap2 and Ibsp. Furthermore, the level of P-ERK binding to chromatin increased with differentiation, whereas RUNX2 binding remained relatively constant. The P-ERK-chromatin interaction was seen only in RUNX2-positive cells, required intact RUNX2-selective enhancer sequences, and was blocked with MAPK inhibition. These studies show for the first time that RUNX2 specifically targets P-ERK to the chromatin of osteoblast-related genes, where it may phosphorylate multiple substrates, including RUNX2, resulting in altered chromatin structure and gene expression. © 2010 American Society for Bone and Mineral Research [source] Removal of TEX vapours from air in a peat biofilter: influence of inlet concentration and inlet loadJOURNAL OF CHEMICAL TECHNOLOGY & BIOTECHNOLOGY, Issue 3 2006Carmen Gabaldón Abstract This paper presents the results of the study of the removal of toluene, ethylbenzene, and o -xylene (TEX) by biofiltration using a commercial peat as filter-bed material. Runs with a single organic compound in air, and with the mixture of TEX in air, were carried out for at least 55 days in laboratory-scale reactors inoculated with a conditioned culture. The influence of organic compound inlet load and of gas flow rate on the biofilter's performance was studied, including relatively high values of pollutant inlet concentration (up to 4.3 gC m,3 for ethylbenzene, 3.2 gC m,3 for toluene, and 2.7 gC m,3 for o -xylene). Results obtained show maximum elimination capacities of 65 gC m,3 h,1 for o-xylene, 90 gC m,3 h,1 for toluene, and 100 gC m,3 h,1 for ethylbenzene, and high removal efficiency (>90%) even for moderately elevated concentrations: 3.0, 2.5 and 1.8 gC m,3 for ethylbenzene, toluene and o -xylene, respectively. The behaviour of the TEX mixture was in good agreement with the results obtained for the runs in which only one organic compound was present. Ethylbenzene and toluene are degraded easier than o -xylene, and inhibitory effects due to the presence of multiple substrates were not observed. Copyright © 2005 Society of Chemical Industry [source] Peroxisomal alanine : glyoxylate aminotransferase (AGT1) is a photorespiratory enzyme with multiple substrates in Arabidopsis thalianaTHE PLANT JOURNAL, Issue 5 2001Aaron H. Liepman Summary At least two glyoxylate aminotransferases are hypothesized to participate in the steps of photorespiration located in peroxisomes. Until recently, however, genes encoding these enzymes had not been identified. We describe the isolation and characterization of an alanine : glyoxylate aminotransferase (AGT1, formerly AGT) cDNA from Arabidopsis thaliana. Southern blot analysis confirmed that Arabidopsis AGT1 is encoded by a single gene. Homologs of this class IV aminotransferase are also known in other plants, animals, and methylotrophic bacteria, suggesting an ancient evolutionary origin of this enzyme. AGT1 transcripts were present in all tissues of Arabidopsis, but were most abundant in green, leafy tissues. Purified, recombinant Arabidopsis AGT1 expressed in Escherichia coli catalyzed three transamination reactions using the following amino donor : acceptor combinations: alanine : glyoxylate, serine : glyoxylate, and serine : pyruvate. AGT1 had the highest specific activity with the serine : glyoxylate transamination, and apparent Km measurements indicate that this is the preferred in vivo reaction. In vitro import experiments and subcellular fractionations localized AGT1 to peroxisomes. Sequence analysis of the photorespiratory sat mutants revealed a single nucleotide substitution in the AGT1 gene from these plants. This transition mutation is predicted to result in a proline-to-leucine substitution at residue 251 of AGT1. When this mutation was engineered into the recombinant AGT1 protein, enzymatic activity using all three donor : acceptor pairs was abolished. We conclude that Arabidopsis AGT1 is a peroxisomal photorespiratory enzyme that catalyzes transamination reactions with multiple substrates. [source] Reduction of a set of elementary modes using yield analysisBIOTECHNOLOGY & BIOENGINEERING, Issue 2 2009Hyun-Seob Song Abstract This article proposes a new concept termed "yield analysis" (YA) as a method of extracting a subset of elementary modes (EMs) essential for describing metabolic behaviors. YA can be defined as the analysis of metabolic pathways in yield space where the solution space is a bounded convex hull. Two important issues arising in the analysis and modeling of a metabolic network are handled. First, from a practical sense, the minimal generating set spanning the yield space is recalculated. This refined generating set excludes all the trivial modes with negligible contribution to convex hull in yield space. Second, we revisit the problem of decomposing the measured fluxes among the EMs. A consistent way of choosing the unique, minimal active modes among a number of possible candidates is discussed and compared with two other existing methods, that is, those of Schwartz and Kanehisa (Schwartz and Kanehisa, 2005. Bioinformatics 21: 204,205) and of Provost et al. (Provost et al., 2007. Proceedings of the 10th IFAC Symposium on Computer Application in Biotechnology, 321,326). The proposed idea is tested in a case study of a metabolic network of recombinant yeasts fermenting both glucose and xylose. Due to the nature of the network with multiple substrates, the flux space is split into three independent yield spaces to each of which the two-staged reduction procedure is applied. Through a priori reduction without any experimental input, the 369 EMs in total was reduced to 35 modes, which correspond to about 91% reduction. Then, three and four modes were finally chosen among the reduced set as the smallest active sets for the cases with a single substrate of glucose and xylose, respectively. It should be noted that the refined minimal generating set obtained from a priori reduction still provides a practically complete description of all possible states in the subspace of yields, while the active set covers only a specific set of experimental data. Biotechnol. Bioeng. 2009;102: 554,568. © 2008 Wiley Periodicals, Inc. [source] Kinetic Study of the Conversion of Different Substrates to Lactic Acid Using Lactobacillus bulgaricusBIOTECHNOLOGY PROGRESS, Issue 3 2000Concepción N. Burgos-Rubio Lactic acid fermentation includes several reactions in association with the microorganism growth. A kinetic study was performed of the conversion of multiple substrates to lactic acid using Lactobacillusbulgaricus. Batch experiments were performed to study the effect of different substrates (lactose, glucose, and galactose) on the overall bioreaction rate. During the first hours of fermentation, glucose and galactose accumulated in the medium and the rate of hydrolysis of lactose to glucose and galactose was faster than the convesion of these substrates. Once the microorganism built the necessary enzymes for the substrate conversion to lactic acid, the conversion rate was higher for glucose than for galactose. The inoculum preparation was performed in such a way that healthy young cells were obtained. By using this inoculum, shorter fermentation times with very little lag phase were observed. The consumption patterns of the different substrates converted to lactic acid were studied to determine which substrate controls the overall reaction for lactic acid production. A mathematical model (unstructured Monod type) was developed to describe microorganism growth and lactic acid production. A good fit with a simple equation was obtained. It was found experimentally that the approximate ratio of cell to substrate was 1 to 10, the growth yield coefficient (YXS) was 0.10 g cell/g substrate, the product yield (YPS) was 0.90 g lactic acid/g substrate, and the , parameter in the Luedeking-Piret equation was 9. The Monod kinetic parameters were obtained. The saturation constant (KS) was 3.36 g/L, and the specific growth rate (,m ) was 1.14 l/h. [source] | ||||||||||