Copper molybdate synthesized by sonochemistry route at room temperature as an efficient solid catalyst for esterification of oleic acid.

Copper molybdate nanoplates were synthesized by a sonochemical process at room temperature, which we report as a simple and cost-effective route. Structural analysis of the material by the Rietveld method of X-ray diffraction (XRD) data revealed lindgrenite Cu3(MoO4)2(OH)2 in a single-phase structure. All the vibrational modes characteristic of the space group were identified by Raman vibrational and near-infrared (NIR) spectroscopies. The profile obtained for N2 adsorption/desorption was type III hysteresis, characteristic of mesoporous materials, with a surface area of 70.77(1) m2 g-1. The micrographs of the material obtained by scanning electron microscopy showed nanoplates with nanometric sizes and an anisotropic growth aspect. The catalytic activity of lindgrenite was evaluated by esterifying oleic acid with methanol, showing high conversion rate to methyl oleate and good catalyst stability after seven recycling cycles. Above all, the best catalytic performance was reached when we optimized parameters such as oleic acid:methanol molar ratio of 1:5, 5% of catalyst dosage, and reaction time of 5 h, resulting in 98.38% of conversion at 413 K. Therefore, sonochemically synthesized lindgrenite proved to be a high potential material for biofuel production by oleic acid esterification.

MRNA encoding a putative RNA helicase of the DEAD-box gene family is up-regulated in trypomastigotes of Trypanosoma cruzi.

Differential display of mRNAs from Trypanosoma cruzi epimastigote and metacyclic trypomastigote stages showed several mRNA species differing in their expression level. The cDNA corresponding to one of these mRNAs was used as a probe in Northern blots and identified a RNA product of 2.6 kb with an expression level eight or more times higher in trypomastigotes than in epimastigotes. This probe was also used to screen a genomic library of T. cruzi CL Brener clone prepared in lambda FIX. A clone of about 15 kb was selected that, after partial sequencing, revealed an open reading frame of 688 amino acids encoding a deduced protein with similarity to RNA helicases of the DEAD-box gene family. The presence of the eight conserved motifs characteristic of the DEAD protein family was observed in the T. cruzi sequence, indicating that it corresponds to a putative RNA helicase gene, which we named HelTc. Southern blot analysis indicated that HelTc is a single-copy gene. Pulsed-field gel electrophoresis separation of chromosomes of several isolates of T. cruzi showed that this gene was localized in one or two chromosomal bands.

Structural characterization and promoter activity analysis of the gamma-kafirin gene from sorghum.

A genomic clone encoding the gamma-kafirin gene from sorghum was isolated and sequenced. A 2938 bp sequenced fragment includes an intronless open reading frame of 636 nucleotides encoding a putative polypeptide of 212 amino acids. Comparison of the deduced amino acid sequence of gamma-kafirin with the published sequences of gamma-prolamins of maize, and Coix revealed highly conserved domains. The N-terminal region of these proteins contains the conserved hexapeptide PPPVHL, which is repeated eight times in gamma-zein, four times in gamma-kafirin and three times in gamma-coixin. The number of PPPVHL repeats accounts predominantly for the differences in the molecular weights of gamma-prolamins. Several putative regulatory sequences common to the gamma-kafirin and gamma-zein genes were identified in both the 5' and the 3' flanking regions. Putative GCN4-like regulatory sequences were found at positions -192 and -476 in the 5' flanking region of gamma-kafirin. In the 3' noncoding region, three putative polyadenylation signals, two AATAAT and one AATGAA, were found at positions +658, +716, and +785, respectively. In order to investigate the role of the putative GCN4-like motifs and other possible cis-acting element(s) of the gamma-kafirin promoter, a series of deleted and chimeric promoter constructs were introduced into maize, Coix and sorghum tissues by particle bombardment. Histochemical analysis of beta-glucuronidase (GUS) activity in different tissues indicated that the element(s) responsible for tissue specificity is probably located in the 285-bp proximal region of the promoter, while the remaining promoter sequence seems to carry the element(s) responsible for the quantitative response.