Biomineralization of 2,3,4,6-Tetrachlorophenol by Bacillus sp. and Staphylococcus sp. Isolated from Secondary Sludge of Pulp and Paper Mill

Three 2,3,4,6-tetrachlorophenol (2,3,4,6-TeCP)-mineralizing bacteria were isolated from the secondary sludge of a pulp and paper industry. The isolates used 2,3,4,6-TeCP as a source of carbon and energy and were capable of degrading this compound, as indicated by stoichiometric release of chloride and biomass formation. Based on 16S rRNA gene sequence analysis, the bacteria were identified as Bacillus megaterium (CL3), Staphylococcus suciri (CL10), and Bacillus thuringensis (CL11). High-performance liquid chromatography (HPLC) analysis revealed that these isolates were able to degrade 2,3,4,6-TeCP at higher concentrations (600 mg/L or 2.5 mM). A consortia of the isolates completely removed 2,3,4,6-TeCP from the sludge obtained from a pulp and paper mill within 2 weeks when supplemented at a rate of 100 mg/L or 0.43 mM. A bacterial consortium also significantly reduced absorbable organic halogen (AOX) and extractable organic halogen (EOX) by 63% and 68%, respectively, from the sludge. These isolates have a high potential to remove 2,3,4,6-TeCP and may be used for remediation of pulp paper mill waste containing 2,3,4,6-TeCP.     

Biosynthesis and Genetic Engineering of Lignin

Lignin, a complex heteropolymer of cinnamyl alcohols, is, second to cellulose, the most abundant biopolymer on Earth. Lignification has played a determining role in the adaptation of plants to terrestrial life. As all extracellular polymers, lignin confers rheological properties to plant tissues and participates probably in many other functions in cell and tissue physiology orin cell-to-cell communication. Economically, lignin is very important because it determines wood quality and it affects the pulp and paper-making processes as well as the digestibility of forage crops. For all these reasons the lignin biosynthesis pathway has been the subject of many studies. At present, most genes encoding the enzymes involved in the biosynthesis of lignin have been cloned and characterized. Various recent studies report on the alteration of the expression of these genes by genetic engineering, yielding plants with modified lignin. In addition, several mutants have been analyzed with changes in lignin content or lignin composition resulting in altered properties. Thanks to these studies, progress in the knowledge of the lignin biosynthesis pathway has been obtained. It is now clear that the pathway is more complex than initially thought and there is evidence for alternative pathways. A fine manipulation of the lignin content and/or composition in plants is now achievable and could have important economical and environmental benefits.     

Identification of a procarboxypeptidase A-truncated protease E binary complex in human pancreatic juice

The characterization, in human pancreatic juice, of a binary complex associating procarboxypeptidase A with a 32 kDa inactive glycoprotein (G32) is reported in this paper. Free G32 was isolated after dissociation of the binary complex. N-terminal sequence analysis revealed a complete homology between this protein and human protease E (HPE 1), except for the two strongly hydrophobic N-terminal residues (Val-Val) which are missing in G32. This protein might be a truncated protease E highly analogous to the subunit III of the ruminant procarboxypeptidase A-S6 ternary complex. The analogy with bovine subunit III is further supported by interspecies reassociation experiments showing that bovine procarboxypeptidase A can specifically bind human G32.     

Catalytic DNA and RNA for Targeting MDR1 mRNA

Abstract

Design, synthesis and properties of catalytic NAs for targeting MDR1 mRNA are reported.     

A biomolecular recognition approach for the functionalization of cellulose with gold nanoparticles

Materials with new and improved functionalities can be obtained by modifying cellulose with gold nanoparticles (AuNPs) via the in situ reduction of a gold precursor or the deposition or covalent immobilization of pre‐synthesized AuNPs. Here, we present an alternative biomolecular recognition approach to functionalize cellulose with biotin‐AuNPs that relies on a complex of 2 recognition elements: a ZZ‐CBM3 fusion that combines a carbohydrate‐binding module (CBM) with the ZZ fragment of the staphylococcal protein A and an anti‐biotin antibody. Paper and cellulose microparticles with AuNPs immobilized via the ZZ‐CBM3:anti‐biotin IgG supramolecular complex displayed an intense red color, whereas essentially no color was detected when AuNPs were deposited over the unmodified materials. Scanning electron microscopy analysis revealed a homogeneous distribution of AuNPs when immobilized via ZZ‐CBM3:anti‐biotin IgG complexes and aggregation of AuNPs when deposited over paper, suggesting that color differences are due to interparticle plasmon coupling effects. The approach could be used to functionalize paper substrates and cellulose nanocrystals with AuNPs. More important, however, is the fact that the occurrence of a biomolecular recognition event between the CBM‐immobilized antibody and its specific, AuNP‐conjugated antigen is signaled by red color. This opens up the way for the development of simple and straightforward paper/cellulose‐based tests where detection of a target analyte can be made by direct use of color signaling.