ABSTRACT
Phosphorus (P) is considered a scarce macronutrient for plants in most tropical soils. The application of rock phosphate (RP) has been used to fertilize crops, but the amount of P released is not always at a necessary level for the plant. An alternative to this problem is the use of Phosphorus Solubilizing Microorganisms (PSM) to release P from chemically unavailable forms. This study compared the P sorption capacity of soils (the ability to retain P, making it unavailable for the plant) and the profile of organic acids (OA) produced by fungal isolates and the in vitro solubilization efficiency of RP. Trichoderma and Aspergillus strains were assessed in media with or without RP and different soils (Andisol, Alfisol, Vertisol). The type and amount of OA and the amount of soluble P were quantified, and according to our data, under the conditions tested, significant differences were observed in the OA profiles and the amount of soluble P present in the different soils. The efficiency to solubilize RP lies in the release of OAs with low acidity constants independent of the concentration at which they are released. It is proposed that the main mechanism of RP dissolution is the production of OAs.
ABSTRACT
The goal of this study was to optimize methyl parathion (O,O-dimethyl-O-4-p-nitrophenyl phosphorothioate) degradation using a strain of Escherichia coli DH5α expressing the opd gene. Our results indicate that this strain had lower enzymatic activity compared to the Flavobacterium sp. ATCC 27551 strain from which the opd gene was derived. Both strains were assessed for their ability to degrade methyl parathion (MP) in a mineral salt medium with or without the addition of glucose either as suspended cells or immobilized on tezontle, a volcanic rock. MP was degraded by both strains with similar efficiencies, but immobilized cells degraded MP more efficiently than cells in suspension. However, the viability of E. coli cells was much higher than that of the Flavobacterium sp. We confirmed the decrease in toxicity from the treated effluents through acetylcholinesterase activity tests, indicating the potential of this method for the treatment of solutions containing MP.
Subject(s)
Aryldialkylphosphatase/genetics , Bacterial Proteins/genetics , Environmental Restoration and Remediation/methods , Escherichia coli/genetics , Escherichia coli/metabolism , Flavobacterium/enzymology , Methyl Parathion/metabolism , Aryldialkylphosphatase/metabolism , Bacterial Proteins/metabolism , Biodegradation, Environmental , Cells, Immobilized/chemistry , Cells, Immobilized/metabolism , Escherichia coli/chemistry , Flavobacterium/genetics , Gene ExpressionABSTRACT
BACKGROUND: Expansins and expansin-like proteins loosen cellulose microfibrils, possibly through the rupture of intramolecular hydrogen bonds. Together with the use of lignocellulolytic enzymes, these proteins are potential molecular tools to treat plant biomass to improve saccharification yields. RESULTS: Here we describe a new type of expansin-related fungal protein that we have called loosenin. Its corresponding gene, loos1, from the basidiomycete Bjerkandera adusta, was cloned and heterologously expressed in Saccharomyces cerevisiae. LOOS1 is distantly related to plant expansins through the shared presence of a DPBB domain, however domain II found in plant expansins is absent. LOOS1 binds tightly to cellulose and chitin, and we demonstrate that cotton fibers become susceptible to the action of a commercial cellulase following treatment with LOOS1. Natural fibers of Agave tequilana also become susceptible to hydrolysis by cellulases after loosenin treatment. CONCLUSIONS: LOOS1 is a new type of protein with disrupting activity on cellulose. LOOS1 binds polysaccharides, and given its enhancing properties on the action of hydrolytic enzymes, LOOS1 represents a potential additive in the production of fermentable sugars from lignocellulose.
