Abstract: This invention pertains to methods for using oxalate oxidase in plant pathology. A substantially pure gene encoding the oxalate oxidase enzyme is elucidated. The expression product of the gene which can be stably incorporated into a foreign plant host has a unique profile including a pH optimum of 3.5, a positive heat stability, a single sub-unit of approximately 25 kilodaltons and protease stability. The methodology of this invention exploiting oxalate oxidase for protection against oxalic acid encompasses providing to a plant in need of oxalic acid protection an oxalic acid degrading enzyme in an amount sufficient to protect the plant from the oxalic acid.

Abstract: A method for long term storage of a stable monodispersed aqueous suspension of conidia has been developed. This is based on the use of surfactants in a concentration range significantly higher than expected that is completely compatible with conidia, generally in the range of between 1 and 2% (w/v) in an aqueous suspension of between 0.01 and 50% (w/v) conidia. Fungal propagules (conidia) of entomopathogenic fungi such as M. anisopliae and B. bassiana can be successfully combined with higher than expected concentrations of commercially available anionic surfactants and wetting agents such as dioctyl sulfosuccinates (DSS) salts and derivatives thereof with no apparent negative impact upon either viability or insecticidal activity of the conidia. Other surfactants, dispersants and non-fungicidal materials can be added to the stabilized conidial suspensions without loss of viability, dispersibility, or shelf-life.

Abstract: A process to produce products, in particular polysaccharides, from filamentous fungi, in an immobilized cell bioreactor wherein the fungus is fixed and adheres to the surface of a porous, non-particulate support and aqueous liquid medium is passed through the immobilized system and product containing medium is recycled or withdrawn from the system.

Abstract: An improved method for the purification of ribulose, 1,5-bisphosphate carboxylase (RuBisCO) comprises comminuting and homogenizing a plant material, such as leaves, in an aqueous solution. After fractionation to release the RuBisCO, sufficient polyethylene glycol (PEG) is added to cause crystallization of the RuBisCO. It has been found that treatment of the resulting PEG supernatant first by acidification to remove other proteins, and then by addition of a strong base to remove phosphorylated sugars, allows the recycling of the PEG in the process. Moreover, it is found that the phosphorylated sugars are a valuable by-product, suitable for example as a carbon source for the culture of microorganisms.

Abstract: A method for the purification of ribulose 1,5-bisphosphate carboxylase (RuBisCO) to a greater than 90% purity from a wide variety of plant species is disclosed. The steps include comminuting and homogenizing a plant material, such as leaves, in aqueous solution. The solution is filtered and the residue discarded. After fractionation, sufficient polyethylene glycol (PEG) is added to bring the concentration of PEG in the range of from 8 to 13 (weight/volume) percent, causing precipitation of the RuBisCO. To enhance crystal formation, magnesium chloride can be added to the solution. As a purification step, or as an alternate (to crystallization) separation step, the RuBisCO may be applied to a strong basic ion-exchange resin. The RuBisCO is selectively eluted in the presence of a divalent metal ion, such as Mg.sup.+2, Ca.sup.+2 or Zn.sup.+2.