Abstract: A process for the production of amine oxidase, which comprises culturing an amine-oxidase-producing microorganism belonging to the genus Talaromyces, genus Eupenicillium, genus Petromyces, genus Neosartorya or genus Eurotium, and isolating the thus-prepared amine oxidase from the cultured medium. The preferred strains of microorganisms under these genera are Talaromyces flavus var. flavus M 4175 FERM-P No. 5866, Eupenicillium parvum M 5051 FERM-P No. 5870, Petromyces alliaceus M 4648 FERM-P No. 5867, Neosaytorya fischeri M 4690 FERM-P No. 5868 and Eurotium chevalieri M 4805 FERM-P No. 5869.

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.

Abstract: Thermophilic aspartase is produced by culturing a microorganism belonging to the genus Bacillus. The enzyme is useful as a catalyst in the production of L-aspartic acid from ammonium fumarate or a mixture of fumaric acid and ammonia.

Abstract: Described herein is a process for isolating the enzymatic protein ribulose 1,5-diphosphate carboxylase from the green leaves of plants. In the process, which is particularly suited to obtaining the protein from tobacco, the leaves are ground or otherwise pulverized in the presence of a reducing agent. A liquid portion containing the desired protein is separated from the pulp and its pH adjusted to within the range of from about pH 6.0 to 5.3 and then cooled to cause the crystallization of the ribulose 1,5-diphosphate carboxylase. After separation of the crystalline material, the supernatant is acidified to yield lower molecular weight proteins.

Abstract: Heparinase is produced by growing the bacteria, Flavobacterium heparinum, in a defined medium consisting of a carbon source, two or more amino acids and mineral salts in the absence of protein. Heparinase is recovered by batch chromatography of the cell extract from hydroxylapatite by elution with sodium chloride and sodium phosphate buffer washes.

Abstract: Various enzymes, in particular Cu,Zn-superoxide dismutase (SOD), catalase and carbonic acid anhydrase, are recovered from blood by admixing wholly or partly isolated blood cells with ethanol or a homologous alcohol until a concentration of 10 to 70% by volume and allowing them to stand for hemolysis of the blood cells and denaturation of the hemoglobin, and then adding water up to the double volume or more, and removing the precipitate of cell residuals, hemoglobin and other denatured proteins from the suspension. Then the desired enzymes are isolated from the solution obtained.In particular, SOD and catalase can both be isolated by chromatography of the solution at a pH of 4.7 to 5.5 on a cation exchange resin of the same polarity as SOD in the pH range used and elution of the resin with a buffer solution which has a pH in the range 4.7 to 7.5 and an ionic strength in the range 0.01 to 1.0 M, SOD being eluted at the lowest pH and/or the lowest ionic strength.

Abstract: Fraction I protein from plant leaves is purified and subsequently crystallized. The crystallization methods disclosed herein unexpectedly produce crystallization in all crop leaves examined, although for some species modification by salt addition is required to achieve crystallization and to prevent formation of substantial percentages of amorphous protein precipitates. It has been found that a fraction I protein solution, when mixed with a precipitant solution having a pH generally within the range of 4.8-7.2, in an amount and at a pH sufficient to provide a mixed solution (protein solution mixed with precipitant solution) having a final pH in the range of 6.6-7.0, causes crystallization of fraction I protein from plant leaves, provided that the precipitant solution is at a pH lower than the pH of the protein solution. Optimum results have been obtained when the pH of the precipitant solution is in the range of 5.0 to 6.0 and the protein solution in the range of 7.0 to 7.5.

Abstract: A single, simple, uniform protocol for the rapid large scale purification and crystallization of ribulose 1,5-bisphosphate carboxylase (RuBisCO) to a greater than 90% purity from a wide variety of plant species, involving the steps of grinding and homogenizing plant material, such as leaves, with a suitable, acqueous buffer solution. The solution is filtered and the residue discarded. While maintaining temperature and pH control, sufficient quantities of polyethylene glycol (PEG) are added while stirring to bring the final concentration of PEG in the range of 8 to 15 (weight/volume) percent. To enhance crystal formation, magnesium chloride can be added to the solution. The precipitated material is discarded and the pure RuBisCO crystals which separate out of the remaining supernatant are collected, washed, dried and stored.

Abstract: Strain UK 788 (FERM-P No. 5141) that belongs to Bacillus stearothermophilus, the cell of which is longer than about 10 microns and which permits easier release of intracellular components than a type culture Bacillus stearothermophilus, IAM 11001 is disclosed. Also, a process for producing a useful enzyme selected from the group consisting of a heat-resistant polynucleotide phosphorylase, heat-resistant maleate dehydrogenase, heat-resistant glucokinase, heat-resistant glucose-6-phosphate dehydrogenase and heat-resistant pyruvate kinase by culturing such UK 788 and recovering the desired enzyme from the culture is disclosed. Since the cell of the strain UK 788 is easy to settle and its membrane is also easy to break, the useful enzymes mentioned above can be efficiently produced on an industrial scale.

Abstract: A process for producing L-aspartic acid economically and efficiently from fumaric acid or a salt thereof and ammonia or an ammonium salt using a cultured product obtained by aerobically culturing an microorganism belonging to the Genus Brevibacterium and having resistance to .alpha.-amino-n-butyric acid.

Abstract: Described herein is a process for isolating the enzymatic protein ribulose 1,5-diphosphate carboxylase from the green leaves of plants. In the process, which is particularly suited to obtaining the protein from tobacco, the leaves are ground or otherwise pulverized in the presence of a reducing agent, followed by heating the resulting pulp to about 50.degree. C. A liquid portion containing the desired protein is separated from the pulp and then cooled to cause the crystallization of the ribulose 1,5-diphosphate carboxylase. After separation of the crystalline material, the supernatant is acidified to yield lower molecular weight proteins.

Abstract: Phenylalanine level in blood or another medium is considerably reduced and can even be annulled by causing blood or the other medium to flow through a mass of porous fibers in which the enzyme phenylalanine ammonia lyase has been occluded: the fibers have been previously made biocompatible, if necessary.

Abstract: A novel methylguanidine-decomposing enzyme can be obtained by cultivating in a medium a bacterium belonging to Genus Alcaligenes and having an ability to produce a methylguanidine-decomposing enzyme. This methylguanidine-decomposing enzyme has an ability to decompose methylguanidine into methylamine and urea. Its optimum pH range is 10.9-12.3 and its stable pH range is 5.0-10.6.

Abstract: A method is described for the manufacture of epoxides or glycols from olefins. An olefin is contacted with a reaction mixture of a halogenating enzyme, an oxydizing agent and a halide ion source, for a sufficient period to convert the olefin to a halohydrin. The halohydrin is then converted to an epoxide or glycol.