Abstract: Disclosed herein is a novel monoglygeride lipase at least capable of catalyzing an enzymatic reaction of the following equation (a) and as substrate specificity, capable of acting on monoglyceride but incapable of acting on diglyceride and triglyceride:Monoglyceride+H.sub.2 O.fwdarw.Glycerol+Fatty acid (a)The monoglyceride lipase is produced by culturing a specific monoglyceride lipase producing microorganism of Bacillus and then collecting the monoglyceride lipase from the resulting culture. A method is also disclosed for the analysis of a monoglyceride-containing sample solution. The monoglyceride lipase is caused to act on the sample solution upon measurement of the monoglyceride in the sample solution. Either one of glycerol and the fatty acid formed in accordance with the equation (a) is then measured.

Abstract: Reagent for analysis of triglycerides contained in blood serum is provided, which comprises lipases and monoglyceride lipases capable of acting on monoglycerides having substrate specificity and capable of catalyzing the following enzymatic reaction: monoglyceride+H.sub.2 O.fwdarw.glycerol+fatty acids. The glycerol or fatty acids are measured to learn an amount of the triglycerides or fatty acid by any known analytical method.

Abstract: An assay with high sensitivity for activity of lecithin-cholesterol acyltransferase in blood for functional analysis of liver, by bringing the blood into contact with lecithin and free cholesterol until lysolecithin and cholesterol ester are produced, allowing the lysolecithin produced to react with lysophospholipase and glycerophosphocholine phosphodiesterase and assaying glycerol-3-phosphate produced simultaneously or successively in the reaction by means of an enzymatic cycling reaction in which glycerol-3-phosphate, dihydroxyacetone-3-phosphate, nicotinamide adenine dinucleotide (NAD), reduced NAD, O.sub.2, H.sub.2 O.sub.2, glycerophosphate oxidase and glycerophosphate dehydrogenase take part.

Abstract: Ethanolamine in a sample can be assayed by treating the sample with ethanolamine oxidase, thereby to catalyze a reaction-consuming ethanolamine, oxygen and water, and forming glycolaldehyde, ammonia and hydrogen peroxide. The amount of consumed oxygen or the amount of generated ammonia or hydrogen peroxide is then determined, as a measure of the ethanolamine that was originally the sample. The ethanolamine can appear in the sample as such, or can be liberated simultaneously with or prior to the catalysis reaction, from an ethanolamine derivative, e.g. phosphatidyl ethanolamine by the action of phospholipase D. Ethanolamine oxidase can be produced from Bacillus sp. B-0783 FERM-P No. 5798 in a conventional culture medium, preferably by submerged aeration liquid culturation.

Abstract: Disclosed herein is a novel monoglyceride lipase at least capable of catalyzing an enzymatic reaction of the following equation (a) and as substrate specificity, capable of acting on monoglyceride but incapable of acting on diglyceride and triglyceride:(a) Monoglyceride+H.sub.2 O.fwdarw.Glycerol+Fatty acidThe monoglyceride lipase is produced by culturing a specific monoglyceride lipase producing microorganism of Bacillus and then collecting the monoglyceride lipase from the resulting culture. A method is also disclosed for the analysis of a monoglyceride-containing sample solution. The monoglyceride lipase is caused to act on the sample solution upon measurement of the monoglyceride in the sample solution. Either one of glycerol and the fatty acid formed in accordance with the equation (a) is then measured.

Abstract: A novel bilirubin oxidase is provided having a substrate specificity for bilirubin but not to, at least, biliverdin, catechol and hemin and which catalyzes the enzyme reaction between two moles of bilirubin and one mole of oxygen to yield two moles of biliverdin and two moles of water. A process is also provided for the production of said novel bilirubin oxidase, which comprises cultivating a bilirubin oxidase-producing fungus of the genus Penicillium in a culture medium and collecting the bilirubin oxidase from the culture mixture. A method of determining the content of bilirubin in a sample to be analyzed is further provided which comprises contacting the sample with the bilirubin oxidase to convert bilirubin in the sample into biliverdin and determining the amount of biliverdin formed or the amount of oxygen consumed therefor, as well as a method for removing bilirubin contained in a sample to be analyzed, which comprises contacting the sample with said novel bilirubin oxidase.

Abstract: A novel NAD synthetase is produced by culturing a broth of Bacillus stearothermophilus H-804 FERM BP-1408. This new enzyme selectively catalyzes the reaction ##STR1## without catalyzing the reaction ##STR2## The enzyme uses ammonia or ammonium ion as a substrate, but does not use either glutamine or asparagine. Also disclosed is an assay method using the enzyme, for any one of ATP, deamide-NAD, ammonia or ammonium ion in a specimen to be assayed.

Abstract: Glucose dehydrogenase having the following biochemial properties:(a) enzymatic action: catalyzes a reaction which generates glucono-.delta.-lactone and reduced NADP from glucose and NADP;(b) substrate specificity: has substrate specificity on glucose and no substrate specificity on 2-deoxyglucose;(c) optimum pH: pH 6-8,(d) optimum temperature: approximately 55.degree. C.,(e) pH-stability: stable at pH 6.0-7.5,(f) molecular weight: 11.times.10.sup.4 .+-.11000,(g) Km-value: 2.6.times.10.sup.-3 .+-.2.6.times.10.sup.-4 M(glucose) 4.2.times.10.sup.-6 35 4.2.times.10.sup.-7 M(NADP) and(h) isoelectric point: 4.9.+-.0.5,comprises culturing a glucose dehydrogenase-producing microorganism Cryptococcus uniguttulatus Y 0033 FERM P-8709, now FERM BP-1352 in a nutrient medium and isolating glucose dehydrogenase thus produced from the cultured medium.

Abstract: A composition and method for lipase assay, comprising the use of an aqueous solution of a 1,2-diglyceride of a higher fatty acid, and a nonionic surface active agent. The higher fatty acid is a higher fatty acid of 8 or more and preferably 12 or more carbons, most preferably a higher unsaturated fatty acid of more than 16 carbons. The concentration of 1,2-diglyceride is more than 0.5 g per liter of solution. The nonionic surface active agent is a polyoxyethylene-type nonionic surface active agent, a polyhydric-alcohol-type nonionic surface active agent or a block-polymer-type nonionic surface active agent, whose concentration is more than 0.1% by weight in the composition and which has an HLB more than 10. The composition preferably contains 0.5-10 g of 1,2-diglyceride and 10-50 g of nonionic surface active agent per liter of solution.

Abstract: Ethanolamine in a sample can be assayed by treating the sample with ethanolamine oxidase, thereby to catalyze a reaction-consuming ethanolamine, oxygen and water, and forming glycolaldehyde, ammonia and hydrogen peroxide. The amount of consumed oxygen or the amount of generated ammonia or hydrogen peroxide is then determined, as a measure of the ethanolamine that was originally the sample. The ethanolamine can appear in the sample as such, or can be liberated simultaneously with or prior to the catalysis reaction, from an ethanolamine derivative, e.g. phosphatidyl ethanolamine by the action of phospholipase D. Ethanolamine oxidase can be produced from Bacillus sp. B-0783 FERM-P No. 5798 in a conventional culture medium, preferably by submerged aeration liquid culturation.

Abstract: Thermostable bilirubin oxidase having substrate specificity to at least bilirubin and capable of catalyzing a reaction in which biliverdin and water are formed from bilirubin and oxygen. It can be produced by culturing a bilirubin oxidase producing micro-organism belonging to the genus Bacillus, for example, Bacillus licheniformis and then preparing the resultant bilirubin oxidase from the cultured broth.

Abstract: The invention is to provide a method for the production of sphingomyelinase, by culturing in a medium a sphingomyelinase-producing strain belonging to genus Streptomyces and collecting the resulting sphingomyelinase from the cultured medium. The strain, Streptomyces sp. A 9107, newly separated from a soil, is found preferable for the method of the present invention, and has been deposited as NRRL 15100 and FERM-P 4978.

Abstract: An enzyme having enoyl-CoA hydratase activity, 3-hydroxyacyl-CoA dehydrogenase activity and 3-ketoacyl-CoA thiolase activity, all in the same enzyme, is produced by culturing the microorganism strain Pseudomonas fragi B-0771 FERM-P No. 5701, and isolating the enzyme thus produced from the culture medium. Such an enzyme is useful in an assay method for a fatty acid component in a sample, which fatty acid is originally present in the sample or is liberated from a fatty acid ester in the sample, comprising:(a) converting the fatty acid to acyl-CoA;(b) converting the thus-produced acyl-CoA to dehydroacyl-CoA;(c) converting the thus-produced dehydroacyl-CoA to hydroxyacyl-CoA;(d) converting the thus-produced hydroxyacyl-CoA to ketoacyl-CoA;(e) converting the thus-produced ketoacyl-CoA to acyl-CoA; and measuring the detectable changes in the reaction mixture.

Abstract: A novel glycerol kinase is produced from the microorganism Streptomyces canus FERM-P No. 4977 and is useful as a diagnostic reagent for assay of triglycerides and glycerol in body fluids such as serum.

Abstract: A process for the production of acyl-Coenzyme A oxidase, comprises culturing an acyl-Coenzyme A-oxidase-producing microorganism belonging to genus Macrophomina, genus Cladosporium, genus Aspergillus, genus Monascus, genus Saccharomyces or genus Arthrobacter in a nutrient medium, and isolating the thus-formed acyl-CoA oxidase therefrom. The preferred species of microorganism are Macrophomina phaseoli ATCC 14383, Cladosporium resinae IFO 6367, Aspergillus candidus M-4815 FERM-P No. 5226, Monascus sp. M-4800 FERM-P No. 5225, Saccharomyces cerevisiae Y 0036 FERM-P No. 5174, and Arthrobacter sp. B-720 FERM-P No. 5224, respectively.

Abstract: A novel enzyme choline oxidase is produced by culturing a microorganism belonging to the genus Arthrobacter, and particularly the species Arthrobacter globiformis B-0577 FERM-P No. 3518, NRRL B-11097, and isolating the choline oxidase thus produced from the culture medium. Choline oxidase is useful for the determination of choline or betaine aldehyde in a sample by mixing the new product with the sample and then measuring the generated hydrogen peroxide, betaine or consumed oxygen.