Toyo Jozo Kabushiki Kaisha

Toyo Jozo Company, Ltd.

Asahi Kasei Kogyo Kabushiki Kaisha

Fuji Spinning Co., Ltd.

Toyo Yozo Company, Ltd.

Shigeyuki Imamura

Hideo Misaki

Kazuo Matsuura

Mamoru Takahashi

Naoki Muto

Masaki Takada

Kenya Ishizawa

Shigeru Ikuta

Shigeru Ueda

Hidehiko Ishikawa

Yoshihide Kawamura

Hiroaki Tanibe

Yoshifumi Horiuchi

Eiichi Yoshino

Tohru Matsumoto

Mamoru Takahasi

Junko Harada

An enzyme immobilizing carrier is produced by dissolving low-molecular weight chitosan in an aqueous acid solution and dropping the solution into a basic solution to produce regenerated porous chitosan in particles, reacting the regenerated porous chitosan in particles with the glycidyl ether of an aliphatic polyalcohol, and reacting further the resulting chitosan with the acid halide or acid anhydride of a higher fatty acid in a polar organic solvent. An enzyme and a polyfunctional cross-linking agent are reacted with the carrier to covalently immobilize the enzyme on the carrier. In a preferred embodiment, the enzyme is lipase and the carrier is produced by introducing the glycidyl ether of an aliphatic polyalcohol at 0.01 to 0.4 mole to 1 mole of the pyranose ring residue of the chitosan and by introducing a higher fatty acid having a total carbon number of 6 to 20 at 0.05 to 1 mole to 1 mole of the pyranose ring residue of the chitosan.

Lipase immobilized on a chitosan carrier

Myo-inositol in a specimen is assayed by reacting a specimen containing myo-inositol with:

Highly sensitive assay method for myo-inositol, composition for

A novel .omega.-carboxyalcohol oxidase catalyzes at least one of the following reactions:

Omega carboxyalcohol oxidase enzyme

A method for assaying aliphatic alcohol, aliphatic aldehyde or .omega.-carboxylic acid derivatives thereof, using a novel .omega.-carboxyalcohol oxidase which catalyzes at least one of the following reactions:

Method for assaying aliphatic alcohol, aliphatic aldehyde or

Omega-carboxyalcohol oxidase

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:

Analytical method making use of monoglyceride lipase

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.

Reagent for analysis of triglycerides and analysis using the same

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.

Assay method for lecithin-cholesterol acyltransferase

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.

Assay method for phosphatidyl ethanolamine

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:

Novel monoglyceride lipase and its production process.

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.

Novel bilirubin oxidase which has a substrate specifity to bilirubin,

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.

Novel NAD synthetase, assay method using said novel NAD synthetase and a

Glucose dehydrogenase having the following biochemial properties:

Glucose dehydrogenase and its production

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.

Growing community of inventors

Shizuoka, Japan

Shigeyuki Imamura