Abstract: A varistor includes a varistor element, a first layer which is porous on the varistor element, and a second layer on th first coating. The thickness t (mm) of the second layer is not smaller than 1.3/V. where V(ml/g) is the volume of pores of the first layer exposed to an outside of the first layer. This varistor includes the outer layers protected from being broken even when a non-ohmic interface in a voltage non-linear resistor is broken down with a voltage exceeding a rated level.

Abstract: A varistor includes a varistor element, a first layer which is porous on the varistor element, and a second layer on the first coating. The thickness t (mm) of the second layer is not smaller than 1.3/V, where V(ml/g) is the volume of pores of the first layer exposed to an outside of the first layer. This varistor includes the outer layers protected from being broken even when a non-ohmic interface in a voltage non-linear resistor is broken down with a voltage exceeding a rated level.

Abstract: A novel .omega.-carboxyalcohol oxidase catalyzes at least one of the following reactions:R--CH.sub.2 OH+O.sub.2 .fwdarw.R--CHO+H.sub.2 O.sub.2 a)R--CHO+O.sub.2 +H.sub.2 O.fwdarw.R--COOH+H.sub.2 O.sub.2 b)wherein R is alkyl, alkenyl, .omega.-carboxyalkyl or .omega.-carboxyalkenyl. The enzyme has substrate specificity on at least 12-hydroxydodecanoic acid, 1-dodecanol, 1-decanol, 1-octanol and 1-hexanol, and has no substrate specificity on methanol, ethanol or glycerol. The enzyme does not require the presence of NAD or NADP for its use. Also disclosed is a process for producing the enzyme, an assay method for substrates of the enzyme, and a process for producing carboxylic acid employing the enzyme.

Abstract: 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:a) R--CH.sub.2 OH+O.sub.2 .fwdarw.R--CHO+H.sub.2 O.sub.2b) R--CHO+O.sub.2 +H.sub.2 O.fwdarw.R--COOH+H.sub.2 O.sub.2wherein R is alkyl, alkenyl, .omega.-carboxyalkyl or .omega.-carboxyalkenyl. The enzyme has substrate specificity on at least 12-hydroxydodecanoic acid, 1-dodecanol, 1-decanol, 1-octanol and 1-hexanol, and has no substrate specificity on methanol, ethanol or glycerol. The enzyme does not require the presence of NAD or NADP for its use. Also disclosed is a process for producing the enzyme, an assay method for substrates of the enzyme, and a process for producing carboxylic acid employing the enzyme.

Abstract: A novel .omega.-carboxyalcohol oxidase catalyzes at least one of the following reactions:a) R--CH.sub.2 OH+O.sub.2 .fwdarw.R--CHO+H.sub.2 O.sub.2b) R--CHO+O.sub.2 +H.sub.2 O.fwdarw.R--COOH+H.sub.2 O.sub.2wherein R is alkyl, alkenyl, .omega.-carboxyalkyl or .omega.- carboxyalkenyl. The enzyme has substrate specificity on at least 12-hydroxydodecanoic acid, 1-dodecanol, 1-decanol, 1-octanol and 1-hexanol, and has no substrate specificity on methanol, ethanol or glycerol. The enzyme does not require the presence of NAD or NADP for its use. Also disclosed is a process for producing the enzyme, an assay method for substrates of the enzyme, and a process for producing carboxylic acid employing the enzyme.

Abstract: A antibiotic L53-18A and a pharmaceutically acceptable salt thereof which are useful for treatment of bacterial inventions are obtained by culturing, for example, Saccharopolyspora sp. L53-18 (FERM BP 2231) in a medium and the antibiotic accumulated therein is collected.

Abstract: L-glutamic acid oxidase having the following biochemical properties:(a) substrate specificity: L-glutamic acid,(b) enzyme action: catalyzes a reaction which forms one mole of .alpha.-ketoglutaric acid, one mole of ammonia and one mole of hydrogen peroxide from one mole of L-glutamic acid, one mole of oxygen and one mole of water, as follows: ##STR1## This oxidase is produced by culturing microorganisms belonging to genus Streptomyces in a nutrient medium and isolating the thus-produced L-glutamic acid oxidase. Particular microorganisms of genus Streptomyces are sp. A7700 FERM P-6241 (NRRL No. 15267) and sp. 8063 FERM P-6242 (NRRL No. 15268). The oxidase can be used for detecting L-glutamic acid or L-glutamate, in an aqueous sample, because it catalyzes a reaction which forms one mole of .alpha.-ketoglutaric acid, one mole of ammonia and one mole of hydrogen peroxide from one mole of glutamic acid, one mole of oxygen and one mole of water.

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: Antibiotic saccharocins of the formula ##STR1## wherein R is hydrogen (saccharocin) or hydroxyl (3'-oxysaccharocin) are produced by culturing a microorganism belonging to the genus Saccharopolyspora, for example Saccharopolyspora sp. AC 3440 FERM-P No. 6238, in a conventional nutrient medium, and separating the thus-produced saccharocins from the cultured medium. The noval saccharocins exhibit anti-bacterial activity against Gram negative bacteria.

Abstract: Antibiotic neplanocin A of the formula ##STR1## is produced by culturing Ampullariella sp. A 11079 FERM-P No. 4494 in a nutrient medium and then separating the neplanocin A thus produced from the culture medium.

Abstract: Aminoglycoside antibiotic G-367-2 believed to have the formula ##STR1## is produced by culturing Dactylosporangium thailandense G-367 FERM-P No. 4840 in a nutrient medium and separating the produced antibiotic therefrom. It has strong antibacterial effect against Gram negative bacteria.

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: Neplanocin-B and -F of the formula ##STR1## in which Y is oxygen or a valence bond, are produced by culturing Ampullariella sp. A 11079 FERM-P No. 4494 in a nutrient medium and then separating the neplanocin-B and -F thus produced from the culture medium.

Abstract: Aminoglycoside antibiotic G-367-1 believed to have the formulae ##STR1## is produced by culturing Dactylosporangium thailandense G-367 FERM-P No. 4840 in a nutrient medium and separating the produced antibiotic therefrom. It has strong antibacterial effect against Gram negative bacteria.

Abstract: A novel microorganism species belonging to the genus Micromonospora, i.e. Micromonospora sp. A 11725 is found to be capable of producing novel macrolide antibiotics A 11725 I, A 11725 II and A 11725 III. Novel antibiotics A 11725 Ia and A 11725 IIa are also found to be derived by chemical modification of the antibiotics A 11725 I and A 11725 II, respectively. All of these antibiotics or salts thereof exhibit excellent antibacterial and anti-mycoplasmal activities against various microorganisms such as Staphylococcus or Mycoplasma, and therefore useful for various purposes including medicaments.

Abstract: A group of sulfur-containing antibiotics, planothiocin-A, -B, -C, -D, -E, -F and -G, are produced by culturing Actinoplanes sp. A12526 in a nutrient medium, and separating the thus-produced planothiocins therefrom. The novel antibiotics have utility in therapeutic or prophylactic antibacterial compositions or feed additives for livestock, poultry or fish.

Abstract: An amino sugar compound represented by the general formula: ##STR1## (wherein m is an integer of 0 to 8, n is an integer of 1 to 8 and m+n is an integer of 1 to 8) has strong glycosidase inhibiting action and is produced by culturing an amino sugar compound producing microorganisms belonging to Streptomyces.

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.