Abstract: A novel alpha-acetolactate decarboxylase enzyme product with improved stability is provided. The novel enzyme is produced in high levels by cultivation of Bacillus strains selected from the group consisting of Bacillus brevis and Bacillus licheniformis ATCC 11031, ATCC 12759, ATCC 12713, ATCC 11946, ATCC 27326, NRRL B-3751, NCTC 2120, NCTC 8721, NCIB 6816, NCIB 8537 and NCIB 11868.

Abstract: A process for preparing a fructoside, especially a fructosyl disaccharide, comprises reacting a fructosyl saccharide such as sucrose or raffinose with an alcohol or aldose in the presence of a fructosyl-transferase, especially one derived from B. subtilis NCIB 11811, 11872 or 11873. In particular, aldose is a compound of the formula ##STR1## in which A represents a hydrogen atom or the group CH.sub.2 X, where X represents a hydrogen atom or an alkoxy group, and the fructosyl disaccharide so formed is halogenated to provide a halosucrose or halogalactosucrose sweetener.

Abstract: An improved powdered bacterial growth medium composition adapted to be admixed with water is described. The powdered growth medium includes an alkaline earth metal cation in a compound A admixed with a compound B containing an anion which reacts with the alkaline earth metal cation in compound A in an aqueous growth medium to form an essentially water insoluble salt or base, including the alkaline earth metal cation and the anion, which is acid neutralizing. The water insoluble salt is thus formed in situ in the aqueous growth medium when compounds A and B are added to the aqueous solution. Also described is an improved method for growing acid producing bacteria in an aqueous growth medium by forming the insoluble salt or base. The resulting growth medium is particularly adapted for neutralizing acids generated during growth of lactic acid producing bacteria which are grown for use in various food fermentations.

Abstract: The present invention consists of an analytical method for assay of L-glutamic acid in a sample by the use of an L-glutamic acid oxidase which is an L-amino acid oxidase catalyzing the oxidative deamination of the .alpha.-amino group of L-glutamic acid in the presence of water and oxygen to form .alpha.-ketoglutaric acid, ammonia and hydrogen peroxide, and having a very high substrate specificity for L-glutamic acid substantially without acting on L-glutamine and L-histidine, and also having a high stability, a reagent for analysis to practice the analytical method, a kit for analysis comprising the reagent, and a biosensor employing the enzyme.

Abstract: Sugar or sugar-alcohol fatty acid esters such as sucrose fatty acid esters are synthesized by incubating an aqueous mixture of a sugar or sugar-alcohol, a fatty acid and a catalytically active amount of a lipolytic enzyme, and recovering the resulting ester from the mixture.

Abstract: This invention relates to an alpha-amylase enzyme exhibiting thermostability at an acidic pH, produced by a strain of Clostridium thermohydrosulfuricum. This enzyme is especially useful for the preparation of glucose-containing syrups from starch.

Abstract: The gene coding for a thermostable pullulanase enzyme is incorporated into chimeric plasmids which are inserted into and reproduced by E. coli or B. subtilis host microorganisms. When microorganisms containing the chimeric plasmids are grown in fermentation media, they produce the pullulanase enzyme.

Abstract: A novel glutathione oxidase which acts on reduced glutathione alone and not no other sulfhydryl compounds is obtained by culturing Calodon or Cortinarius of the class Basidiomycetes.

Abstract: A novel microorganism is disclosed which has the identifying characteristics of Bacillus subtilis DSM 2704, including high productivity of alpha amylase.

Abstract: The present invention relates to a process for the production of a purified glucose isomerase which comprises contacting an impure extract containing glucose isomerase and soluble impurities with a weakly basic ion exchange material known to adsorb glucose isomerase; adding a first salt solution of a concentration which removes unadsorbed and weakly adsorbed impurities, but not glucose isomerase; and adding a second, buffered salt solution which elutes the adsorbed glucose isomerase.

Abstract: A protease moiety having direct fibrinolytic activity which is useful in thrombolytic therapy is isolated from snake venom and shown to comprise a metalloproteinase having a molecular weight of from 25 to 27 kd and an isoelectric point of about 6.5 to 7.0. The moiety is separated from venom by a series of diverse fractionation steps including molecular sieve, ion-exchange and affinity chromatography.

Abstract: A process is disclosed for chemically modifying naturally occurring proteins to produce enzyme-like modified proteins. The process comprises partially denaturing a cofactor containing holoprotein by removal of the cofactor to produce a partially denatured cofactorless or so-called apoprotein. The partially denatured protein is contacted with an inhibitor of a selected model enzyme and cross-linked. The resultant protein product is an enzyme-like modified protein having the catalytic characteristics of the model enzyme whose inhibitor is contacted with the partially denatured apoprotein.

Abstract: The enzyme D-2-hydroxy-4-methylpentanoic acid dehydrogenase has been prepared by culturing readily available Lactobacillus or Leuconostoc, microorganisms, such as Lactobacillus casei ssp. pseudoplantarum and Leuconostoc mesenteroides. The microbiologically produced enzyme has special characteristics and is capable of converting D-2-hydroxycarboxylic acids, such as D-2-hydroxy-4-methylpentanoic acid to the corresponding 2-ketocarboxylic acid and is capable of enzymatically converting 2-ketocarboxylic acids, such as 2-keto-4-methylpentanoic acid and 2-ketobutyric acid to the corresponding D-2-hydroxycarboxylic acid.

Abstract: A method for producing S-adenosyl-L-homocysteine hydrolase, which comprises cultivating a microorganism having the ability to produce S-adenosyl-L-homocysteine hydrolase within its cells in a nutrient medium to accumulate said hydrolase in the cells, said microorganism being a bacterium belonging to the genera Alcaligenes, Pseudomonas, Acinetobacter, Arthrobacter, Enterobacter, Rhodopseudomonas, Agrobacterium, Micrococcus, Corynebacterium, Brevibacterium, Chromobacterium, Xanthomonas, Flavobacterium, Cellulomonas, Azotobacter and Protaminobacter, or an actinomycete belonging to the genera Streptomyces, Mycobacterium, Nocardia, Streptoverticillium, Micromonospora, Micropolyspora, Streptosporangium and Microellobosporia; and then recovering S-adenosyl-L-homocysteine hydrolase from the cells.

Abstract: A method and apparatus are disclosed for growing a confluent layer of cells on the surface of a substrate which is held by a holding and positioning device so as to be in the form of a taut, planar substrate having upper and lower exposed surfaces. The device is arranged in a nutrient-containing receptacle which also contains a plate material having a solid upper planar surface extending above the plane of the bottom of the receptacle. The lower layer of the receptacle is in contact with the upper surface of the plate material and cells disposed on the upper surface of the substrate are found to anchor to the substrate and grow to a confluent layer.

Abstract: An assay for determining the Lewis blood group of a patient consists of testing a body sample for the presence of Lewis.sup.a and Lewis.sup.b antigens. Monoclonal antibodies specific for either of these antigens are employed which do not cross-react with other related antigens, such as the H blood antigen. Body samples which may be tested include: saliva, serum, urine, and paraffin-embedded tissue samples. Hybridoma cell lines and the antibody compositions they produce specific for these antigens are provided for use in the assay.

Abstract: Process for preparing fructose by treating starch with alpha-amylase, contacting the resulting liquefied starch with glucoamylase to hydrolyzed said starch to glucose, and isomerizing at least part of the resulting glucose to fructose by contacting said glucose with glucose isomerase. The three enzymes are obtained from organisms of the Basidiomycetes class of fungi.

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: This invention relates to a method for producing a plasminogen preparation which has been pasteurized to produce a hepatitis safe injectable plasminogen. The method comprises: adding to an aqueous solution of plasminogen the protective agent of methyl lysine ester, or ethyl lysine ester or a hydrochloride salt thereof which has antifibrinolytic acitivity to thereby attach the agent to plasminogen and form a modified plasminogen; and subjecting the resulting modified agent to a heat treatment of at least 60.degree. C. for at least 10 hours. Further, the protective agent may be separated from the modified plasminogen by affinity chromatography.

Abstract: The invention provides a flavin adenine dinucleotide (FAD) synthetase preparation with a specific activity at 25.degree. C. greater than at least 75 nanomoles per minute per milligram of protein in the preparation and usually greater than at least 150 nanomoles per minute per milligram of protein in the preparation as measured utilizing flavin mononucleotide (FMN) as the substrate. The purified preparation is obtained by disrupting a cellular source of FAD synthetase activity, precipitating the protein and separating an FAD synthetase active fraction by column chromatography. FAD synthetase catalyzes the reaction of adenosine triphosphate and flavin mononucleotide to flavin adenine dinucleotide and pyrophosphate, among others.