Abstract: Described is a process for screening of microorganisms for the production of amylolytic enzymes. Microorganisms capable of amylolytic enzyme synthesis and growing on the surface of a solid medium are detected by identifying a zone of hydrolyzed starch surrounding each microorganism. The process is particularly useful for the detection of .alpha.-amylase activity in strains of Bacillus licheniformis as it employs a selection step under anaerobic conditions prior to the detection of the enzyme.

Abstract: A sensitive direct immunoassay system is provided for the detection of an antigen associated with hepatitis in body fluids. A single antibody which reacts with a hepatitis antigen or antigens and which is bonded to an insoluble member, is incubated with a test sample. During this first period of incubation a portion of an antigen present in the test sample will combine with the antibody immobilized on the insoluble member. The antibody bonded member, to which antigen is attached, is then washed and incubated with an enzyme tagged antibody reagent. During the second incubation, the tagged antibody reacts with antigen fixed to the antibody member in the first incubation. Thus, an immobilized "sandwich" is formed of an insoluble member- antibody-antigen-enzyme tagged antibody. After the second incubation, the member is washed again to remove unreacted enzyme antibody reagent. The member is then exposed to a substrated which is converted by the enzyme to produce an end product.

Abstract: Assay reagents for the determination of enzymes such as .alpha.-amylase, .alpha.-glucosidase, .beta.-glucosidase, and acid and alkaline phosphatases are described. The reagents comprise a substrate capable of releasing the chromophore p-nitrophenol at a rate proportional to the amount of enzyme being assayed and a buffer material that eliminates the temperature dependence of the chromophore.

Abstract: This invention relates to diagnostic reagents and a method for increasing the sensitivity of chemical and enzymatic analysis. In particular, it relates to an improved reagent and method wherein the sensitivity of the analysis is improved by the addition of a water-soluble inclusion compound.

Abstract: An assay method for amylase activity in a biological specimen such as serum, saliva or urine. The enzyme amylase in the specimen is used to decompose a substrate which is a glucose polymer having a modified reducing terminal glucose residue or a cyclic glucose polymer. A component of the decomposed substrate is measured as an indication of amylase activity in the specimen. The residue may be amylose, amylopectin, starch, starch hydrolyzate, an etherified reducing terminal, an esterified reducing terminal, gluconolactone or a gluconic acid residue or its derivative. Decomposed substrate assay may be effected by contacting the same with maltose dehydrogenase and NAD or NADP, whereupon the assay is performed by measuring the amount of reduced NAD or reduced NADP, by reacting the same with reduced-form hydrogen transport colorimetric reaction reagent. This reagent may be a tetrazolium salt and diaphorase, or tetrazolium salt and phenazinemethosulfate.

Abstract: The present invention provides a process for the determination of NAD(P)H or of salicylate, wherein, in a NAD(P)H-dependent reaction, salicylate is decarboxylated by salicylate hydroxylase and a colored material is formed from the decarboxylation product in the presence of tyrosinase by oxidative coupling with an appropriate colored material component, the colored material formed then being determined photometrically.The present invention also provides a reagent for the determination of NADH or NADPH, wherein it contains salicylate, a chromogenic hydrazone or amine, salicylate hydroxylase, tyrosinase and buffer, as well as a reagent for the determination of salicylate, wherein it contains NAD(P)H, a chromogenic hydrazone or amine, salicylate hydroxylase, tyrosinase and buffer.

Abstract: A method for decomposing hydrogen peroxide is disclosed. The hydrogen peroxide is reacted with a compound represented by the formula (I) ##STR1## wherein Z represents OH or NR.sub.4.R.sub.5 wherein R.sub.4 and R.sub.5 are the same or different and represent hydrogen, alkyl, substituted alkyl or acyl, and R.sub.1,R.sub.2 and R.sub.3 are the same or different and represent hydrogen, halogen, alkyl, alkoxy, amino, nitro, carboxyl or sulphonyl, in the presence of peroxidase.

Abstract: A method for the assay of .alpha.-amylase activity, which comprises adding an .alpha.-amylase-containing sample to maltohexaitol or maltohexaonic acid used as substrate, reacting, at the same time or subsequent to the addition, .alpha.-glucosidase with the resulting mixture, and determining the reaction product to assay the .alpha.-amylase activity.

Abstract: New indoxylmaltodextrins, an enzymatic process for their preparation and their use as a substrate for the analytical detection and the determination of amylases, and rapid diagnostic agents which contain such indoxylmaltodextrins are described.

Abstract: A stabilized composition comprising apoglucose oxidase is disclosed. In addition to the apoenzyme, a stabilizing agent comprising poly(vinyl alcohol), bovine serum albumin or mixtures thereof is included. The composition can also comprise, in addition to the apoenzyme and stabilizing agent, reagents for a homogeneous specific binding assay system capable of producing a detectable response which is a function of a ligand in, or the ligand binding capacity of a test sample, wherein the apoenzyme is itself one of the reagents in the assay system. The stabilized composition can be utilized in a test device for assaying a ligand in, or the ligand binding capacity of a liquid sample, whereby the device comprises a test device incorporated with the composition.

Abstract: For determining both water-insoluble and water-soluble plant fibre components in plant fibre material, more particularly dietary fibre components in dietary plant material, a sample which has been solubilized and degraded with regard to other plant components is passed through a glass filter (2) capable of retaining the water-insoluble fibre components of the sample and then through an ultrafilter (1) capable of retaining the water soluble fibre components and the sample.

Abstract: A method of determining the concentration of pancreatic .alpha.-amylase and salivary .alpha.-amylase in a body fluid containing a mixture of said .alpha.-amylases. First and second samples of said body fluid are prepared, and the second samples are treated with an effective amount of an inhibitor capable of selectively inhibiting the activity of said .alpha.-amylases. The amount of total .alpha.-amylase, i.e. the sum of salivary .alpha.-amylase and pancreatic .alpha.-amylase, is then measured for said first and second samples, and the concentration of salivary and pancreatic .alpha.-amylase present in said first and second samples is determined by comparing the measured total .alpha.-amylase values with a standard. The inhibitor used has a discrimination factor--expressed as the ratio between the quantity of inhibitor necessary for reducing the activity of one of said two .alpha.-amylases by 50% and the quantity of inhibitor necessary for reducing the same activity of the other of said .alpha.

Abstract: Method for determining .alpha.-amylase by incubating with a starch substrate, wherein the substrate is based upon particulate starch derivatized with detectable groups for the determination of .alpha.-amylase, the substrate consisting of superficially cross-linked starch or amylose grains having a regulated, reduced swellability, said grains having a diameter of from 0.01 to 0.20 mm; these grains are prepared by suspending non-swollen grains in a solution with only enough cross-linking agent to achieve superficial cross-linking and then derivatizing the grains with the detectable groups for the determination of .alpha.-amylase.

Abstract: A stable enzyme reference composition having an excellent shelf-life. The composition comprises at least one enzyme of known value; about 20 to about 40 weight percent of at least one alkylene polyol having from 2 to 5 carbon atoms; about 3 to about 8 grams (gm) per deciliter (dl) total protein present in a human serum albumin matrix; and about 60 to about 80 weight percent water.

Abstract: A blood biochemistry control standard for the quality control of the analytical measurement of blood biochemistry components is disclosed. The control standard comprises an aqueous suspension of red blood cells which have been stabilized by mild treatment with aldehyde and saline and then slowly equilibrated with at least one additionally incorporated non-gaseous biochemical analyte in a concentration of clinical significance.

Abstract: A chromogenic substrate for the assay of polysaccharide endo-hydrolases is the reaction product of a polysaccharide susceptible to endo-hydrolase degradation, a chemical reagent for increasing the solubility of the polysaccharide so as to increase its susceptibility to enzyme degradation, and a dye substance for coloring the polysaccharide and rendering it capable of estimation by absorption spectrometry. The amount of chemical reagent should be such as to produce a degree of chemical substitution in the range 0.06 to 0.6 DS.

Abstract: An enzyme assay reagent comprises a substance which is capable of interaction with the enzyme to give rise to the formation of a compound of formula X--A--Y--NO.sub.2, wherein A comprises an aromatic nucleus, X comprises an auxochromic group and Y comprises an unsaturated group which is capable of transmitting electron resonance between the aromatic nucleus and the nitro substituent, said compound per se being capable of producing a visual signal which is easily discernible by eye.

Abstract: A maltodextrin phosphorylase limit dextrin in the presence of maltodextrin phosphorylase and inorganic phosphate, is used as a substrate for alpha-amylase, which initiates a series of enzymatic reactions resulting in a chromogen response which can be used to measure the concentration of alpha-amylase in a body fluid. A novel limit dextrin and its preparation also are described.

Abstract: An integrated material for chemical analysis comprising three or more reagent layer units on a support and a porous spreading layer, said units containing reagents for different chemical analyses and being proximately arranged on a support such that approximately equal portions thereof are within a spreading circle defined by the diffusion of a liquid sample as it passes through the porous spreading layer, and a method for analyzing blood using the same.

Abstract: Novel method for the determination of .alpha.-amylase which method comprises contacting a sample suspected of containing .alpha.-amylase with a starch derivative carrying a substituent capable of dyestuff-forming coupling; separating from the resulting starch-containing phase the low molecular weight soluble fission products formed by splitting of said starch derivative by .alpha.-amylase; coupling the said couplable substituent with another dyestuff forming component; and measuring the dyestuff so formed as a measure of the initial .alpha.-amylase content.

Abstract: An improvement in a method for determining a substance present in a biological fluid by oxidizing a compound produced in the course of the determination in the presence of a dehydrogenase enzyme with the simultaneous production of reduced beta-nicotinamide adenine dinucleotide in an amount proportional to the content of the substance in the fluid, which fluid also contains an endogenous material which or a derivative of which produced during the determination likewise is oxidized in the presence of the enzyme with the simultaneous production of reduced beta-nicotinamide adenine dinucleotide, thereby interfering with the determination, which improvement involves first carrying out the oxidation-reduction reaction of the endogenous material or its derivative, then oxidizing the resulting reduced beta-nicotinamide adenine dinucleotide in the presence of lactate dehydrogenase with the simultaneous reduction of pyruvate to lactate, thereafter inhibiting the lactate dehydrogenase enzymatic activity, and thereafter

Abstract: Bacteria, particularly coliform bacteria, present in a liquid, are rapidly detected. A sample of the liquid to be tested is admixed with an enzyme-inducing agent which induces the production of an enzyme in the bacteria, the enzyme being capable of reacting with a fluorescent conjugate ingested by the bacteria to release its fluorescent portion. Conditions are controlled such that a sufficient number of molecules of enzyme are produced per bacterium present in the liquid sample to effect release of the fluorescent portion. A fluorescent conjugate, capable of being ingested by the bacteria, is admixed with the liquid sample for reaction with the enzyme to release the fluorescent portion of the fluorescent conjugate. The liquid sample is then formed into microdroplets in a liquid carrier such that the fluorescent material is retained in the microdroplets.

Abstract: The present invention provides a process for obtaining maltose phosphorylase and/or .beta.-phosphoglucomutase from micro-organisms, wherein the starting material used is selected from Lactobacillus brevis DSM 20054, NCIB 8836, 8561 and 8562, Lactobacillus plantarum DSM 20174 and 43, Lactobacillus reuteri DSM 20016, Lactobacillus fermentum DSM 20052, Streptococcus spec. DSM 1118, DSM 119, DSM 1120 and DSM 1121.The present invention also provides a composition and process for determining .alpha.-amylase, wherein maltose phosphorylase and .beta.-phosphoglucomutase obtained by such a process is used, as a crude extract or in an enriched form, optionally with the addition of .alpha.-glucose-1,6-diphosphate and of divalent manganese ions.

Abstract: Disclosed herein are a method and a reagent test kit, both using an improved substrate to measure the amylase content of a sample. The substrate used is a glycoside consisting of a defined polysaccharide glycosyl residue and a substituted aromatic radical attached to the terminal unit of the glycoside. When detached from the polysaccharide, the aglycone exhibits a different spectral absorbance than the substrate.

Abstract: Disclosed herein is a method for producing maltooligosaccharide glycosides in substantially pure form which includes the steps of incubating a glucosyl donor and a glucosyl acceptor in the presence of a glucanotransferase enzyme under transglycosylating conditions and separating the maltooligosaccharide glycoside from the reaction mixture.

Abstract: A carbohydrate substrate such as starch for a carbohydrate hydrolyzing enzyme is immobilized on a solid inorganic porous support to form a stable substrate-support composite useful in affinity chromatography and in methods where a precise amount of substrate is needed to perform an enzyme-substrate reaction to quantify the enzyme. The substrate may be activated with an agent such as cyanogen bromide or imidazole prior to deposition on the support so that it may be effectively modified while on the support. After deposition, the substrate is modified by reaction with an epoxyhalogen, aliphatic dihalide or aliphatic diamine to aid in holding it on the support. In an alternative embodiment, the carbohydrate, prior to deposition and modification on the support, is hydrolyzed with an enzyme, preferably dextranase.

Abstract: This invention relates to a method and apparatus for rapid quantitative determination of .alpha.-amylase in aqueous samples such as blood serum, etc. The method comprises a flow-through of the sample through various immobilized reagents contained in sequential stages. A scavenger stage initially removes glucose originally present in the sample and comprises immobilized glucose oxidase and catalase. The glucose-free sample flows through an immobilized starch stage substrate preferably containing a high percentage of amylose to quantitatively react with the .alpha.-amylase in the sample and produce oligosaccharides. The sample with the oligosaccharides flows through a glucose-generating stage containing immobilized glucoamylase which converts the oligosaccharides to glucose. The glucose-containing sample enters a detection stage wherein the glucose is converted to H.sub.2 O.sub.2 by flowing through immobilized glucose oxidase, and the H.sub.2 O.sub.

Abstract: This invention relates to a method and apparatus for rapid quantitative determination of .alpha.-amylase in aqueous samples such as blood serum, etc. The method comprises a flow-through of the sample through various immobilized reagents contained in sequential stages. A scavenger stage initially removes glucose originally present in the sample and comprises immobilized glucose oxidase and catalase. The glucose-free sample flows through an immobilized starch stage substrate preferably containing a high percentage of amylose to quantitatively react with the .alpha.-amylase in the sample and produce oligosaccharides. The sample with the oligosaccharides flows through a glucose-generating stage containing immobilized glucoamylase which converts the oligosaccharides to glucose. The glucose-containing sample enters a detection stage wherein the glucose is converted to H.sub.2 O.sub.2 by flowing through immobilized glucose oxidase, and the H.sub.2 O.sub.