Enzymes and enzyme systems

Enzymes and enzyme systems

Enzymes and Enzyme Systems 5290692 solution of about 10 to about 20 wt % polyvinyl alcohol containing a microorganism or an enzyme is reacted with a...

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Enzymes and Enzyme Systems

5290692

solution of about 10 to about 20 wt % polyvinyl alcohol containing a microorganism or an enzyme is reacted with an aqueous solution of about 3 wt % to saturated boric acid for a period of about l0 minutes to about two hours to form gelled spherical heads. The beads are then hardened by treatment with an aqueous solution of about 3 to about 20 wt % phosphoric acid or phosphate for at least 30 minutes. Preferably, the polyvinyl alcohol has a degree of polymerization of about 1000 to about 3000 and a degree of saponification of about 70 to about 99 mol %. In an alternative embodiment, the boric acid solution can contain the phosphoric acid or phosphate. The microorganism can be an acclimatized activated sludge microorganism from agricultural or industrial waste water. The beads can be used for removing inorganic nitrogen and organic carbon in waste water treatment or in processes for making biochemical products.

BIOADAPTABLE POROUS CRYSTALLINE GLASS CONTAINING AN IMMOBILIZED FIBRINOLYTIC ENZYME FOR DISSOLVING BLOOD CLOTS Takahiro Suzuki, Sukezo Kawamura, Motohiro Toriyama, Yoshiyuki Yokogawa, Yukari Kawamoto, Nagoya, Japan assigned to Agency of Industrial Science & Technology Ministry of International Trade & Industry A fibrinolytic enzyme such as urokinase, tissue plasminogen activator or streptokinase is covalently bounded to a bioadaptable porous crystalline glass to produce a thrombolytic material. Production of the glass involves combining 4050 mol% calcium oxide, 20-30 mol% titanium dioxide and 25-35 mol% diphosphorous pentoxide to form a mixture, and combining the mixture with 0.5-4.0 mol% disodium oxide. A bioreactor for converting plasminogen in blood into plasmin can be prepared by packing the material in a column. When finely comminuted, the material can be administered into the blood of a patient for removing blood clots.

5290695 HEPARITINASE, PROCESS FOR PRODUCING THE SAME AND BACTERIA PRODUCING THE SAME

5290693

Kiyoshi Morikawa, Hirofumi Miyazono, Hiroshi Maruyama, Keiichi Yoshida, Hinode, Japan assigned to Seikagaku Kogyo Kabushiki Kaisha

IMMOBILIZATION OF MICROORGANISMS OR ENZYMES IN POLYVINYL ALCOHOL BEADS

Disclosed are novel enzymes, heparitinase T-I, heparitinase T-II, heparitinase T-III and heparitinase T-IV, which degrade heparan sulfate and/or heparin, a process for producing thereof by cultivating a novel Bacillus circulans HpT 298 having an ability of producing these enzymes and a novel Bacillus circulans HpT 298.

Kuo-Cheng Chen, Ying-Feng Lin, ,ayogaN assigned to National Science Council Microorganisms or enzymes are immobilized by using polyvinyl alcohol to form beads containing a microorganism or an enzyme. An aqueous 143

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PATENT ABSTRACTS

5292448 ENZYMATIC DETERGENT COMPOSITION

5292652 AMYLOIDIN PROTEASE USES THEREOF

AND

Jan Klugkist, Vlaardingen, Netherlands assigned to Lever Brothers Company Division of Conopco Inc

Harry F Dovey, Peter Seubert, Sukanto Sinha assigned to Athena Neurosciences lnc; Eli Lilly and Compa

A detergent composition comprising an anionic surfactant, a nonionic surfactant and a lipase enzyme, characterised in that: (a) the nonionic surfactant of the composition comprises a nonionic surfactant component selected from alkoxylate adducts of fatty alcohols, fatty acids, fatty esters, fatty amides and fatty amines of at least C10 chain length and mean alkylene oxide content of less than 5 alkylene oxide groups per molecule, forming at least 30~o by weight of the total nonionic surfactant of the composition; and in that (b) the total amount of the nonionic and anionic surfactant in the composition is in the range 1~ to 30% by weight; and (c) the lipase enzyme is present in an amount of about 0.005 to 100 Lu/mg based on the weight of the detergent composition.

A proteolytic enzyme isolated from human tissue which exhibits a proteolytic activity to hydrolyze Met-Asp peptide bond in an amyloidlike substrate is disclosed. This enzyme has been designated amyloidin because it proteolytically cleaves a Met-Asp bond similar to the one present in the amyloid precursor protein to release a fragment having the mature Asp terminus of the beta-amyloid peptide. Antibodies to the amyloidin protease are also provided. Methods to isolate and purify the amyloidin protease are provided, as well as assays to screen for inhibitors of the amyloidin protease. Also disclosed is the gene encoding the protease and methods for expression of the protease by recombinant DNA means.

5292660

5292509 METHOD FOR THE DISINSERTION OF VITREOUS B O D Y BY A N E N Z Y M E W H I C H DISRUPTS OR DEGRADES CHONDROITIN SULFATE PROTEOGLYCAN Gregory S Hageman assigned to Bethesda Eye Institute A method for selectively and completely disinserting the ocular vitreous body, epiretinal membranes and/or fibrocellular membranes from the neural retina, ciliary epithelium and posterior lens surface of the mammalian eye as an adjunct to vitrectomy comprises administering to the eye an effective amount of a protease-free glycosaminoglycanase enzyme, such as chondroitinase ABC, adapted to disrupt and/or degrade chondroitin sulfate glycosaminoglycan/proteoglycan localized specifically to sites of vitreoretinal adhesion and thereby permit complete disinsertion of the vitreous body and/or epiretinal membranes.

REMOVAL OF RESIDUAL MONOMERS FROM POLYMERS USING PEROXIDE-GENERATING ENZYME Gerardus Overbeek, Yvonne W Smak, Sprang Capelle, Netherlands assigned to IC1 Resin BV Method for removing radically-polymerisable unsaturated monomer from a dispersion of a polymer, made by non-enzymic polymerisation, by treating the polymer dispersion with a peroxide-generatingenzyme (such as an oxidase) and an enzyme substrate(s), and usually oxygen, optionally with a reducing agent, under conditions to effect a reduction in the level of the residual monomer.

5294539 NITRATE REDUCTASE FROM YEASTS, THE PREPARATION AND USE THEREOF Walther Johannssen, Harry Schwartz, Reiner Gromes, Martin Heinrich, Reinheim, Federal Republic Of Germany assigned to Merck Patent Gesellschaft mit beschrankter Haftung

P A T E N T ABSTRACTS The invention relates to NAD(P)H-dependent nitrate reductase from yeasts, to a process for the preparation thereof and to the use thereof in a reagent for determining nitrate. The nitrate reductase is characterized by a molecular weight of about 350 000 D and can be obtained by yeast cells which have been cultivated in a completely synthetic nutrient medium with nitrate as the sole nitrogen source and which contain nitrate reductase being disrupted in phosphate buffer, the crude extract being chromatographed on an anion exchanger, the fractions containing nitrate reductase being mixed with protein, concentrated by ultrafiltration and dried by fluidized bed granulation. The reagent for determining nitrate contains, besides the nitrate reductase prepared in this way, also N A D ( P ) H and a color reagent for determining nitrite.

5296161 ENZYMATIC PERHYDROLYSIS SYSTEM AND METHOD OF USE FOR BLEACHING Richard J Wiersema, A n n a Stanislowski assigned to The Clorox C o m p a n y A perhydrolysis system or activated oxidant system for in situ generation of peracid in aqueous solutions is disclosed including an esterase or lipase enzyme, a source of hydrogen peroxide, and a functionalized ester substrate having the structure See Patent for Chemical Structure wherein R is a substituent having at least one carbon atom and X is a functional moiety or group. Preferred substrates include glycerides, ethylene glycol derivatives and propylene glycol derivatives. The system is adapted for use in both high and low temperature wash conditions. In one embodiment, a lipase enzyme is employed with an insoluble substfate and an emulsifying agent. In another embodiment, an esterase and/or lipase enzyme, a glyceride substrate and hydrogen peroxide produce a peracid with active oxygen from a peracid of at least about 0.5 ppm. Bleaching processes and stain removal capabilities are also disclosed.

5296231 PURIFICATION AND ADMINISTRATION OF DNA REPAIR ENZYMES Daniel B Yarosh assigned to Applied Genetics Inc

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P C T No. PCT/US89/02873 Sec. 371 Date Dec. 26, 1990 Sec. 102(e) Date Dec. 26, 1990 P C T Filed Jun. 27, 1989.Methods for purifying D N A repair enzymes are provided in which an aqueous solution of a D N A repair enzyme in an impure state is applied to a molecular sieve column having an exclusion limit which will retard the D N A repair enzyme but will not retard contaminants larger than the D N A repair enzyme. The D N A repair enzyme in an enhanced state of purity is eluted isocratically from the molecular sieve column in an elution buffer and applied directly to a D N A affinity column in the same buffer without intermediate dialysis, ultrafiltration, or other procedures. The D N A repair enzyme is eluted from the D N A affinity column using, for example, a salt gradient. The method is rapid, inexpensive, simple to perform, and has been found to produce a h o m o g e n e o u s final product. In accordance with other aspects of the invention, the purified D N A repair enzymes are encapsulated in liposomes and administered to living cells in situ. This form of administration has been found to be non-toxic to the cells and to result in increased incision of damaged D N A , enhanced D N A repair synthesis, and increased cell survival after exposure to ultraviolet light. In certain preferred embodiments, D N A repair enzymes are administered in pH sensitive liposomes.

5296358 PROCESS FOR THE ENZYMATIC PREPARATION OF CEPHALOSPORANIC DERIVATIVES USING A D-AMINO ACID OXIDASE FROM RHODOTORULA GLUTINIS N C I M B 40412 Ezio A Battistel, Pietro Cesti, Goes Vilhelmus van der, Mirella Pilone, La Spezia, Ministero Dell'Universita' Scientifica e Tecnologica

Giuliana Franzosi, Silvana Bonicelli, Italy assigned to e Della Ricerca

The enzymatic preparation of cephalosporanic derivatives, or their salts, having the formula: See Patent for Chemical Structure (I) wherein R is - C O - C O O H or -COOH, R1 is H, OH, or -OC O - R " and R" is an alkyl group with l to 4 carbon atoms, is carried out by the oxidative deamination of compounds, or their salts, having the formula: See Patent for Chemical

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PATENT ABSTRACTS

Structure (II) with an oxidase D-Aminoacid enzyme derived from Rhodotorula glutinis NCIMB 40412. The enzyme can be in a free or immobilized form.

5296496 2-SACCHARINYLMETHYL PHOSPHATES, PHOSPHONATES AND PHOSPHINATES USEFUL AS PROTEOLYTIC ENZYME INHIBITORS AND COMPOSITIONS AND METHOD OF USE THEREOF Ranjit C Desai, John Court, Dennis J Hlasta assigned to Sterling Winthrop Inc 4-R1-R2-R3-2-Saccharinylmethyl and 4,7-C4,5,6, 7-tetrahydro 2-saccharinylmethyl phosphates, phosphonates and phosphinates of formulas I and IIA respectively herein, useful in the treatment of degenerative diseases, and compositions containing them, methods for using them to treat degenerative diseases, and processes for their preparation by reaction of the corresponding 2-halomethylsaccharins with a phosphate, phosphonate or phosphinic acid of formula II1 herein in the presence of an acidacceptor.

5298405 ENZYME PREPARATIONS WITH RECOMBINANTLY-ALTERED CELLULOSE PROFILES AND METHODS FOR THEIR PRODUCTION Helen Nevalainen, Jonathan Knowles, Pirkko Suominen, PentillaMerja, MantylaArj, Espoo, Finland assigned to Alko Limited Enzyme preparations enriched in hemicellulase-, pectin-, and/or lignin-degrading enzymes are described which are also partially or completely deficient in cellulase degrading activity. Such preparations may be utilized in an crude, unpurified form and are especially useful in the production of pulp and paper.

5300421 METHOD FOR QUANTITATIVE MEASUREMENT OF TRACE ENZYME AND SUBSTRATE USED THEREIN Nobuhito Masuda, Nobuo Suzuki, Shoji Ishiguro, Mitsunori Ono, Asaka, Japan assigned to Fuji Photo Film Co Ltd A synthetic substrate used for quantitative analysis of a trace enzyme. The substrate has a molecular structure (B)-(A)-(C) comprising at least one structure (A) catalytically affected by the enzyme to be analysed, at least one photographically active labelling structure (B) linked to the structure (A) and at least one specific adsorbing structure (C) linked to the structure (A). The substrate is used in a quantitative analysis of a trace enzyme, in which the structure (A) or the linkage between the structure (A) and the structure (C), or the linkage between the structure (B) and the structure (A) is cleaved by the action of the analyte enzyme. The reaction product of the enzymatic reaction is separated by allowing the same to contact with an adsorbent for the structure (C). The separated reaction product is developed photographically and then the optical density of the resultant developed silver and/or colored dye is measured.

5304548 BIVALENT LIGANDS EFFECTIVE FOR BLOCKING ACAT ENZYME FOR LOWERING PLASMA TRIGLYCERIDES AND FOR ELEVATING HDL CHOLESTEROL Ronald Gammill, Frank Bell assigned to The Upjohn Company Bivalent ligand compounds synthesized from a tether composition joining two heterocyclic groups comprising furochromones, furobenzoxazinones, and benzobisdifurans. These compounds show pharmacological activity in blocking ACAT enzymes which are major regulators of cholesterol metabolism. The compounds also show activity in lowering plasma triglycerides and elevating HDL cholesterol. They are useful in the prevention or treatment of the constriction or obstruction of arterial vessels, atherosclerosis, hyperlipidemia, hypertriglyceridemia, chylomicronemia, and pancreatitis.

PATENT ABSTRACTS

5304631 SYNTHETIC HELIZYME ENZYMES John M Stewart, Karl W Hahn, Wieslaw A Klis assigned to University of Colorado Foundation Inc The design, and synthesis of peptide-based molecules termed helizymes which possess catalytic activity are described herein The catalytic molecules of the invention comprise a number of amphiphilic helical peptides, which interact via hydrophobic interactions and which are bonded at their carboxyl ends to a multifunctional base. Active site residues functional for catalysis are positioned within or at the N-termini of the helical peptides. The helizyme molecule adopts a conformation in aqueous medium such that a substrate binding pocket is formed and such that functional active site geometry results from the association of the helical peptides Specifically exemplified helizymes possess specificities and at least one catalytic activity of chymotrypsin, trypsin and acetylcholine esterase.

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5306638 AMINE ADDITIVE ASSISTED ENZYMATIC ESTERIFICATION OF 1,2-DIOL MONOSULFONATES NeilWBoazassignedto Eastman Kodak Company A process has been developed for the enzymatic esterification of 1,2-diol monosulfonates comprising contacting an ester; a 1,2-diol monosulfonate; an enzyme derived from a microorganism or animal organ which has stereoselective activity to asymmetrically esterify said 1,2-diol monosulfonate; in the presence of a nonhydroxylic organic solvent and an amine additive of the general formula R32R4N, wherein R3 may be the same or different and is selected from hydrogen or a straight or branched C1-C20 alkyl; and R4 is a straight or branched C1-C20 alkyl; or an unsubstituted or substituted C3-C20 aryl or heteroaryl group (with saisd substituent selected from C1-C4 alkyl, halogen, or C1-C4 alkoxy, and said hetero atom selected from nitrogen, sulfur, or oxygen); to produce a mixture of enantiomerically enriched unreacted 1,2diol monosulfonate and the corresponding antipodal enantiomerically enriched ester. The resulting enantiomerically enriched products are useful chemical intermediates that may be employed in the synthesis of pharmaceutical and agricultural chemicals.

5306413 5306639 ASSAY APPARATUS AND ASSAY METHOD Ryuzo Hayashi, Yukie Inoue, Akio Kariyone, Higashiosaka, Japan assigned to Kanzaki Paper Manufacturing Co Ltd The present invention relates to a simple and yet multifunctional system for assay employing immobilized enzymes.

DNA ENCODING GLUCANASE ENZYMES Aiz Matsushiro, Aoyamadai, Japan Disclosed is the isolation and cloning of genes encoding glucanohydrolase enzymes and the expression and secretion of exogenous glucanase gene products in host cells.