Abstract: Disclosed herein is a process for preparing a novel monoester of the formula ##STR1## in which the associated novel diester ##STR2## is hydrolyzed in the presence of one or more water-soluble enzymes or microorganisms capable of selectively hydrolyzing the --O--C(O)--R.sup.1 group, wherein the treatment is carried out in a biphasic solvent system comprising an aqueous phase having the enzymes or microorganisms and an organic phase immiscible in water having the diester. Also disclosed is a process for preparing [1S-[1.alpha., 2.alpha.(Z),3.alpha.,4.alpha.]]-7-[3[[[[(1-oxoheptyl)amino]acetyl]-amino]m ethyl-7-oxabicyclo-[2.2.1]hept-2-yl]-5-heptenoic acid using this enzymatic/microbial process.

Abstract: A process for the preparation of an organic ester of ascorbic acid or erythorbic acid represented by the general formula (II) or (III): ##STR1## wherein R.sub.1 is alkyl, aralkyl, or aryl, by reacting ascorbic acid or erythorbic acid with an organic acid or an ester thereof of the general formula (I) :R.sub.1 COOR.sub.2 (I)wherein R.sub.1 is as defined above and R.sub.2 is hydrogen, methyl, ethyl or propyl, in an organic solvent in the presence of an ester hydrolase.

Abstract: 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:(a) Monoglyceride+H.sub.2 O.fwdarw.Glycerol+Fatty acidThe monoglyceride lipase is produced by culturing a specific monoglyceride lipase producing microorganism of Bacillus and then collecting the monoglyceride lipase from the resulting culture. A method is also disclosed for the analysis of a monoglyceride-containing sample solution. The monoglyceride lipase is caused to act on the sample solution upon measurement of the monoglyceride in the sample solution. Either one of glycerol and the fatty acid formed in accordance with the equation (a) is then measured.

Abstract: A process is provided for the enrichment in R isomer of an aryloxypropioic acid ester and for the stereoselective hydrolysis of an aryloxypropionic acid ester to form the corresponding aryloxypropionic acid in predominantly S configuration which comprises subjecting an aryloxypropionic acid ester of formula I ##STR1## wherein A is an ester residue and preferably an alkyl group, optionally substituted or branched, wherein R' is an optionally substituted aryl or heterocyclic ring system, containing in addition to carbon atoms one or more atoms selected from nitrogen, sulphur and oxygen, this ring system being optionally substituted and wherein B and D are for example a hydrogen or a halogen atom, to the action of a microorganism or substance derived thereof capable of stereoselective hydrolysis of the COOA group to form the corresponding carboxylic acid predominantly is S configuration.

Abstract: A process for the preparation of an organic ester of ascorbic acid or erythorbic acid represented by the general formula (II) or (III): ##STR1## wherein R.sub.1 is alkyl, aralkyl, or aryl, by reacting ascorbic acid or erythorbic acid with an organic acid or an ester thereof of the general formula (I):wherein R.sub.1 is as defined above and R.sub.2 is hydrogen, methyl, ethyl or propyl, in an organic solvent in the presence of an ester hydrolase.

Abstract: Compound labelled by the acetyl cholinesterase of Electrophorus electricus, its preparation process and its use in enzymoimmunology.This compound is constituted by a molecule chosen from among the antigens, haptens and antibodies, bonded by a covalent bond to an enzyme formed by the acetyl cholinesterase of Electrophorus electricus (electric eel).For example, the molecule is the substance P or a prostaglandin and the compound can be used for the enzymoimmunological determination of these molecules.

Abstract: A process for the preparation of a pharmaceutically active compound in a stereospecific form of the formula ##STR1## or a pharmaceutically acceptable salt or ester thereof, like an alkali metal salt or an alkaline earth metal salt or a pivaloyl ester, wherein R.sub.1 represents an optionally substituted aryl group such as a phenyl or naphthyl group optionally included in a heterocyclic ring system, which is optionally substituted, or represents a heteroaromatic ring system containing in addition to carbon atoms one or more atoms selected from nitrogen, sulphur and oxygen, this ring system being optionally substituted, which comprises subjecting a compound of the formula ##STR2## wherein R.sub.

Abstract: An analog-ligand having a conformation that substantially corresponds to the conformation of a hydrolytic transition state of an amide or ester reactant ligand is used to produce receptor molecules of predetermined specificity. The receptor molecules include an antibody combining site that binds to a reactant ligand and thereby stabilizes the tetrahedral carbon atom of the amide or ester hydrolysis transition state of that reactant ligand to catalytically hydrolyze the reactant ligand at a predetermined site.

Abstract: An acyloxyacyl hydrolase from the human promyelocyte cell line HL-60 has been found to specifically hydrolyze fatty acids from their ester linkages to hydroxy groups of 3-hydroxyfatty acids, the latter being being bound in turn to lipopolysaccharide glycosaminyl residues. The hydrolyzed fatty acids may include dodecanoic acid, tetradecanoic acid and hexadecanoic acid. This enzyme showed a molecular weight by gel exclusion chromatography between about 50,000 Daltons and about 70,000 Daltons, and a molecular weight by polyacrylamide gel electrophoresis with sodium dodecylsulphate, using reduced molecular weight standards, of approximately 54,000 to 60,000 Daltons.Altered bacterial lipopolysaccharide substantially without fatty acids bound in ester linkage to hydroxy groups of 3-hydroxyfatty acids covalently linked to a glucosaminyl moiety of lipopolysaccharide lipid A are produced.

Abstract: The present invention relates to a process for making an isocyanate which comprises the steps of: (a) reacting an amine with dimethyl carbonate in the presence of a hydrolase enzyme catalyst, preferably at a temperature not exceeding 50.degree. C. to form a methyl urethane, and (b) subjecting said methyl urethane to an elevated temperature in order to thermally cleave the urethane to produce an isocyanate.

Abstract: An isoenzyme from tomato, acid phosphatase-1 isoenzyme (Apase-1.sup.1), has ben purified to homogeneity and is subjected to amino acid sequencing and used to prepare anti-Apase-1 antibodies. The amino acid sequence permits design of probes to recover Apase-1.sup.1 -encoding cDNA; the antibodies are also useful for this purpose. The cDNA is useful to recover the genomic DNA encoding Apase-1.sup.1, which can then be used in walking or jumping techniques to recover the genomic DNA which confers nematode resistance, since this DNA resides immediately adjacent to the Apase-1.sup.1 gene on chromosome 6 of Lycopersicon esculentum.

Abstract: An acyloxyacyl hydrolase from the human promyelocyte cell line HL-60 has been found to specifically hydrolyze fatty acids form their ester linkages to hydroxy groups of 3-hydroxyfatty acids, the latter being bound in turn to LPS glycosaminyl residues. The hydrolyzed fatty acids may include dodecanoic acid, tetradecanoic acid and hexadecanoic acid. This enzyme showed a molecular weight between about 50,000 daltons and about 70,000 daltons.Altered bacterial LPS substantially without fatty acids bound in ester linkage to hydroxy groups of 3-hydroxyfatty acids covalently linked to a glucosaminyl moiety of LPS lipid A are produced. Since the structure of the lipid A moiety is highly conserved, acyloxyacyl hydrolase may act on LPS of many different pathogenic bacteria (for example Salmonella, Escherichia, Hemophilus, and Neisseria).

Abstract: A method of resolving glycidyl esters to high enantiomeric excess involves fractionation of hydrolytic enzymes (e.g. lipases) to prepare biocatalysts with high enantioselectivity, and using these catalysts to selectively hydrolyze one enantiomer of the glycidyl esters. Also a method for fractionation includes stirring an aqueous solution of the enzyme with a solid inert adsorbent to provide an adsorbed and non-adsorbed enzyme fraction, where the non-adsorbed fraction displays a higher enantioselectivity than the crude non-fractionated enzyme. Also a composition composed of a glycidyl ester is obtained with an enantiomeric excess of greater than or equal to 97%.

Abstract: R- and S-1-Phenyl-1,3-propanediol, each of high optical purity, were prepared by a chemoenzymatic sequence starting with ethyl benzoylacetate. The first step was a catalytic hydrogenation of the .beta.-ketoester conducted at room temperature. The enzymatic hydrolysis of the resulting hydroxyester proceeded in a facile manner using a commercial preparation of the lipase from Pseudomonas fluorescens. The enzymatic hydrolysis proceeded at a moderate rate (350 mg lipase/0.10 mol of racemic ester required a 20-hour reaction time with an enantiomeric rate ratio (E value) of 36). The hydrolysis was run to 45-50% conversion to afford isolated S-3-phenyl-3-hydroxypropionic acid of 85-90% ee after separation from the residual ester (aqueous base extraction). The optical purity of the hydroxy acid was determined by conversion to the methyl ester (CH.sub.3 I, KHCO.sub.3, acetone), and derivatization with S-MTPA-Cl, and .sup.1 H NMR analysis.

Abstract: A novel esterase (molecular weight 54,000.+-.2,000) derived from a microorganism belonging to genus Bacilus is extensively utilizable for organic synthetic reaction, especially for asymmetric hydrolysis of ethyl 2,2-dimethyl-3-(2,2-dichlorovinyl)cyclopropane carboxylate (ethyl permethrate), in the same manner as pig liver esterase.The microorganism suitable for production of the above novel esterase is Bacillus sp. DC-1 (FERM BP-1254).

Abstract: A process for preparing optically active indoline-2-carboxylic acid by an optical resolution, which comprises subjecting a racemic ester of (R,S)-indoline-2-carboxylic acid having the general formula [(R,S)-I] to the action of an enzyme or a microorganism having a stereo-selective esterase activity, which is capable of asymmetrically hydrolyzing the racemic ester [(R,S)-I] to give optically active indoline-2-carboxylic acid having the formula [II*] so as to produce the hydrolysis product, i.e. optically active indoline-2-carboxylic acid [II*] and an unreacted optically active ester of indoline-2-carboxylic acid having the general formula [I*], isolating each optically active form, and further, if necessary, hydrolyzing the obtained optically active ester [I*] to give an optical antipode of the acid [II*].According to the process of the present invention, optically active indoline-2-carboxylic acid with a high optical purity can be prepared in a simple process with a good yield.

Abstract: Process for the production of optically active (+)-bicyclo[3.3.0]octanol derivatives of formula (+)-I, in which R.sub.1 and R.sub.2 represent jointly an oxygen atom or the double-bond residue --O--X--O-- with X as a straight or branched-chain alkylene with 1-7 C-atoms, or R.sub.1 and R.sub.2 represent separately the residue OR.sub.5 with R.sub.5 as a straight or branched-chain alkyl with 1-7 C-atoms, and R.sub.3 the residue COOZ with Z as a hydrogen atom, straight or branched chain alkyl with 1-7 C atoms, cycloalkyl with 3-6 C atoms, phenyl or aralkyl with 7-10 atoms or R.sub.3 is the residue --(CH.sub.2).sub.n --O--COR.sub.4 with n having the meaning 1-4 and R.sub.4 as a straight or branched-chain alkyl with 1-7 C atoms, cycloalkyl with 3-6 C atoms, phenyl or aralkyl with 7-10 C atoms. The process is characterized in that racemic 3.alpha.-cyloxy-cis-bicyclo[3.3.0]-octane derivatives of formula (+)-II, wherein R.sub.1, R.sub.2 R.sub.3 and R.sub.

Abstract: A process for obtaining D-2-(6-methoxy-2-naphthyl)-propionic acid from a mixture of D- and L-2-(6-methoxy-2-naphthyl)-propionic acid lower alkyl esters is provided by asymmetric hydrolysis of the L-ester with a microbial enzyme, separation of the 2-(6-methoxy-2-naphthyl)-propionic acid from the D-2-(6-methoxy-2-naphthyl)-propionic acid lower alkyl ester and saponification of the latter, wherein the saponification is carried out enzymatically with esterase from hog liver or from Pleurotus ostreatus.

Abstract: Proteins having a hydrophobic cavity proximate to which is a residue promoting hydrolysis of functional moieties are effective semisynthetic hydrolases. Heme proteins from which the heme has been removed usually have at least one imidazole residue proximate to the cavity, and thus act as quite effective esterases. Because the size and shape of the cavities of such proteins are capable of broad diversity a wide spectrum of substrates may be hydrolyzed by these semisynthetic enzymes.

Abstract: Racemic carboxylic acid esters of epoxy alcohols are enantio selectively hydrolyzed with hydrolytic enzymes to provide chiral epoxy alcohol and chiral unhydrolyzed ester.

Abstract: Method for the selective extraction of desired lipophilic proteins from transformed cells of the genus Pichia by cell lysis in the presence of chaotrophic salts is disclosed. The total protein extracted under the invention cell lysis conditions is reduced while the recovery of desired lipophilic proteins remains relatively constant, thereby producing a cell extract with enhanced concentration of the desired lipophilic protein relative to a control cell extract.

Abstract: The present invention provides a process for obtaining cholesterol esterase by culturing an appropriate micro-organism in an appropriate nutrient medium and recovering the enzyme from the culture broth or from the biomass, wherein the culturing is carried out in a mineral salt medium containing n-alkanes with 10 to 20 carbon atoms as the sole source of carbon and in the form of an aerated submersion culture.

Abstract: Disclosed is combination of an acylase and esterase for selective enzymatic hydrolysis of only the L-isomer of an L and D mixture of .alpha.N-acyl-.alpha.-amino acid ester whose alpha carbon atom is chiral to yield a mixture containing L-.alpha.-amino acid and D-.alpha.-N-acyl-.alpha.-amino acid ester but essentially no D-.alpha.-amino acid.

Abstract: The present invention provides a process for obtaining cholesterol esterase from micro-organisms by culturing a micro-organism capable of forming cholesterol esterase in an appropriate nutrient medium in the presence of an inductor and obtaining the enzyme from the culture liquid and/or from the cells, therein the inductor used is a compound of the general formula: ##STR1## in which R and R.sub.1 are alkyl or alkoxy radicals containing 14 to 18 carbon atoms and R or R.sub.1 can also be a hydrogen atom and R.sub.2 is an alkylamino radical containing 2 to 8 carbon atoms, an alkyl-trimethylammonium radical containing 3 to 8 carbon atoms, an alkylpyridine radical containing up to 4 carbon atoms in the alkyl moiety or a radical of the general formula --CH.sub.2 --(CHOH).sub.n --CH.sub.2 OH, in which n is a whole number of from 1 to 4.

Abstract: A method for the determination of the amount of lipase in a sample comprises the steps of:(a) contacting the sample with a reagent composition comprising:(i) a lipase substrate which is a glycerol triester oil having in one of its two .alpha.-ester positions a long chain alkyl group having at least 8 carbon atoms and, in its two remaining ester positions, short chain alkyl groups such that, if the long chain alkyl group is hydrolyzed, the resulting diester is water soluble; and(ii) an esterase enzyme capable of catalyzing the hydrolysis of a water soluble glycerol diester to glycerol; and(b) detecting the rate at which glycerol is formed.The compositions of the present invention include the substrate and enzyme as defined. The element of the invention comprises a support having thereon the described composition. The invention is useful for determining lipase in samples which contain endogenous glycerol, such as blood serum and other body fluids.

Abstract: Process for the dissolution of peptides and proteins in non-aqueous and mixed non-aqueous/aqueous solvents using crown ethers, solutions thereby obtained and their use. Purification of proteins and/or enzymes, modification and optimisation of the activity of enzymes. Use of peptide-crown ether complexes as membrane materials, use of enzyme-crown ether complexes as detergents.

Abstract: Production of undesired desacetylcephalosporin C during fermentation of cephalosporin C-producing microorganisms is substantially reduced by addition of certain phosphorous compounds to the culture medium.

Abstract: New acetylesterases are prepared from Aureobasidium pullulans IFO 4466 which are capable of hydrolyzing cephalosporin C to deacetylcephalosporin C.

Abstract: A process for producing cyclodextrin from starch in which an aqueous solun of starch is subjected to the action of an active cyclodextrin glycosyltransferase and the reaction mixture containing cyclodextrin, starch degradation products and active enzyme is continuously subjected to an ultrafiltration process to effect passage of the formed cyclodextrin through the membrane, while retaining substantially all of the other starch degradation products and active enzyme, thus permitting more cyclodextrin to be formed in the retentate, which will then pass the membrane, collecting the aqueous solution of cyclodextrin and recovering the cyclodextrin.

Abstract: The present invention provides a process for the stabilization of an aqueous solution of cholesterol esterase from Pseudomonas, especially in the presence of a surface-active agent, wherein the enzyme is dissolved in a phosphate-free buffer which contains 10 to 200 mMol/liter of magnesium ions.

Abstract: An enzyme which catalyzes the hydrolysis of glycerol esters is disclosed. The enzyme is specific for alkyl esters wherein the alkyl group has from 1 to 4 carbon atoms inclusive. The enzyme is particularly useful in hydrolyzing a diacetyl glycerol ester. The enzyme is from the microorganism Bacillus subtilis ATCC No. 31954.

Abstract: A method for separating isoenzymes is disclosed. The method involves polyacrylamide gel electrophoresis in a buffer solution of a salt of 2-amino-2-methyl-1,3-propanediol at a pH of about 6.4 to 7.3 and an electrolyte buffer of 2-amino-2-methyl-1,3-propanediol taurine at a pH of about 8.0 to 10.0. After separation of the isoenzymes, the amount of individual isoenzymes present is determined.

Abstract: Deacetylcephalosporin C is converted to cephalosporin C by contact with an acetylesterase produced by Aureobasidium pullanans strain 1F0 4466.

Abstract: The disclosed methods and devices for detecting or monitoring or identifying substances (such as chemical warfare agents) and residual environmental pollutants (such as pesticides) utilize the discovery that spectra (e.g. infrared absorption spectra) of an uninhibited enzyme (e.g., a cholinesterase) can differ from spectra of the same enzyme which has been complexed with the agent pollutant. For example, the infrared spectrum of uninhibited butyrylcholinesterase (BuChE) lacks a distinct absorption peak found at about 1000 cm.sup.-1 in the BuChE-Malathion spectrum. The enzyme is used to collect and concentrate the agent or pollutant, and the resulting complexed enzyme can then be analyzed (e.g., by infrared spectroscopy) and its spectrum compared to an uninhibited enzyme spectrum.

Abstract: The enzyme cholesterol esterase is produced by cultivating a strain of the Achromobacter delicatulus type, isolated from vegetable debris and identified by the symbol NRRL B-12115. Under the described culture conditions, the enzyme is exocellular and therefore does not require extraction from the cells.In addition, the micro-organism has a duplication time less than that of moulds and Actinomycetes. Cholesterol esters of fatty acids can be hydrolysed by adding them to the culture medium before inoculating the strain.

Abstract: A novel hydroxy-cinnamic acid ester hydrolase can be obtained by cultivating, in a medium, a mold strain belonging to Genus Aspergillus or Genus Botrytis and having an ability to produce a hydroxy-cinnamic acid ester hydrolase specifically hydrolyzing the ester linkage of hydroxy-cinnamic acid ester substances represented by the following general formula: ##STR1## wherein R is hydrogen atom, hydroxyl group or methoxyl group and X is tartaric acid residue or quinic acid residue, followed by collecting the hydroxy-cinnamic acid ester hydrolase from the cultivated product.

Abstract: The present invention provides a process for obtaining cholesterol esterase from micro-organisms of the genus Pseudomonas, wherein Pseudomonas sp. DSM 1280 or DSM 1281 is cultured in an appropriate culture medium in the presence of an inducer and the enzyme is obtained from the culture medium and/or from the cells.

Abstract: The present invention provides a process for obtaining cholesterol esterase from micro-organisms, wherein a micro-organism capable of cholesterol esterase formation is cultured in an appropriate nutrient medium in the presence of lecithin as inducer and the enzyme is obtained from the culture medium and/or from the cells.

Abstract: The microorganism Streptomyces capillispira, NRRL 12279, produces an enzyme which deesterifies cephalosporin methyl esters.

Abstract: 9-(2-O-Acyl-.beta.-D-arabinofuranosyl)adenine compounds and their production by enzymatic removal of the 3-O-acyl and 5-O-acyl groups of a 9-(2,3-di-O-acyl-.beta.-D-arabinofuranosyl)adenine compound or a 9-(2,3,5-tri-O-acyl-.beta.-D-arabinofuranosyl)adenine compound. The monoester compounds are useful as antiviral agents. The compounds are water-soluble and lipophilic, thereby being adaptable to a wide variety of pharmaceutical formulations.

Abstract: A novel pectin esterase which randomly hydrolyzes the methyl ester bond of pectin can be obtained by cultivating, on a medium, a mold strain belonging to Genus Aspergillus, Genus Penicillium, Genus Fusarium or Genus Sclerotinia and having an ability to produce said novel pectin esterase. A demethoxylated pectin having a uniform methoxyl group content can be obtained by adding said novel pectin esterase to pectin. The demethoxylated pectin thus obtained can be utilized as gelling agent, emulsifier or thickener for food processing.