Abstract: The present invention discloses the preparation of R-configured trialkylsilylethynyl .alpha.-alcohols from similarly substituted .alpha.-ketones, and vice versa, catalyzed by the alcohol dehydrogenase of Lactobacillus kefir, ATCC No. 35411. Also disclosed is the acceptance or transfer of a hydride ion from or to the pro-R face of NADPH or NADP, respectively, as catalyzed by that enzyme.

Abstract: A process for the preparation of ascorbic acid-2-phosphate, which comprises reacting ascorbic acid or araboascorbic acid with a phosphate donor other than ATP in an aqueous medium in the presence of an effective amount of an enzyme derived and capable of preferentially catalyzing the enzymatic phosphorylation in the 2-position of ascorbic acid or araboascorbic acid by said phosphate donor, and recovering the resultant ascorbic acid-2-phosphate from the reaction solution.

Abstract: A method of preparing a soluble monovalent salt of a phosphatidyl ester which comprises reacting a phospholipid with a primary alcohol in the presence of an enzyme catalyst in a divalent cationic buffered solution and a water immiscible non-ether solvent that does not inactivate the enzyme, to form a divalent cationic salt of the phosphatidyl ester, and suspending the product in the presence of a stoichiometric amount of a monovalent cationic salt whose anion forms an insoluble salt with the divalent cation. The use of Centrifugal Partition Chromatography facilitates the enzyme reaction. The monovalent salt is preferably an ammonium/sodium mixed salt.

Abstract: Lysophospholipids-containing phospholipids with reduced neutral lipids content can be produced by a process which comprises subjecting neutral lipids- and lysophospholipids-containing phospholipids to treatment with acetone in the presence of an acid. In accordance with the present invention, it is possible to produce on a commercial scale by a simple procedure lysophospholipids-containing phospholipids wherein the neutral lipids content is reduced to 10% by weight or less of the total lipids content.

Abstract: The invention relates to a novel method for preparing pyrocatecholic compounds from monophenolic compounds using catalysis by monophenol monooxygenase in an aqueous solution containing metal ions. The metal ions form complexes with the pyrocatecholic products. This method increases the yield of pyrocatecholic products. In particular, the method of the instant invention can be used to increase the yield of L-DOPA, a drug used in the treatment of Parkinson's disease.

Abstract: A method is provided for converting therapeutic glycosidase inhibitors to novel prodrugs by phosphorylation of a free hydroxyl group on the molecule to substantially reduce the glycosidase inhibitory activity without thereby substantially reducing the therapeutic activity.

Abstract: A method for preparing highly purified phosphatidylinositol comprises the steps of treating a mixed phospholipid with a phospholipase D, then treating the product with an alkali or acidic phosphatase and separating unreated phosphatidylinositol from the reaction mixture. The method makes it possible to isolate phosphatidylinositol useful in various fields in a high purity in the order of 80 to 99%.

Abstract: A compound of the formula (I): ##STR1## wherein R.sup.1, R.sup.2, and R.sup.3 are --COOR.sup.4, --COOR.sup.5, and --COOR.sup.6, respectively; R.sup.4, R.sup.5, and R.sup.6 each is hydrogen, lower alkyl, or alkali metal; W is hydroxyl; X, Y, and Z each is hydrogen or hydroxyl; a dotted line indicates the presence or absence of a single bond; or where W/R.sup.3, X/R.sup.1, and/or Z/R.sup.3 may be combined together, a lactone is formed, which compound is useful as a phospholipase A.sub.2 inhibitor. Process for the production of the compound (I) and a cell culture of a microorganism Circinotrichum falcatisporum RF-641 producing the same are also provided.

Abstract: A method is provided for converting therapeutic glycosidase inhibitors to novel prodrugs by phosphorylation of a free hydroxyl group on the molecule to substantially reduce the glycosidase inhibitory activity without thereby substantially reducing the therapeutic activity.

Abstract: A method is provided for converting coal to low molecular weight organic compounds comprising combining an aqueous solution of an aqueous-soluble polymeric coal substrate with a lignin peroxidase, oxygen and hydrogen peroxide. The invention is exemplified using the lignin peroxidase from Phanerochaete chrysosporium. Also provided are aqueous-soluble polymeric coal substrates suitable for lignin peroxidase-catalyzed depolymerization and methods of preparing such substrates. Finally, a method is provided for isolating the lignin peroxidase from mycelia-free, unconcentrated media of cultures of P. chrysosporium producing the enzyme.

Abstract: A method producing a non-heme haloperoxidase which is substantially resistant to inactivation, at room temperature, in up to 0.3M H.sub.2 O.sub.2 for up to 25 hours, and up to 0.5mM HOCl for up to two minutes. One such haloperoxidase, isolated from Curvularia inaequalis, contains about 2 gram atoms of zinc per molecule. A halogenation reaction employing the enzyme can be performed at H.sub.2 O.sub.2 and hypohalous acid concentrations which produce rapid inactivation of heme-containing haloperoxidases.

Abstract: A halogenation method using a haloperoxidase obtained from a fungus selected from the dematiaceous hyphomycetes. The enzyme has an optimum activity above about pH 5.0, and can oxidize chloride, bromide, or iodide ions.

Abstract: An immunogenicity increasing carrier substance for immunogenic determinants is composed of particles derived from gram-negative cells substantially devoid or depleted of their natural immunogenic determinants, more particularly prepared by stripping the O-antigen and core region off the lipid A by chemical cleavage (acid hydrolysis). These socalled "naked bacteria" are chemically treated with a linking reagent to provide covalently bonded intermediate linking moieties while preserving the adjuvant effect of the particles. The linking moieties have functional groups. These serve for the covalent bonding of selected haptens or antigens comprising the desired immunogenic determinants against which antibodies are to be elicited in living antibody-producing cells.

Abstract: A process for producing a primary or secondary alcohol derivative of a phosopholipid which comprises reacting the phospholipid with a primary or secondary alcohol in the presence of phospholipase DM.

Abstract: A process for producing a sphingophospholipid derivative comprising reacting a sphingophospholipid with a specified compound having an alcoholic hydroxyl group selected from the group consisting of specified primary alcohol compounds, specified secondary alcohol compounds and specified saccharides or their phenol glycosides in the presence of phospholipase DM.

Abstract: Process for the production of 6-hydroxynicotinic acid by biotechnological methods. Nicotinic acid is enzymatically hydroxylated in the presence of equivalent quantities of magnesium or barium ions with the help of nicotinic acid-hydroxylating microorganisms. The resultant magnesium or barium salt of the 6-hydroxynicotinic acid is separated from the reaction mixture. Then the 6-hydroxynicotinic acid is freed from the separated salts. Examples of the microorganism are the species Pseudomonas, Bacillus or Achromobacter, for example, Achromobacter xylosoxydans. Preferably the enzymatic hydroxylation is carried out at 20.degree. to 40.degree. C. and a pH of 5.5 to 9.0 under aerobic conditions.

Abstract: A method of producing a non-heme haloperoxidase which is substantially resistant to inactivation, at room temperature, in up to 0.3M H.sub.2 O.sub.2 for up to 25 hours, and up to 0.5 mM HOCl for up to two minutes. One such haloperoxidase, isolated from Curvularia inaequalis, contains about 2 gram atoms of zinc per molecule. A halogenation reaction employing the enzyme can be performed at H.sub.2 O.sub.2 and hypohalous acid concentrations which produce rapid inactivation of heme-containing haloperoxidases.

Abstract: A halogenation method using a haloperoxidase obtained from a fungus selected from the dematiaceous hyphomycetes. The enzyme has an optimum activity above about pH 5.0, and can oxidize chloride, bromide, or iodide ions.

Abstract: A process for producing a saccharide derivative of a phospholipid, which comprises reacting a phospholipid with a monosaccharide having 5 to 7 carbon atoms, at least one primary alcohol group and at least three hydroxyl groups in total including the OH of the primary alcohol group or a disaccharide thereof, said saccharide being optionally substituted by a group selected from the class consisting of amino and acetylamino groups, or a phenol glycoside of said saccharide in the presence of phospholipase DM. The phospholipid-saccharide derivatives are useful as a liposome-forming substrate, or as an emulsifier for cosmetics, such as cream and lotion, fat solutions for transfusion and agricultural chemicals, such as pesticides and herbicides.

Abstract: There are disclosed polyprenyl sulfone derivatives of the general formula: ##STR1## wherein n represents an integer of 1-4, R.sub.1 represents an aryl group d R.sub.2 represents a hydroxymethyl or carboxyl group. The polyprenyl sulfone derivatives are prepared by cultivating a microorganism of the genus Nocardia capable of oxidizing a compound of the general formula: ##STR2## wherein n and R.sub.1 have the same meanings as defined above, in a culture medium containing a compound of the above general formula (II), and then collecting the oxidation product from the culture mixture. The polyprenyl sulfone derivatives are useful as intermediates for preparing various useful polyprenyl compounds.

Abstract: A phospholipid mixture, rich in N-acylphosphatidylserine (NAPS), is produced by growth of certain bacterial cultures in media containing effective amounts of tris (hydroxymethyl) aminomethane. NAPS may be isolated in high purity by chromatographic techniques.

Abstract: A compound having the formula ##STR1## can be prepared by enzymatically coupling a compound of the formula ##STR2## with a compound of the formula ##STR3## in the presence of Escherichia coli acylase at a pH of from about 4.0 to about 6.0.