Abstract: Postoperative scars are treated by a method of applying a microporous paper tape to the scar running along the length of the scar. A contact medium is applied to the exposed surface of the tape and penetrates to the skin. The contact medium comprises an expressed gel from the plant Bulbine frutescens and may contain asiaticoside and panthenol. These active ingedients are contained in a pharmaceutically acceptable cream. The contact material is applied each morning and evening. The tape is replaced when it falls away from the skin normally, e.g. every seven days and the treatment is then continued. Improved scar healing results from the use of this method.

Abstract: Disclosed are improved methods for treating cotton-containing fabrics and non-cotton containing cellulosic fabrics as well as the fabrics produced from these methods. In particular, the disclosed methods are directed to contacting cotton-containing fabrics and non-cotton containing cellulosic fabrics with a cellulase solution containing a fungal cellulase composition which is substantially free of all CBH I type cellulase components. Cotton-containing fabrics so treated possess decreased strength loss as compared to fabrics treated with a cellulase solution containing a complete cellulase composition.

Abstract: A keto ester reductase capable of being used in an NADH-dependent enzymatic reaction for converting .beta., .gamma. and .delta. ketonic acid esters into the corresponding optically active .beta., .gamma. and .delta. hydroxycarboxylic acid esters can be isolated from strains of Candida parapsilosis, Yarrowinia cellobiosa, Rhodococcus erythropolis or Pseudomonas acidovorans, preferably cultivated on a long -chain alkane and/or alkane acid-containing culture medium, approximately in the presence of an inductor. The microorganism is preferrably, Candida parapsilosis DSM 70125. A usable enzyme preparation can be recovered by fractionated PEG-precipitation from the cell raw extract: high specific activities (for example 1855 U/mg) may then be obtained by chromatographic purification.

Abstract: A chondroitinase II is isolated from Proteus vulgaris. This enzyme together with chondroitinase I, is useful for selectively and completely disinserting the ocular vitreous body from the neural retina of the eye. The chondroitinase II has the amino acid sequence of SEQ. ID No. 2, an isoelectric point of from about 8.4 to about 8.45, and a molecular weight of 111,772+27 daltons as determined by electrospray and 111,725+20 daltons as determined by laser desorption. Preferrably, the chondroitinase II and chondroitinase I are co-purified chondroitinases which can then be separately eluted from each other.

Abstract: This invention relates to the preparation of new, modified organisms, through challenge growth processes, that are viable in the extreme temperature, pressure and pH conditions and salt concentrations of an oil reservoir and that are suitable for use in microbial enhanced oil recovery. The modified microorganisms of the present invention are used to enhance oil recovery and remove sulfur compounds and metals from the crude oil. The processes are comprised of steps which successively limit the carbon sources and increase the temperature, pressure and salinity of the media. This is done until microbial strains are obtained that are capable of growing in essentially crude oil as a carbon source and at a temperature range from about 70.degree. C. to 90.degree. C., at a pressure range from about 2,000 to 2,500 psi and at a salinity range from about 1.3 to 35%.

Abstract: An isolated xylosidase from Bacillus stearothermophilus NRRL B-18659, Bacillus stearothermophilus NRRL B-18660 and Bacillus stearothermophilus NRRL B-18661 is disclosed. The xylosidase has a maximum activity at about pH 6.0 and at about 75.degree. C., maintains at least about 60% of its maximum activity at about 65.degree. C. and pH 7 after 4 hours, is resistant to end-product inhibition maintaining over 75% of maximum activity in the presence of 1 molar xylose and has an isoelectric point of about 5.0. The xylosidase can be used in a method of hydrolyzing xylan present in wood pulp at temperatures of at least about 60.degree. C. and a pH of at least about 7.0. The xylosidase is used along with at least two xylanases and an arabinofuranosidase isolated from the above Bacillus stearothermophilus strains.

Abstract: A microbial catalase having a catalase activity at 0.degree. C. of 95% or more of its catalase activity at 30.degree. C., when measured at pH 7, and a process for producing the same. The microbial catalase preferably has (1) an operative temperature of 0.degree. to 60.degree. C. and an optimum temperature of 0.degree. to 30.degree. C., (2) an optimum pH of 7 to 10, (3) a resistance to 10 mM potassium fluoride, (4) a molecular weight is 65,000.+-.3,000, when measured by SDS polyacrylamide gel electrophoresis, and (5) an isoelectric point is about 4.8, when measured by isoelectric focusing. The catalase is obtainable from Bacillus subtilis IAM 1206 (FERM BP-4844) or a mutant strain thereof.

Abstract: A reusable, miniature, implantable electrochemical sensor, a method of making the same, and a powder therefor are provided. Enzyme material is immobilized on bulk particulate matter, and a reaction chamber of the sensor is then filled therewith. The sensor is implanted in an environment where it comes into contact with a specific component of a fluid with which the enzyme material chemically reacts to produce electrical signals for measuring the reaction. The method preferred for preparing the powder which is used in the electrochemical sensor involves first covalently bonding a quantity of an enzyme to fine particles in powder form to immobilize the enzyme is cross-linked to a non-enzyme protein with a cross-linking agent. Finally, the particles are added containing the immobilized enzyme cross-linked to a protein from the first step to the enzyme cross-linked to a protein from the second step to obtain the powder.

Abstract: There is disclosed a novel microbial bioconversion process for the synthesis of a trans-hydroxy sulfone intermediate, which is the precursor to topical carbonic anhydrase inhibitors (TCAI's). TCAI's are effective in the treatment of glaucoma and ocular hypertension. The bioconversion process is carried out in the presence of the microorganism Rhodotorula rubra, or Rhodotorula piliminae and results in a trans-hydroxy sulfone which exhibits a diastereomeric excess of greater than 95%.

Abstract: An isolated sorbitol oxidase from Xanthomonas maltophilia FERM BP-4512 is disclosed. The oxidase catalyzes the reaction of D-sorbitol+O.sub.2 .fwdarw.D-glucose+H.sub.2 O.sub.2, has a substrate specificity for D-sorbitol, D-mannitol, D-xylitol, and D-arabitol, has an optimum pH of 6.5 to 7.5, and has a molecular weight of 54 kD as determined by gel filtration or 43 kD as determined by SDS-PAGE. The enzyme can be used for measuring a polyol in a sample and as a reagent in a kit used for determining the presence of D-sorbitol.

Abstract: A method of increasing xanthan gum production, comprising culturing a Xanthomonas campestris strain having a xanthan-increasing modification in a culture medium, wherein the modification is selected from the group consisting of (1) a mutation causing rifampicin-resistance; (2) a mutation causing bacitracin-resistance; or (3) exogenous genetic information controlling the synthesis of xanthan; and separating xanthan from the culture medium, is provided along with specific DNA sequences and Xanthomonas campestris strains showing increased xanthan gum production. The strain is preferably ATCC 55429.

Abstract: A protease obtainable from Dendryphiella arenaria DSM 6260 or Dendryphiella salina DSM 6332 is disclosed. The protease has a pl of approximately 9.1 as determined by isoelectric focusing, a molecular weight of approximately 18-20 kD as determined by SDS-PAGE, is active towards haemoglobin, casein, skimmed milk, and Suc-Ala-Ala-Pro-Phe-pNA and has immunochemical properties identical to those of a protease obtained from Dendryphiella arenaria DSM 6260 or Dendryphiella salina DSM 6332. A process for its production, use in a detergent composition and as a detergent additive are disclosed.

Abstract: Labelled triglyceride oils are produced for use in diagnostic breath test. The process involves the cultivation of microorganisms capable of producing the oils in an appropriately controlled environment wherein the microorganisms are fed .sup.13 C or .sup.14 C labeled carbon substrates to induce the microorganisms to produce the labeled oils. The preferred labelled carbon substrate is a substrate containing .sup.13 C. The oil produced is preferrably enriched in oleic acid. The microorganisms can be induced to produce the oil by nitrogen depletion during cultivation.

Abstract: A cocaine esterase has been isolated from a strain of the bacteria Pseudomonas maltophilta, The cocaine esterase catalyses the debenzoylation of cocaine, This reaction may be used in the detection of cocaine. The enzyme may be incorporated into sensors for this purpose. The cocaine esterase is preferably obtainable from Pseudomonas sp. NCIMB 40427. It catalyzes the debenzoylation of cocaine, has a molecular weight in the unaggregated form of about 120,000 daltons as determined by gel filtration, has esterase activity specifically at the benzoate ester linkage of cocaine, separates at a major band of Rf about 0.2 on PAGE in its aggregated form, and it is completely inhibited by 1 mM phenylmethylsulphonyl fluoride but ineffectively inhibited by 1 mM eserine, each determined at 30.degree. C. with respect to 2 mM cocaine as substrate.

Abstract: A D-arabinitol dehydrogenase enzyme is disclosed. The enzyme is capable of catalyzing the oxidation of D-arabinitol and substantially incapable of catalyzing the oxidation of D-mannitol and is substantially free of other enzymes capable of oxidizing D-mannitol. Also disclosed are methods for determining D-arabinitol. In one embodiment the method comprises the steps of providing in combination (1) a medium suspected of containing D-arabinitol and (2) a D-arabinitol dehydrogenase enzyme and examining the medium for the product of the oxidation of the D-arabinitol. The enzyme utilized is capable of catalyzing the oxidation of D-arabinitol and substantially incapable of catalyzing the oxidation of D-mannitol. Kits for conducting the present method are also disclosed. The D-arabinitol dehydrogenase in purified form has all of the characteristics of a D-arabinitol dehydrogenase which is obtainable from Candida tropicalis ATCC 750 or Candida shehatae.

Abstract: A method for reacting an enzyme in a non-aqueous organic solvent is disclosed. The method comprises preparing a lyophilizate of a salt which activates the enzyme and an enzyme wherein the lyophilizate contains a weight ratio of salt to enzyme of at least 60% salt sufficient to activate the enzyme in an organic solvent. The method then calls for dispersion of the lyophilizate in a non-aqueous organic solvent in the presence of a substrate for the enzyme.

Abstract: An enzyme composition having a synergetic phytate hydrolyzing activity comprising a phytase having phytate hydrolyzing activity at a pH of from 2.5 to 5.0 and an acid phosphatase having phytate hydrolyzing activity at a pH of 2.5, in a low ratio corresponding to a pH 2.5/5.0 activity profile of from 0.8/1.0 to 3/1. Said enzyme composition preferably displays a higher synergetic phytate hydrolyzing efficiency through thermal treatment. Fungal enzymes, especially those from Aspergillus, are preferred. Use of said enzyme composition in food, feed and fodder products to improve phytate hydrolysis.

Abstract: Carboxymethylcellulases 5430 and 5812 which show strong activity toward carboxymethylcellulose and lichenan, and moreover are broad in active pH range and active temperature range, stable in the presence of various surfactants and excellent in thermal stability and particularly, in alkali resistance. These enzymes can be advantageously used as formulation components for detergent compositions. The carboxymethylcellulases are isolated from Bacillus strains FERM BP-4087 and FERM BP-4088. Some of the characteristics of the enzymes include: a molecular weight of 26,000.+-.1,000 as estimated by gel filtration on Bio-Gel A 0.5 m, the ability to hydrolyze carboxymethylcellulose, two optimum pH values of about 7.7 and 9.5, and a temperature optimum at about 55.degree. C.

Abstract: A process for the production of glyoxylic acid by reacting glycolic acid with oxygen in an aqueous solution in the presence of an amine buffer capable of forming a chemical adduct with glyoxylic acid, and glycolate oxidase and catalase immobilized or co-immobilized on an insoluble support is disclosed. The reaction is carried out at a pH of 7 to 10, preferably 8 to 9.5, an initial concentration of glycolic acid of 200 to 2500 mM, a concentration of amine wherein the initial mole ratio of amine to glycolic acid is within the range of 1.0 to 3.0, a concentration of immobilized catalase of 50 to 100,00 IU/mL, preferably 350 to 14,000 IU/mL, an oxygen pressure of up to 50 atmospheres, preferably 15 atmospheres, an immobilized glycolate oxidase concentration of about 0.01 to 10 IU/mL, preferably about 0.1 to 4 IU/mL, and a temperature of 0.degree. to 40.degree. C. preferably 5.degree. to 15.degree. C. Preferred insoluble immobilization supports are Eupergit C-250L and Eupergit C (Oxirane acrylic beads).

Abstract: Five xylanases are purified from the microorganism, Microtetraspora flexuosa,preferably strain ATCC 35864. Each biochemically unique xylanase is thermostable and has optimal activity in alkaline conditions. These enzymes are excellent candidates for enhancing the delignification and bleaching of pulp. Furthermore, treating the pulp with the above enzymes prior to bleaching may reduce the amount of chlorine containing and/or peroxide chemicals required in the bleaching process.