Abstract: A saccharide composition containing trehalulose, which is obtainable by allowing a maltose/trehalose converting enzyme to act on a sucrose solution to produce trehalulose, and collecting the resulting trehalulose-containing mixture. Since the enzyme converts sucrose into trehalulose in a relatively high yield and the conversion rate is controllable, a saccharide composition rich in trehalulose is readily obtained on an industrial scale.

Abstract: A method for production of toxin-binding, non-toxic, modified, biopolymers and the use thereof for the treatment of septic shock, infections and toxic states and to the use of them as carriers for transportation of biologically or therapeutically important materials (enzymes or drugs) into phagocytes or cells bearing Fc and complement receptors and as a natural source of energy for cells. The toxin binding, non-toxic structurally modified biopolymers are prepared by the reaction of polysaccharides containing alpha 1,4 or 1,6 linkages with glucose-1-phosphate catalyzed by glycogen phosphorylase enzyme in a buffer solution at pH 6.8-7.4 at a temperature of 20.degree.-30.degree. C. and by the separation of the obtained biopolymers in a well-known manner.

Abstract: A recombinant cyclodextrin glucanotransferase mutant is provided, which mutant produces lowered amounts of .beta.-cyclodextrins and .gamma.-cyclodextrins compared to wild-type cyclodextrin glucanotransferase.

Abstract: The present invention is directed to nucleic acids encoding glycosyltransferases, the proteins encoded thereby, and to methods for synthesizing oligosaccharides using the glycosyltransferases of the invention. In particular, the present application is directed to identification a glycosyltransferase locus of Neisseria gonorrhoeae containing five open reading frames for five different glycosyltransferases. The functionally active glycosyltransferases of the invention are characterized by catalyzing reactions such as adding Gal .beta.1.fwdarw.4 to GlcNAc or Glc; adding GalNAc or GlcNAc .beta.1.fwdarw.3 to Gal; and adding Gal .alpha.1.fwdarw.4 to Gal. The glycosyltransferases of the invention are particularly suited to the synthesis of the oligosaccharides Gal.beta.1.fwdarw.4GlcNAc .beta.1.fwdarw.3Gal.beta.1.fwdarw.4Glc (a mimic of lacto-N-neotetraose), GalNAc.beta.1.fwdarw.3Gal.beta.l.fwdarw.4GlcNAc.beta.1.fwdarw.3Gal.beta.1. fwdarw.4Glc.beta.1.fwdarw.4 (a mimic ganglioside), and Gal.alpha.1.fwdarw.4Gal.beta.1.

Abstract: Novel non-reducing oligosaccharide having a structure represented by the formula of alpha-D-oligoglucosyl alpha-D-oligoglucoside is obtained by exposing either an aqueous solution which contains trehalose and an alpha-glucosyl saccharide or an aqueous solution which contains a non-reducing saccharide bearing a trehalose structure at its end to a saccharide-transferring enzyme. The oligosaccharide has a reduced sweetness, superior stability, appropriate viscosity and less or no susceptibility to crystallization or superior solubility when in crystalline form. These features make the oligosaccharide very useful in various compositions including foods, beverages, cosmetics, pharmaceuticals and shaped bodies.

Abstract: A method for genetically engineering cells to produce soluble and secretable Golgi processing enzymes instead of naturally occurring membrane-bound enzymes. Cells are genetically engineered to express glycosyltransferases which lack both a membrane anchor and a retention signal. The resulting altered enzyme becomes soluble and secretable by the cell without losing its catalytic activity. Secretion of the soluble glycosyltransferase by the cell provides for increased production and simplified recovery of glycosyltransferase.

Abstract: Disclosed is a process of enzymatically preparing .alpha.-glucoside esters. First, .alpha.-glucosides are produced by placing an acyclic alcohol or a mixture of acyclic alcohols having a water solubility of at least 2.7% v/v at 20.degree. C. in contact with starch, maltodextrins or maltose, in the presence of a purified enzymatic preparation having .alpha.-transglucosylation activity, wherein the enzymatic preparation is free of .beta.-glucosidase activity. Then, the .alpha.-glucosides are contacted with at least one fatty acid and a preparation having lipase activity to produce the .alpha.-glucoside esters, which may then be recovered. The preparation having .alpha.-transglucosylation activity may originate from a fungus such as Talaromyces duponti, Aspergillus niger, Aspergillus oryzae or Aspergillus batatae.

Abstract: Oligosaccharide compounds that are substrates and inhibitors of glycosyltransferase and glycosidase enzymes and compositions containing such compounds are disclosed. A method of glycosylation is also disclosed. An E. coli transformed with phagemid CMPSIL-1, which phagemid comprises a gene for a modified CMP-sialic acid synthetase enzyme, which transformed E. coli has the ATCC accession No. 68531 is also provided.

Abstract: A .beta.-fructofuranosidase with a molecular weight of 49,000.+-.5,000 daltons on SDS-PAGE, an isoelectric point of 4.6.+-.0.5, an optimum pH of about 5.5-6.0, and an optimum temperature of about 50.degree. C. in the presence of calcium ion. The enzyme acts on saccharides with a .beta.-fructofuranosidic linkage and other substances including other saccharides, sugar alcohols, and alcohols to produce fructosyl-transferred saccharides in a relatively high yield.

Abstract: The present invention is directed to the modification of reserve polysaccharides in plants. Specifically, it has been found that host plants can be successfully transformed with a nucleic acid sequence capable of expressing a chimeric reserve polysaccharide modification enzyme gene sequence which will synthesize novel reserve polysaccharides in plants or convert the transformed plant's endogenous starch reserves to novel starch degradation products.

Abstract: Extracellular fructosyltransferase of Acetobacter diazotrophicus was isolated and purified and its enzymatic properties were established. Cloning, sequencing and genetic manipulation of the fructosyltransferase gene so as to produce high levels of the enzyme in recombinant prokaryotic and eukaryotic cells. Both natural and recombinant fructosyltransferase of Acetobacter diazotrophicus produce fructose-containing oligosaccharides and fructans. The enzyme yields in particular high levels of fructooligosaccharides from sucrose, such as kestose and kestotetraose which can be used as natural low-calorie sweeteners.

Abstract: The present invention provides improved methods for the formation of glycosidic linkages. These methods are useful for the preparation of compounds of formula:NeuAc.alpha.(2.fwdarw.3)Gal.beta.(1.fwdarw.4)(Fuc.alpha. 1.fwdarw.3)GlcN(R').beta.(1.fwdarw.3)Gal.beta.

Abstract: The present invention is directed to nucleic acids encoding glycosyltransferases, the proteins encoded thereby, and to methods for synthesizing oligosaccharides using the glycosyltransferases of the invention. In particular, the present application is directed to identification a glycosyltransferase locus of Neisseria gonorrhoeae containing five open reading frames for five different glycosyltransferases. The functionally active glycosyltransferases of the invention are characterized by catalyzing reactions such as adding Gal .beta..fwdarw.4 to GlcNAc or Glc; adding GalNAc or GlcNAc .beta.1.fwdarw.3 to Gal; and adding Gal .alpha.1.fwdarw.4 to Gal. The glycosyltransferases of the invention are particularly suited to the synthesis of the oligosaccharides Gal.beta.1.fwdarw.4GlcNAc.beta.1.fwdarw.3Gal.beta.1.fwdarw.4Glc (a mimic of lacto-N-neotetraose), GalNAc.beta.1.fwdarw.3Gal.beta.1.fwdarw.4GlcNAc.beta.1.fwdarw.3Gal.beta.1. fwdarw.4Glc.beta.1.fwdarw.4 (a mimic ganglioside), and Gal.alpha.1.fwdarw.4Gal.beta.1.

Abstract: The present invention provides a novel .beta.1.fwdarw.6 N-acetylglucosaminyltransferase, which forms core 2 oligosaccharide structures in O-glycans, and a novel acceptor molecule, leukosialin, CD43, for core 2 .beta.1.fwdarw.6 N-acetylglucosaminyltransferase activity. The amino acid sequences and nucleic acid sequences encoding these molecules, as well as active fragments thereof, also are disclosed. A method for isolating nucleic acid sequences encoding proteins having enzymatic activity is disclosed, using CHO cells that support replication of plasmid vectors having a polyoma virus origin of replication. A method to obtain a suitable cell line that expresses an acceptor molecule also is disclosed.

Abstract: Disclosed is a novel non-reducing oligosaccharide with neotrehalose structure represented by the general formula as shown by: ##STR1## The oligosaccharide is obtainable by exposing an aqueous solution containing neotrehalose to a saccharide-transferring enzyme, and has a superior stability, reduced sweetness, appropriate viscosity, no susceptibility to crystallization and less fermentability. These features make it very useful in various compositions including foods, beverages, cosmetics and pharmaceuticals.

Abstract: .alpha.-Glycosyl hesperidin, a novel hesperidin derivative wherein equimolar or more D-glucose residues are bound to hesperidin via the .alpha.-bond, is formed by a saccharide-transferring enzyme in a liquid containing hesperidin and .alpha.-glucosyl saccharide. The .alpha.-glycosyl hesperidin is easily recovered from the reaction mixture with a synthetic macroporous resin. .alpha.-Glycosyl hesperidin is superior in water-solubility, substantially tasteless and odorless, free of toxicity, and readily hydrolyzable in vivo into hesperidin and D-glucose to exhibit the physiological activity inherent to hesperidin. Thus, .alpha.-glycosyl hesperidin is favorably usable in vitamin P-enriching agents, foods, beverages, tobaccos, foods, pet foods, pharmaceuticals for susceptive diseases, cosmetics and plastics.

Abstract: There is disclosed a variant-type carbohydrate hydrolase that has been increased transglycosylation activity by substituting another amino acid residue for the tyrosine residue that is present in the active center of the hydrolase, which hydrolase is an amylase or an enzyme analogous to amylase; a gene or a DNA sequence of the carbohydrate hydrolase with mutation introduced into the base sequence that encodes the tyrosine residue; and a vector or a transformant which comprises the DNA sequence. There is also disclosed a method for producing a variety of oligosaccharides and the like by using the variant-type carbohydrate hydrolase.

Abstract: A cyclodextrin having a galactosyl group which is bonded to a 6-hydroxyl group of a glucosyl group of the cyclodextrin via an .alpha.-bond or a .beta.-bond; a cyclodextrin having a mannosyl group which is bonded to a 6-hydroxyl group of the cyclodextrin via an .alpha.-bond.

Abstract: A method of producing a mannosyl-cyclodextrin having a mannosyl group bonded to the hydroxyl group of the glucosyl group of a cyclodextrin via an alpha-bond. The method includes treating a liquid containing a cyclodextrin and an alpha-mannosyl compound with an alpha-mannosyl transfer agent.

Abstract: A cyclodextrin which when added to water produces a haze-free solution is made by the use of starch which contains at least about 90% amylopectin in a two-stage process wherein first a starch hydrolysate is formed by means of an alpha-amylase or an acid and a second subsequent step wherein the cyclodextrin is formed by means of a cyclodextrin-glycosyl-transferase.

Abstract: Anti-inflammatory compounds are useful, for example, in treating arthritis and heart attack patients. Novel oligosaccharides useful in the rapid synthesis of certain anti-inflammatory compounds are disclosed, as is a rapid method of synthesizing the oligosaccharides. Low pH can loosen the acceptor specificity of galactosyltransferase (lactose synthase: EC 2.4.1.22), allowing the rapid synthesis of novel oligosaccharides. The disaccharides cellobiose (.beta.1.fwdarw.4), laminaribiose (.beta.1.fwdarw.3), gentiobiose (.beta.1.fwdarw.6) and maltose (.alpha.1.fwdarw.4) acted as acceptors for lactose synthase under low pH conditions. From these four acceptors, the following four novel trisaccharides were synthesized: Gal.sub.p (.beta.1.fwdarw.4)Glc.sub.p (.beta.1.fwdarw.3)-Glc, Gal.sub.p (.beta.1.fwdarw.4)Glc.sub.p (.beta.1.fwdarw.4)-Glc, Gal.sub.p (.beta.1.fwdarw.4)Glc.sub.p (.beta.1.fwdarw.6)-Glc and Gal.sub.p (.beta.1.fwdarw.4)Glc.sub.p (.alpha.1.fwdarw.4) Glc.

Abstract: Disclosed are novel non-reducing saccharide-forming enzyme, and its preparation and uses. The enzyme is obtainable from the culture of microorganisms such as Rhizobium sp. M-11 (FERM BP 4130) and Arthrobacter sp. Q36 (FERM BP-4316), and capable of forming non-reducing saccharides having a trehalose structure when allowed to act on reducing partial starch hydrolysates. Glucoamylase and .alpha.-glucosidase readily yield trehalose when allowed to act on the non-reducing saccharides. These non-reducing saccharides and trehalose are extensively useful in food products, cosmetics and pharmaceuticals.

Abstract: This invention relates to an apparatus containing specific binary combinations of glycosyltransferases, for the synthesis of specific saccharide compositions such as, for example, oligosaccharides, polysaccharides, glycolipids, and glycopeptides.

Abstract: A novel .alpha.-glycosyl quercetin, wherein at least equimolar D-glucose residues are attached to quercetin via the .alpha.-bond, has a satisfactory water-solubility, light tolerance and stability, and exerts the inherent activity of quercetin in vivo. The .alpha.-glycosyl quercetin is prepared by a process comprising subjecting a solution containing quercetin and an .alpha.-glucosyl saccharide to the action of a saccharide-transferring enzyme to form an .alpha.-glycosyl quercetin, and recoverying the resultant .alpha.-glycosyl quercetin. The .alpha.-glycosyl quercetin can be advantageously used in combination with other materials in food products, cosmetic compositions and pharmaceutical compositions as a highly-safe and natural vitamin P-enriched agent, yellow-color-imparting agent, antioxidant, deodorant, stabilizer, quality-improving agent, antiseptic, prophylactic agent, therapeutic agent and ultraviolet-absorbing agent.

Abstract: A process for producing trehalose from inexpensive saccharide raw materials via an enzymic method uses stable enzymes with high productivity. The process includes incubating a saccharide raw material and an inorganic phosphoric acid and/or a salt thereof in the presence of phosphorylase to produce .alpha.-glucose 1-phosphate, and contacting the produced .alpha.-glucose 1-phosphate with glucose in the presence of a trehalose phosphorylase to produce trehalose. The isolation and purification of trehalose is easier in comparison to conventional fermentation methods.

Abstract: The present invention; is a method of producing .beta.-cyclodextrin at a higher efficiency from a raw material other than starch, comprising making a malto-oligosaccharide with 2 to 10 glucoses co-exist with cyclodextrin glucanotransferase in a solution containing an organic solvent which can precipitate 50% or more of .beta.-cyclodextrin when an excessive amount of the solvent is added to the solution of the .beta.-cyclodextrin and effecting the reaction at a lower temperature than 40.degree. C.

Abstract: The sequence of cyclomaltodextrin glucanotransferase (CGTase) gene derived from a microorganism of genus Bacillus and the amino acid sequence of CGTase are determined. A recombinant DNA carrying the CGTase gene is introduced by in vitro genetic engineering technique into a host microorganism of species Bacillus subtilis or Escherichia coli. The recombinant microorganism carrying the recombinant DNA autonomically proliferates to secrete a large amount of CGTase.

Abstract: A method for genetically engineering cells to produce soluble and secretable Golgi processing enzymes instead of naturally occurring membrane-bound enzymes. Cells are genetically engineered to express glycosyltransferases which lack both a membrane anchor and a retention signal. The resulting altered enzyme becomes soluble and secretable by the cell without losing its catalytic activity. Secretion of the soluble glycosyltransferase by the cell provides for increased production and simplified recovery of glycosyltransferase.

Abstract: Disclosed are (1) a novel galactosyl-cyclodextrin having a galactosyl group as bonded to the hydroxyl group of the glucosyl group of a cyclodextrin via an .alpha.-bond and a method of producing said galactosyl-cyclodextrin; (2) a novel galactosyl-cyclodextrin having a galactosyl group as bonded to the hydroxyl group of the glucosyl group of a cyclodextrin via a .beta.-bond and a method of producing said galactosyl-cyclodextrin; and (3) a novel mannosyl-cyclodextrin having a mannosyl group as bonded to the hydroxyl group of the glucosyl group of a cyclodextrin via an .alpha.-bond and a method of producing said mannosyl-cyclodextrin. The new branched cyclodextrins are expected to be widely useful in various fields of drug industry, food industry and cosmetic industry.

Abstract: Disclosed is a novel non-reducing oligosaccharide with neotrehalose structure represented by the general formula as shown by: ##STR1## The oligosaccharide is obtainable by exposing an aqueous solution containing neotrehalose to a saccharide-transferring enzyme, and has a superior stability, reduced sweetness, appropriate viscosity, no susceptibility to crystallization and less fermentability. These features make it very useful in various compositions including foods, beverages, cosmetics and pharmaceuticals.

Abstract: A one-pot glycosylation reaction is disclosed in which a N-acetylgalactosamine (GalNAc) or N-acetylglucosamine (GlcNAc) group is enzymatically transferred to an acceptor molecule. The starting glycoside is a N-acetylamino monosaccharide 1-phosphate that is enzymatically converted to its UDP derivative via UTP and a pyrophorylase. The formed UDP derivative is epimerized, and the epimerized UDP derivative is used in the enzyme-catalyzed glycosyl transfer. That enzyme-catalyzed glycosyl transfer to an acceptor releases UDP that is enzymatically converted to UTP for further conversion of the N-acetylamino monosaccharide 1-phosphate into its UDP derivative.

Abstract: Disclosed is a novel non-reducing oligosaccharide with neotrehalose structure represented by the general formula as shown by: ##STR1## The oligosaccharide is obtainable by exposing an aqueous solution containing neotrehalose to a saccharide-transferring enzyme, and has a superior stability, reduced sweetness, appropriate viscosity, no susceptibility to crystallization and less fermentability. These features make it very useful in various compositions including foods, beverages, cosmetics and pharmaceuticals.

Abstract: Novel cyclodextrin glycosyl transferases (CGTase) can be produced by anaerobic cultivation of strains of Thermoanaerobacter or Thermoanaerobium. They are more thermostable than known CGTases and have temperature optimum about 95.degree. C.The novel CGTases can be used for starch liquefaction at pH 4.5 and temperature exceeding 100.degree. C. in the production of dextrose or ethanol. They can also be used for conversion of liquefied starch to cyclodextrin at a temperature of 80.degree.-90.degree. C.A method for enzymatically converting solid and liquefied starch into cyclodextrin using cyclodextrin glycosyl transferases (CGTase) elaborated by thermophilic obligate anaerobic strains belonging to the genus Clostridium. These CGTases are characterized by thermostability and a capability to liquefy starch and/or to convert liquefied starch to cyclodextrin at pH 5.0-5.5 and 60.degree.-90.degree. C.

Abstract: A method of assaying for glycosyltransferase activity in a sample. In a first step, a sample is reacted with a first sugar donor and an acceptor substrate to produce a transferase product. The first sugar donor and acceptor substrate are selected such that the sugar from the first sugar donor is capable of being transferred to the acceptor substrate in the presence of the glycosyltransferase to be assayed. In a second step, the transferase product is reacted with a second sugar donor having a sugar which is labelled with a labelling agent and an enzyme which is capable of transferring the sugar from the second sugar donor to the transferase product to produce a labelled transferase product and which has a higher affinity for the glycosyltransferase product compared to the affinity of the glycosyltransferase for the acceptor substrate. The labelling agent activity of the labelled transferase product or unreacted second sugar donor is assayed to determine transferase activity in the sample.

Abstract: The particular strain of Klebsiella oxytoca No. 19-1 has been isolated from soil which produces a cyclomaltoglucanotransferase enzyme capable of converting starch to .alpha.-cyclodextrin in very high proportion, nearly close to 100 percent, rather than another types of cyclodextrins.

Abstract: A cyclodextrin glycosyltransferase (CGTase) which, in the conversion of starch or starch-like substrates to CD, produces .gamma.-CD in an increased amount, and whose protein sequence, in the region between amino acid position 180 and amino acid position 240, contains the amino acid sequence (SEQ ID NO: 1), where position 1 of the protein sequence is the beginning of the signal peptide of the CGTase and Xxx denotes a natural amino acid.

Abstract: The present invention discloses a method of synthesizing a novel form of cellulose I as well as methods of synthesizing a novel form of cellulose I in vitro. One method comprises contacting an activated saccharide substrate with an endoglucanase in an appropriate organic solvent/buffer ratio. The invention also encompasses a partially purified endoglucanase and a method of synthesizing cellooligosaccharides. A second method comprises contacting a nucleotide sugar with a purified glycosyl transferase in an appropriate buffer medium to insure polymerization and crystallization of parallel glucan chains from the enzyme/micelle complex to form cellulose I.

Abstract: Method of producing oat extract from rolled oats and oat flour by performing a series of mixing, cooking, filtering and concentrating steps. The method comprises the steps of mixing rolled white oats with oat flour, bacterial or fungal enzymes, and water to form an oat/enzyme solution. The oat/enzyme solution is then mashed by cooking the solution to convert the starches present in the oats into sugars. The undissolved solids remaining from the rolled oats are separated from the oat mash by filtering the cooked oat mash using some of the undissolved solids as a filter bed. The filtering operation produces oat wort which is then concentrated to produce oat extract.

Abstract: A method of preparing a hetero-branched cyclodextrin comprising a glucosyl or a maltosyl group side chain and a mannosyl group .alpha.-bonded to a hydroxyl group of the glucosyl group or the maltosyl group of the side chain, the method involving reacting a liquid containing a branched cyclodextrin having a glucosyl or maltosyl group as the side chain and an .alpha.-mannosyl compound with an .alpha.-mannosyl transfer enzyme.

Abstract: Disclosed is a novel non-reducing saccharide-forming enzyme. The enzyme can be obtained from the culture of microorganisms such as Rhizobium sp. M-11 (FERM BP 4130) and Arthrobacter sp. Q36 (FERM BP-4316), and is capable of forming non-reducing saccharides having a trehalose structure when allowed to act on reducing partial starch hydrolysates having a degree of polymerization of 3 or greater. Glucoamylase and .alpha.-glucosidase readily yield trehalose when allowed to act on the non-reducing saccharides. These non-reducing saccharides and trehalose are useful in food products, cosmetics and pharmaceuticals.

Abstract: The present invention relates to a novel cycloisomaltooligosaccharide selected from the group consisting of novel cycloisomaltoheptaose having a cyclic structure composed of 7 glucose residues in .alpha.-1,6 linkage, novel cycloisomaltooctaose having a cyclic structure composed of 8 glucose residues in .alpha.-1,6 linkage and novel cycloisomaltononaose having a cyclic structure composed of 9 glucose residues in .alpha.-1,6 linkage, novel cycloisomaltooligosaccharide synthase forming said oligosaccharides from dextran, and a process for producing said oligosaccharides by use of said enzyme or a microorganism capable of producing said enzyme.

Abstract: Anti-inflammatory compounds are useful, for example, in treating arthritis and heart attack patients. Novel oligosaccharides useful in the rapid synthesis of certain anti-inflammatory compounds are disclosed, as is a rapid method of synthesizing the oligosaccharides. Low pH can loosen the acceptor specificity of galactosyltransferase (lactose synthase: EC 2.4.1.22 ), allowing the rapid synthesis of novel oligosaccharides. The disaccharides cellobiose (.beta.1.fwdarw.4) , laminaribiose (.beta.1.fwdarw.3) , gentiobiose (.beta.1.fwdarw.6) and maltose (.alpha.1.fwdarw.4) acted as acceptors for lactose synthase under low pH conditions. From these four acceptors, the following four novel trisaccharides were synthesized: Gal.sub.p (.beta.1.fwdarw.4)Glc.sub.p (.beta.1.fwdarw.3)-Glc, Gal.sub.p (.beta.1.fwdarw.4)Glc.sub.p (.beta.1.fwdarw.4)-Glc, Gal.sub.p (.beta.1.fwdarw.4)Glc.sub.p (.beta.1.fwdarw.6)-Glc and Gal.sub.p (.beta.1.fwdarw.4)Glc.sub.p (.alpha.1.fwdarw.4)Glc.

Abstract: A process for preparing difucosyl Y.sub.2 antigen (dimeric Le.sup.x) , said process comprising: (1) preparing a lactonorhexaosylceramide backbone or a lactonorhexaosylsaccharide backbone linked to a carrier molecule; and (2) enzymatically fucosylating said backbone at the III.sup.3 and V.sup.3 positions through an .alpha.1.fwdarw.3 linkage. A process for preparing Le.sup.y antigen analogues, said process comprising: (1) preparing a lactonorhexaosyl-ceramide backbone or a lactonorhexaosylsaccharide backbone linked to a carrier molecule; and (2) enzymatically fucosylating said backbone at the terminal .beta.-Gal through an .alpha.1.fwdarw.2 linkage; and (3) enzymatically fucosylating said backbone at one or more positions through an .alpha.1.fwdarw.3 linkage, provided that steps (2) and (3) can be conducted simultaneously or in any order.

Abstract: Two nucleotide sequences encoding two different polypeptides found in yeast trehalose synthase have been isolated and cloned. The coding sequences can be inserted into suitable vectors and used to transform host cells. The transformed cells will produce increased amounts of trehalose compared to the untransformed wild types and have increased tolerance to a variety of stresses, in particular to decreased availability of water. The invention may be used to improve the stress tolerance of organisms, to increase the storage life of foodstuffs and to produce trehalose economically on an industrial scale in an organism (e.g, baker's yeast) that is a traditional and safe foodstuff.

Abstract: A single vessel cyclic synthesis process for preparation of a sialyl.alpha.2.fwdarw.3.beta.galactoside is disclosed. In accordance with this process, a sialyltransferase acceptor is sialylated in an aqueous reaction medium by an .alpha.(2,3)sialyl transferase and CMP-sialic acid to form a sialyl donor substrate and CMP. In the presence of the trans-sialidase of Trypanosoma crusi, that sialyl donor substrate provides a sialyl group for a trans-sialidase acceptor, thereby preparing the sialyl.alpha.2.fwdarw.3.beta.galactoside. The .alpha.(2,3)sialyltransferase acceptor is reformed upon trans-sialidation of the latter acceptor, and the sialyl donor substrate is reformed using the .alpha.(2,3)sialyltransferase and a CMP-sialic acid recycling system that combines CMP with sialic acid that is also present in the vessel. The K.sub.m /V.sub.max value for the .alpha.(2,3)sialyltransferase acceptor is less than one-tenth the value of K.sub.m /V.sub.max of the trans-sialidase acceptor for the .alpha.

Abstract: 2-O-.alpha.-D-Glucopyranosyl-L-ascrobic acid is crystallizable in its supersaturated solution. Crystalline 2-O-.alpha.-D-glucopyranosyl-L-ascorbic acid is substantially nonhygroscopic, free flowing, free of deliquescence, consolidation and direct reducing activity, but is readily soluble in water. Because of these, characteristics crystalline 2-O-.alpha.-D-glucopyranosyl-L-ascorbic acid is handleable with an ease, and superiorly high in stability and physiological activities. Thus, crystalline 2-O-.alpha.-D-glucopyranosyl-L-ascorbic acid is favorably useful in vitamin C-enriching agents, foodstuffs, pharmaceuticals and cosmetics.

Abstract: A process for the production of cyclodextrins, comprising reacting non-treated starch with cyclodextrin-glycosyl-transferase produced by Bacillus ohbensis (FERM BP-3180), or produced by a mutant derived from Bacillus ohbensis (e.g., FERM BP-3180), or produced by any other strain in which the CGTase gene from B. ohbensis has been cloned, in an aqueous solution at pH between 6.5 and 8.8 and extracting the cyclodextrins from the reaction mixture by ultrafiltration, is provided.

Abstract: A single reaction vessel process for the synthesis of a sialylated galactoside is disclosed. The synthesis utilizes a .beta.-galactosidase to catalyze the reaction of a galactose-containing substrate and an acceptor to form a new galactosyl glycoside that is then sialylated using a cyclic multienzyme synthesis system to form CMP-sialic acid that sialylates the formed galactosyl glycoside in the presence of an .alpha.-sialyltransferase. The value of K.sub.m /V.sub.max for the formed galactosyl glycoside as a substrate for the .alpha.-sialyltransferase is less than one-third the K.sub.m /V.sub.max value for the galactose-containing substrate for that .alpha.-sialyltransferase.

Abstract: A simplified process is provided for producing saccharides of definite chain length, such as glucose, maltose and maltooligosaccharides, each in an isolated state and with a high purity.The process comprises transferring a saccharide chain, using a saccharide chain transferase, from a saccharide chain source to a substance substantially separable from the saccharides mentioned above and treating the thus-obtained oligosaccharide with an enzyme capable of excising the saccharide chain of definite chain length in an exo manner.

Abstract: The present invention provides a novel .beta.1.fwdarw.6 N-acetylglucosaminyltransferase, which forms core 2 oligosaccharide structures in O-glycans, and a novel acceptor molecule, leukosialin, CD43, for core 2 .beta.1.fwdarw.6 N-acetylglucosaminyltransferase activity. The amino acid sequences and nucleic acid sequences encoding these molecules, as well as active fragments thereof, also are disclosed. A method for isolating nucleic acid sequences encoding proteins having enzymatic activity is disclosed, using CHO cells that support replication of plasmid vectors having a polyoma virus origin of replication. A method to obtain a suitable cell line that expresses an acceptor molecule also is disclosed.