WO2003046194A1 - Nouveaux disaccharides non reduits contenant $g(a)-galactosyl et leur procede de production - Google Patents

Nouveaux disaccharides non reduits contenant $g(a)-galactosyl et leur procede de production Download PDF

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Publication number
WO2003046194A1
WO2003046194A1 PCT/JP2002/012215 JP0212215W WO03046194A1 WO 2003046194 A1 WO2003046194 A1 WO 2003046194A1 JP 0212215 W JP0212215 W JP 0212215W WO 03046194 A1 WO03046194 A1 WO 03046194A1
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Prior art keywords
reducing
producing
galactose
galactosidase
galactosyl group
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PCT/JP2002/012215
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English (en)
Japanese (ja)
Inventor
Masamichi Okada
Shigeharu Mori
Hiroyuki Hashimoto
Koki Fujita
Kozo Hara
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Amano Enzyme Inc.
Bio Research Corporation Of Yokohama
Ensuiko Sugar Refining Co.,Ltd.
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Publication of WO2003046194A1 publication Critical patent/WO2003046194A1/fr

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    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07H—SUGARS; DERIVATIVES THEREOF; NUCLEOSIDES; NUCLEOTIDES; NUCLEIC ACIDS
    • C07H3/00—Compounds containing only hydrogen atoms and saccharide radicals having only carbon, hydrogen, and oxygen atoms
    • C07H3/04—Disaccharides
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07H—SUGARS; DERIVATIVES THEREOF; NUCLEOSIDES; NUCLEOTIDES; NUCLEIC ACIDS
    • C07H17/00—Compounds containing heterocyclic radicals directly attached to hetero atoms of saccharide radicals
    • C07H17/04—Heterocyclic radicals containing only oxygen as ring hetero atoms

Definitions

  • the present invention relates to a novel non-reducing disaccharide containing a 0; -galactosyl group and a method for producing the same.
  • the present invention relates to a non-reducing disaccharide, and methods for their preparation including the novel alpha _ galactosyl groups, in particular, non-reducing disaccharide G a 1 ⁇ 1 - 1; . 3 G a 1 ( hereinafter , G a1 is galactose,) and G a1 ⁇ 1-1 ⁇ G1c (hereinafter, G1c is glucose) and a method for producing them.
  • G a 1 hereinafter , G a1 is galactose,
  • G1c is glucose
  • trehalose G1c ⁇ 1-1-G1c
  • heat and acid resistance It is known that there is little adverse effect on other materials in food processing and preservation, such as the amino acid / protein is not damaged by a single reaction. In addition, it has excellent properties as a food material, such as a strong inhibitory effect on starch aging, protein denaturation, and lipid sleep.
  • a carbohydrate having a non-reducing end with a galactosyl group is naturally known as the trisaccharide raffinose permeribose, which has strong bifidobacterial selective growth activity and anti-cariogenic activity, as well as immune cell activation.
  • Various physiological functions such as action, anti-cancer effect, and improvement effect on atopic dermatitis have been reported. (Seipura Motoi-: Japanese Cancer Society-(General Assembly Article), 40, 13 2 (1 981), Taizo Nakura et al .: Food Industry, 2.2.28, 29, 1999).
  • non-reducing disaccharide containing a monogalactosyl group can be synthesized, the above-mentioned properties of trehalose or the functions of raffinose and melibiose can be provided, and as a result, excellent food and pharmaceutical materials can be provided. Can be expected.
  • non-reducing disaccharides containing an ⁇ -galactosyl group have conventionally been only Galal-laGlc described in JP-A-10-308488, and other sugars There is no known quality.
  • the present invention is to provide a novel non-reducing disaccharide containing a galactosyl group, which is expected as a useful food material or pharmaceutical material, and to provide a simple production method thereof. Aim. Disclosure of the invention
  • the present invention relates to a non-reducing disaccharide represented by the following formula (1).
  • the non-reducing disaccharide is prepared by subjecting a galactose or a substance containing galactose to a hypergalactosidase derived from a microorganism to produce an oligosaccharide containing an ⁇ -galactosyl group by a dehydration condensation reaction. It can be produced by decomposing the reducing sugar in the sugar and then separating it.
  • ⁇ -galactosidase was derived from Aspergillus niger (A spergi 11 usniger) APC-9319 strain (deposit number: FE RM BP—7680) which has excellent dehydration condensation reaction activity. Can be used.
  • the decomposition of the reducing sugar in the oligosaccharide produced in the above-mentioned production method can be performed by alkali decomposition.
  • the present invention also relates to a non-reducing disaccharide represented by the following formula (2).
  • the non-reducing disaccharide is obtained by reacting a substance containing galactose and glucose with ⁇ -galactosidase derived from a microorganism to form an oligosaccharide containing a single galactosyl group by a dehydration condensation reaction.
  • ⁇ a1-1 ⁇ Ga1 can be produced by hydrolyzing the reducing sugar in the oligosaccharide and then separating the oligosaccharide.
  • Hi-galactosidase was derived from Aspergillus niger APC-9319 strain (deposit number: FE RM BP-7680) which has excellent dehydration condensation reaction activity. Can be used.
  • the hydrolysis of Galal to lj3Gal mixed in the above production method can be carried out with one galactosidase. Further, the decomposition of the reducing sugar in the oligosaccharide produced in the above-mentioned production method can be carried out by alcohol decomposition.
  • microorganisms that produce monogalactosidase include, but are not limited to, microorganisms such as the genus Aspergillus (A spergi 11 us), the genus Penicillium (Penici 11 ium), and the genus Trichoderma (Trichoderma).
  • Aspergillus molds include Aspergillus
  • Punorebenorerentus (A spergi 1 1 uspulverulentus), as a genus of the genus Penicillium, Penicillium 'Citrinanum Penicillium 1 enium citrinum), Henicirium-Manore Chilean (Penicilli um mu lticolor), As the Trichoderma fungi, Trichoderma's viride (T richodermaviride) is preferable, and among them, Aspergillus ⁇ Niger (A spergillusniger) power is more preferable.
  • Aspernoregizoles' nigers (Aseergii11 uSniger)
  • Aspernoreginoles niger Aspergir1 11 uSniger
  • APC-9319 strain is particularly preferred. This strain was obtained by the applicant based on the Bustust Treaty, the Patent Organism Depositary Center, National Institute of Advanced Industrial Science and Technology (IPOD, Japan). Deposit No. 1 No. 1 Central No. 6) and its deposit number is FE RM BP—7680 (transferred from domestic deposit to international deposit, original deposit date August 29, 2000, national deposit) Accession number F ERM P—1 800 3).
  • Conidium head spherical to radial, conidia (optical microscope): spherical to subspherical, smooth to slightly rough, conidia (electron microscopy): rough (with bumps), diameter (3.5 to 4)
  • Leachate little formation (transparent to brown), odor: almost none, sterigmata: two-stage, colony growth rate (malt extract agar medium, culture at 25 ° C):> 85 mm (7 days) Culture),> 85 mm '(cultured for 12 days), growth rate of colonies (deep cultivated agar medium, 25 ° C culture): 60-67 mm (cultured for 7 days), 65-73 mm (cultured for 7 days) 1 2 days culture), settlement 0212215 color (malt extract agar medium): black (front), colorless (back), settlement color (Vapeckeast agar): black to gray-black (front), talium-gray-yellow (back)
  • This strain is classified into Aspergillus' Niker, Aspergillus nilu, niger, var. Niger, based on the conidial shape, the sterigmata, and the color of the colony.
  • ⁇ - galactosidase produced by this strain has extremely high dehydration condensation activity, and Candidaguilliermondii (C andidaguilliermondii), which is known to have the highest catalytic activity of dehydration condensation reaction among ⁇ -galactosidases in the past.
  • An oligosaccharide containing an ⁇ -galatatosyl group can be produced at a high yield from ⁇ -galactosidase produced by the H-404 strain (deposit number: FERMP—11062) (WO 02 / 186 14), and correspondingly, the non-reducing disaccharide of the formula (1) or (2) can be produced in high yield.
  • Saccharomyces cerevisiae Ne S accharomycescervis ⁇ ae
  • Nono Tenoresu bacteria belonging to the genus Bacillus' Megateri ⁇ beam B acillusmegaterium
  • the solid culture medium may be wheat bran alone or wheat bran with various additives such as kinako, soybean flour, ammonium salt, nitrate, urea, glutamic acid, aspartic acid, polypeptone, corn steep liquor, meat.
  • Organic and inorganic nitrogen compounds such as extracts, yeast extracts, and protein hydrolysates can be appropriately added and used.
  • suitable inorganic salts can be added.
  • the microorganisms grow well and produce enzymes smoothly.
  • a carbon source starch or a carbohydrate such as a fraction thereof, roasted dextrin, processed starch, starch derivative, physically treated starch and a substance containing -starch or galactose can be used.
  • Specific examples include soluble starch, corn starch, potato starch, sweet potato starch, dextrin, amylopectin, amylose, galataose, lactose, raffinose, and the like. Can be used in combination of two or more.
  • Nitrogen sources include polypeptone, casein, meat extract, yeast extract, corn steep liquor or organic nitrogen source substances such as soybean or soybean meal extracts, ammonium sulfate, ammonium phosphate, etc.
  • Amino acids such as inorganic nitrogen compounds and glutamic acid can be used, and these can be used alone or in combination of two or more.
  • the inorganic salts include phosphates such as potassium phosphate and potassium phosphate, magnesium salts such as magnesium sulfate, calcium salts such as calcium chloride, and sodium salts such as sodium carbonate. Used alone or in combination of two or more.
  • the culture is carried out by stationary culture, and the culture is adjusted to pH 3 to 7, preferably 4 to 7, and the bacterial strain is inoculated into the culture. Incubate at 20-37 ° C for 1-10 days. After the cultivation, 1-galactosidase can be obtained from the culture extract as a crude enzyme precipitate by means such as ethanol precipitation.
  • the culture is performed under aerobic conditions such as shaking culture or aeration-agitation culture, and the medium is adjusted to a pH range of 4 to 10, preferably pH 5 to 8, and the temperature is adjusted.
  • the cells are cultured at a temperature in the range of 10 to 40 ° C, preferably 25 to 37 ° C, for 24 to 96 hours.
  • the cells can be removed by centrifugation or other appropriate solid-liquid separation means to obtain a culture supernatant.
  • the fungus The body can be treated physically or enzymatically to obtain a bacterial extract. Then, high-purity monogalactosidase can be obtained from these crude enzyme solutions by appropriately combining ammonium sulfate salting out, gel filtration, hydrophobic chromatography and the like.
  • the enzymes used for the production of oligosaccharides containing a galactosyl group include, in addition to the enzyme preparations obtained as described above, extracts in the case of solid culture, and extracts in the case of liquid culture. Alternatively, a culture supernatant or an intracellular extract can be used as it is as an enzyme preparation. If necessary, an enzyme purified by a known method can also be used. It is also possible to use the cells as they are as an enzyme preparation. Alternatively, ⁇ -galactosidase mixed with a commercially available enzyme preparation, for example, a cellulase preparation ⁇ protease preparation, can be used. In this case, the enzyme preparation can be used as it is, or a single galactosidase can be prepared from the enzyme preparation by various known methods. It can be used after purification.
  • these enzymes or cells that produce the enzymes can be immobilized and used in a continuous or batch-wise manner in the reaction.
  • the raw material used for the reaction of ⁇ -galactosidase to produce the non-reducing disaccharide of the formula (1) is galactose or a substance containing galactose.
  • specific examples include galactose and hydrolysates of galactose and other compounds containing galactose such as lactose. These can be used alone or in combination.
  • galactose there are not only commercial galatose, but also meribiose, mannino triose, raffinose, stachy, plante, benorenoscose, galactan, galactomannan, arabinogalactan, rhamnogalatatan, ⁇ -galactosyl group or ⁇ -galactol such as galactolipid, ferulated galactose, galactovitol, galactosylglycerol, galactinol, lactose, ratatitol, lactulose, galactoligosaccharide, etc. Natural or synthetic oligosaccharides, glycosides or polysaccharides containing sil groups
  • galactosidase ⁇ -galactosidase, ⁇ -galactosidase, monogalactosidase, etc.
  • galactose prepared from hydrolyzate with acid can be used.
  • hydrolyzate of a compound containing galactose examples include meribiose, mannino triose, raffinose, stachyose, planteose, verbascourse, galactan, galactomannan, arabinogalactan, rhamnogalactan, galactolipid, ferula oxidation.
  • ⁇ -galactose such as galactose, galactopinitol, galata tosyl glycerol, galactinol, lactose, ratatitol, lactulose, galata tori saccharide and the like; natural or synthetic oligos containing a 3-galact tosyl group; Those obtained by hydrolyzing sugars, glycosides or polysaccharides with enzymes (eg, 3-galactanase, ⁇ -galactosidase, ⁇ -galactosidase) or acids can be used as they are.
  • enzymes eg, 3-galactanase, ⁇ -galactosidase, ⁇ -galactosidase
  • Raw materials used for the reaction of ⁇ -galactosidase to produce the non-reducing disaccharide of the formula (2) include substances containing galactose and glucose. Specifically, a mixture of galactose and glucose is suitably used. Examples thereof include a mixture containing lactose and glucose, and a compound containing galactose and glucose at an appropriate ratio. Lactose hydrolyzate obtained by hydrolyzing inexpensive lactose with -galactosidase or an acid is preferably used as it is. The ratio of galactose to dulcose is not particularly limited.
  • Glucose that binds to galactose is not only commercially available glucose, but also starch, malto-oligosaccharide, isomaltoligo-sugar, nigerooligo-sugar, koji-oligosaccharide, cyclodextrin, trehalose, maltitol, cellulose, cellooligo-sugar , Or sophoro-oligo-sugar, laminario-oligo-sugar, gentio-oligosaccharide, etc.
  • Hydrolysis of natural or synthetic oligosaccharides, glycosides or fertility including enzymes, such as amylase, gnorecoamylase, cellulase, a-dalcosidase, ⁇ -g / recosidase, or acids Gnorecose prepared from the product can be used.
  • enzymes such as amylase, gnorecoamylase, cellulase, a-dalcosidase, ⁇ -g / recosidase, or acids Gnorecose prepared from the product can be used.
  • ⁇ -Galactosidase is essentially a hydrolase, but if the concentration of galactose in the substrate is increased, it will also catalyze the reverse dehydration reaction of the hydrolysis reaction. Therefore, when a single galactosidase is allowed to act on a high concentration of galactose, it has the following structural formula: ⁇ — (G a)) n (n is usually an integer of 2 to 10 and G a1 is galactose) It produces an oligosaccharide containing an ⁇ -galactosyl group in a composition in which a large number of oligosaccharides such as disaccharide, trisaccharide, and tetrasaccharide are mixed.
  • G al a l of non-reducing disaccharide of the formula of the present invention (1) -: L 0 G a Ui can manufacture by performing decomposition and separation of reducing sugars oligosaccharide obtained above.
  • the decomposition of the reducing sugar in the oligosaccharide can be carried out by alkali decomposition, for example, by adding an alkali such as sodium hydroxide or potassium hydroxide to the oligosaccharide.
  • Galal — 1 Oligosaccharides other than i3Gal are degraded.
  • the addition amount of alkali is preferably from 0.1 to 6. ON final concentration.
  • the separation operation can be performed using a known separation means such as ion exchange chromatography, reverse phase chromatography, activated carbon column chromatography, and gel filtration column chromatography, but activated carbon mouth chromatography is preferred. .
  • Galal-lj3Glc of the non-reducing disaccharide represented by the formula (2) of the present invention Hydrolyzes the mixed Galal-lj3Gal, and further decomposes and separates the reducing sugar in the ⁇ - (Gal) n-G1c oligosaccharide obtained above. It can be manufactured by performing.
  • the hydrolysis of 110 Gal can be performed using an enzyme, and the enzyme is preferably -galactosidase.
  • the amount of galactosidase to be added is appropriately determined in consideration of the conditions such as the origin and activity of the enzyme, which are appropriate for each enzyme.
  • Decomposition of reducing sugars in oligosaccharides can be carried out by alkali decomposition, for example, by adding alkaline water such as sodium hydroxide or hydroxylic power to oligosaccharides. By this decomposition operation, oligosaccharides other than Galal-1 / 3G1c are decomposed.
  • the added amount of the alkali is preferably 0.1 to 6. ON final concentration.
  • the separation operation can be performed using a known separation means such as ion exchange chromatography, reverse phase chromatography, activated carbon column chromatography, and gel filtration column chromatography, but activated carbon mouth chromatography is preferred.
  • the oligosaccharide containing an ⁇ -galactosyl group synthesized by the dehydration condensation reaction is again subjected to monogalactosidase.
  • the glycosyltransferase is also decomposed and the transglycosylation reaction occurs in parallel, so the transglycosylation also contributes to the synthesis of oligosaccharides containing a single galactosyl group.
  • the galactose bond position and the number of bonds of the produced compound, or the ratio of these compounds are affected by the composition of the raw material galactose and glucose, the origin of the enzyme used and the reaction conditions.
  • reaction conditions for ⁇ -galactosidase vary depending on the enzyme used, but the reaction ⁇ is in the range of 3.0 to 10.0, preferably 4.0 to 9.0.
  • the reaction temperature is desirably high in terms of solubility and reaction rate, and is usually in the range of 20 to 90 ° (preferably 40 to 80 ° C.). It usually varies from 1 to 150 hours, depending on the amount used.
  • the present invention is not limited to the above conditions or only the reaction mode.
  • the galactose-glucose precipitates in the reaction system, and the galactose-glucose is supersaturated. It may be in a state, and is usually used at a concentration of 5 to 110% (w / v), and preferably at a concentration of 50 to 110% (w / V).
  • FIG. 1 is a diagram showing a calibration curve when the molecular weight of ⁇ _galactosidase obtained by a production example in the best mode for carrying out the invention described below is measured by HPLC.
  • FIG. 2 is a view showing the results of measuring, by SDS-PAGE, the molecular weight of ⁇ _galactosidase obtained in a production example in the best mode for carrying out the invention described below.
  • FIG. 3 is a diagram showing a change over time of a dehydration condensation reaction using galactose as a raw material in the best mode for carrying out the invention described below.
  • BEST MODE FOR CARRYING OUT THE INVENTION
  • Reference Example 1 (Paranitrophyl 0; a method for measuring ⁇ -galactosidase activity using galactoside as a substrate)
  • One unit (U) of the enzymatic activity was defined as the amount of the enzyme that liberated 1 micole of paraditrophenol per minute under these conditions.
  • Reference Example 2 Measured activity of Hi-galactosidase using melibiose as substrate
  • the bran koji was crushed finely, 8 L of water was added thereto, and the mixture was extracted overnight at 4 ° C, and then filtered with a filter paper to obtain an extract filtrate.
  • the ⁇ -galactosidase activity of the obtained extract filtrate was measured, it was 3 units (U) per 1 ml of the extract filtrate.
  • 1 L of 6 L of extraction filtrate is filtered with an ultrafiltration membrane (SIP made by Asahi Kasei Corporation) Then, ammonium sulfate was added to achieve 70% saturation, and salting out was performed.
  • the precipitate was collected by centrifugation, dissolved in 500 ml of water, concentrated to 100 ml with an ultrafiltration membrane, and further added with 500 ml of water to 100 ml. After concentration, this operation was repeated three times to perform desalting. After desalting, freeze-drying was performed to obtain a freeze-dried powder (250 UZg).
  • Ammonium sulfate was added to the extract filtrate obtained above so as to be 70% saturated and stirred, and then left at 4 ° C. for a while.
  • the precipitate was collected by centrifugation, dissolved in 10 mM phosphate buffer (pH 6.0), concentrated with an ultrafiltration membrane (SIP manufactured by Asahi Kasei Corporation), and the buffer was reconstituted again. It was added and concentrated. This operation was repeated three times for desalting.
  • the a-galactosidase obtained above has the following physicochemical properties. 1 Action
  • G a1 a 1 OR represents a carbohydrate containing a single galactosyl group
  • G a 1 ⁇ H represents free galactose
  • R—OH represents various sugars, alcohols and Compounds having a hydroxyl group such as fuynols are shown.
  • meliviose acts on meliviose, raffinose, stachyose, etc., which have a single galactosyl group at the non-reducing end, and on paranitrophenyl ⁇ -galactoside. Assuming that the decomposition rate of para-trophenyl hyalgalactoside as a substrate is 100, the relative rate of decomposition of meliviose is about 9.
  • the optimal ⁇ ⁇ is 2.5 to 6.0.
  • the pH is stable in the range of 3.5 to 8.0.
  • the optimum temperature at pH 4.5 (acetate buffer) is 60 ° C. It is stable up to 60 ° C when left at pH 4.5 (acetate buffer) for 15 minutes.
  • the molecular weight measured by a gel filtration method using a YMC-Pack Dio 1 — 200 column is 2,170,000, and the molecular weight measured by SDS-PAGE is 1 17 , 00 0 (FIGS. 1 and 2).
  • the isoelectric point measured by isoelectric focusing is 4.2.
  • This enzyme can be used for a-galactosita produced by Aspergillus niger (A spergi 11 usniger), which has been reported so far, and for 72,000 and 69,000 (all SDS -It is characterized by a higher molecular weight compared to (PAGE).
  • Galactose manufactured by Wako Pure Chemical Industries, Ltd. 60 g and acetate buffer solution with a pH of 4.5 containing 2,100 U M of the galactosidase obtained in the production example 10 Om l (galactose concentration 6 0% (w / v) , enzyme concentration 3 5 U M - Gala click toast) was prepared and 3 0 hours reaction at 5 0 ° C.
  • Figure 3 shows the time course of the reaction.
  • the reaction solution was loaded on an activated carbon column, and oligosaccharide was eluted with water at a concentration gradient of galactose and ethyl alcohol of 0 to 30%.
  • the oligosaccharide-eluted fraction was concentrated and dried to obtain 24 g of an oligosaccharide containing an ⁇ -galactosyl group.
  • this oligosaccharide was hydrolyzed with monogalactosidase or acid, only galactose was formed.
  • ⁇ _galactosidases Candida gilli enolemon tea (C andidagui 11 iermondii) H-404 strain, which is known to have the highest catalytic activity of the dehydration condensation reaction, is used.
  • the yield was 14 g, a production example, and the yield of Hi-galactosidase obtained in this example was excellent.
  • Lactose (produced by Wako Pure Chemical Industries, Ltd.) 100 g is commercially available j3-galactosidase (Lactozym manufactured by Novozym Co., Ltd.) to obtain an equal mixture of galactose and glucose.
  • the oligosaccharide obtained above contains a mixture of Galal-l ⁇ Gal
  • 20 g of this oligo was added to 100 ml of 20 mM phosphate buffer to facilitate purification.
  • the solution was dissolved in a liquid (pH 6.5), and added with 45,000 LAU (unit of lactase from Novozym Co., Ltd.)], followed by addition of 3-galactosidase (Lactozym from Novozym Co., Ltd.). Further, 20 mM phosphate buffer (pH 6.5) was added to the solution so that the solution volume became S180 ml. This solution was treated at 40 ° C.
  • novel non-reducing disaccharides represented by the formulas (1) and (2) of the present invention may cause amino acids and proteins to be damaged by the Maillard reaction caused by the reaction between the amino compound and the reducing sugar. Since it is not available, it is expected as a food material that has little adverse effect on other materials in food processing and storage, and as a pharmaceutical material.
  • the novel method for producing a non-reducing disaccharide of the present invention is a method for producing a non-reducing disaccharide, which is derived from Aspergillus niger APC-9319 strain (FE RM BP-7680).
  • FE RM BP-7680 Aspergillus niger APC-9319 strain

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Abstract

L'invention concerne de nouveaux disaccharides non réduits Galα1-1βGal et Galα1-1βGlc contenant α-galactosyl, utilisés dans des produits alimentaires ou médicaux qui n'endommagent pas les acides aminés ou les protéines lorsqu'on les ajoutent à des aliments ou à des conserves. L'invention concerne également un procédé permettant de produire le disaccharide non réduit Galα1-1βGal, qui consiste à traiter un galactose ou un matériau contenant un galactose avec α-galactosidase, à décomposer des sucres de réduction contenus dans les oligosaccharides contenant α-galactosyl afin d'obtenir des sucres réduits, puis à les séparer. L'invention concerne enfin un procédé permettant de produire le disaccharide non réduit Galα1-1βGlc, qui consiste utiliser d'abord un matériau contenant un galactose et un glucose, à hydrolyser Galα1-1βGlc contenu dans les oligosaccharides contenant α-galactosyl obtenus de la même manière que décrit ci-dessus, à décomposer les sucres réduits et à les séparer.
PCT/JP2002/012215 2001-11-26 2002-11-22 Nouveaux disaccharides non reduits contenant $g(a)-galactosyl et leur procede de production WO2003046194A1 (fr)

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Citations (3)

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WO1994023022A1 (fr) * 1993-03-31 1994-10-13 Novo Nordisk A/S Alpha-galactosidase
EP0841397A2 (fr) * 1996-11-08 1998-05-13 Kabushiki Kaisha Hayashibara Seibutsu Kagaku Kenkyujo Trehalose phosphorylase, la préparation et l'utilisation
WO2002018614A1 (fr) * 2000-08-30 2002-03-07 Amano Enzyme Inc. Methode visant a augmenter le rendement d'oligosaccharides contenant $g(a)-galactosyle et compositions anti-candida

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* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO1994023022A1 (fr) * 1993-03-31 1994-10-13 Novo Nordisk A/S Alpha-galactosidase
EP0841397A2 (fr) * 1996-11-08 1998-05-13 Kabushiki Kaisha Hayashibara Seibutsu Kagaku Kenkyujo Trehalose phosphorylase, la préparation et l'utilisation
WO2002018614A1 (fr) * 2000-08-30 2002-03-07 Amano Enzyme Inc. Methode visant a augmenter le rendement d'oligosaccharides contenant $g(a)-galactosyle et compositions anti-candida

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Title
HASHIMOTO H. ET AL.: "Enzymatic synthesis of alpha-linked galactooligosaccharides using the reverse reaction of a cell-bound alpha-galactosidase from candida guilliermondii H-404", BIOSCI. BIOTECH. BIOCHEM., vol. 59, no. 2, 1995, pages 179 - 183, XP002965228 *
MINAMI Y. ET AL.: "Selectivity and efficiency of galactosyl-oligosaccharides by bifidobacteria", CHEM. PHARM. BULL., vol. 33, no. 2, 1985, pages 710 - 714, XP000617604 *
RONNOW T.E.C.L. ET AL.: "The use of O-glycosyl trichloroacetimidates in the synthesis of unsymmetrical trehalose analogues", TETRAHEDRON: ASYMMETRY, vol. 5, no. 11, 1994, pages 2109 - 2122, XP005068184 *

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