WO1997002341A1 - β-GLUCOSIDASE DE CHAMPIGNONS FILAMENTEUX, ET SES UTILISATIONS - Google Patents
β-GLUCOSIDASE DE CHAMPIGNONS FILAMENTEUX, ET SES UTILISATIONS Download PDFInfo
- Publication number
- WO1997002341A1 WO1997002341A1 PCT/FR1996/001054 FR9601054W WO9702341A1 WO 1997002341 A1 WO1997002341 A1 WO 1997002341A1 FR 9601054 W FR9601054 W FR 9601054W WO 9702341 A1 WO9702341 A1 WO 9702341A1
- Authority
- WO
- WIPO (PCT)
- Prior art keywords
- glucosidase
- bgii
- hydrolysis
- glucose
- activity
- Prior art date
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Classifications
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- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
- A23L2/00—Non-alcoholic beverages; Dry compositions or concentrates therefor; Their preparation
- A23L2/70—Clarifying or fining of non-alcoholic beverages; Removing unwanted matter
- A23L2/84—Clarifying or fining of non-alcoholic beverages; Removing unwanted matter using microorganisms or biological material, e.g. enzymes
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- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N1/00—Microorganisms, e.g. protozoa; Compositions thereof; Processes of propagating, maintaining or preserving microorganisms or compositions thereof; Processes of preparing or isolating a composition containing a microorganism; Culture media therefor
- C12N1/14—Fungi; Culture media therefor
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- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
- C12N9/2402—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
- C12N9/2405—Glucanases
- C12N9/2434—Glucanases acting on beta-1,4-glucosidic bonds
- C12N9/2445—Beta-glucosidase (3.2.1.21)
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- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P19/00—Preparation of compounds containing saccharide radicals
- C12P19/14—Preparation of compounds containing saccharide radicals produced by the action of a carbohydrase (EC 3.2.x), e.g. by alpha-amylase, e.g. by cellulase, hemicellulase
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- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P19/00—Preparation of compounds containing saccharide radicals
- C12P19/44—Preparation of O-glycosides, e.g. glucosides
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y302/00—Hydrolases acting on glycosyl compounds, i.e. glycosylases (3.2)
- C12Y302/01—Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds (3.2.1)
- C12Y302/01021—Beta-glucosidase (3.2.1.21)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y302/00—Hydrolases acting on glycosyl compounds, i.e. glycosylases (3.2)
- C12Y302/01—Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds (3.2.1)
- C12Y302/0104—Alpha-L-rhamnosidase (3.2.1.40)
Definitions
- the present invention relates to a ⁇ -glucosidase of fungal origin, the activity of which is weakly inhibited in the presence of high glucose contents, as well as to the process for obtaining it, and to its uses.
- ⁇ -D-glucosides glucohydrolases (EC 3.2.1.21) commonly called ⁇ -glucosidases catalyze the hydrolysis of alkyl- and aryl- ⁇ -D-glucosides, as well as that of cellobiose.
- ⁇ -glucosidases catalyze the hydrolysis of alkyl- and aryl- ⁇ -D-glucosides, as well as that of cellobiose.
- the use of these enzymes has been proposed in various fields.
- glycosidic precursors constitute an important part of the aromatic potential in fruits, because the proportion of aroma linked to sugars is often higher than the proportion of corresponding free aroma [GUNATA et al., J. Chromatogr. 331, 83-90, (1985); KRAMMER et al., J. Agric. Food Chem. 39, 778-781, (1991)].
- a ⁇ -D-glucopyranosidase then intervenes to release the aglycone from the monoglucosides formed.
- the hydrolysis is carried out directly without going through the first step.
- ⁇ -glucosidases have also been proposed in other fields, such as for example the hydrolysis of toxic cyanogenic glucosides contained in certain plants such as cassava, the synthesis of alkyl glucosides used in the pharmaceutical and food industries such as non-ionic biological detergents and surfactants. it has also been proposed to use ⁇ -glucosidases for the recycling of cellulose.
- Cellulose is present in the cell wall of plant tissues, either in free form, or in the form of lignocellulose or hemicellulose; it represents a very significant part of the waste from industries that use raw materials of plant origin.
- a first stage consists of saccharification, that is to say the production of glucose, which is metabolizable by industrial micro-organisms which allows in the second stage the bioconversion of glucose into an energy source, such as ethanol, or into protein biomass intended for animal feed.
- an energy source such as ethanol
- the enzymatic saccharification processes are preferred over chemical processes • However, for the process to be profitable, the efficiency of conversion of cellulose to glucose should be high. However, during saccharification, the accumulation in the medium of cellobiose, disaccharide formed under the action of cellulases (exo- and endo-i, 4- ⁇ -D-glucanases) from cellulose, inhibits these latter enzymes .
- the hydrolysis of cellobiose by a ⁇ -glucosidase as it is formed prevents its accumulation in the medium, and makes it possible to increase the rate of saccharification.
- Trichoderma reesei is the most used for the production of cellulases.
- the production of ⁇ -glucosidase by this fungus being however very low, its enzymatic complex is supplemented by a ⁇ -glucosidase of fungal origin [WOODWARD and WISEMAN, Enzyme Microbiol. Technol. , 4, 73-79, (1982); WILHEM and SHAM, Acta Biotechnol, 6, 2, 115-121, (1986)].
- a ⁇ -glucosidase of fungal origin [WOODWARD and WISEMAN, Enzyme Microbiol. Technol. , 4, 73-79, (1982); WILHEM and SHAM, Acta Biotechnol, 6, 2, 115-121, (1986)].
- the inhibition of ⁇ -glucosidase by its reaction product, glucose considerably reduces the efficiency of the process.
- the present invention relates to a purified preparation of ⁇ -glucosidase of fungal origin, hereinafter called Bj3I_I, characterized in that it is an exocellular ⁇ -glucosidase, capable of being obtained from fungi filamentous, whose molecular mass estimated by exclusion chromatography is approximately 30,000, the isoelectric point determined by electrofocusing is approximately 4.2, the optimum pH is between 4.5 and 6.0, the constant d
- the inhibition (Ki) for glucose is approximately 950 mM, and which retains all of its activity after 24 hours of incubation at pH 3.0 and at 20 ° C.
- the ⁇ -glucosidase BGII obtained in accordance with the invention is also less inhibited than other ⁇ -glucosidases by ⁇ -gluconolactone.
- the ⁇ -glucosidase BGII is capable of being obtained from a filamentous fungus chosen from the group consisting of A. niger and A. oryzae. These filamentous fungi are GRAS (Generally Recommended As Safe). Depending on the medium on which they are cultivated, these fungi produce a greater or lesser amount of ⁇ -glucosidase BGII.
- the inventors have for example found that the use of a medium comprising quercetin as a carbon source was particularly advantageous with the aim of increasing the yield of ⁇ -glucosidase BGII.
- BGII ⁇ -glucosidase is stable over a wide range of pH and temperature, and can therefore be used in a wide variety of media. It has a broad spectrum of activity and allows the hydrolysis of ⁇ -D-glucosides of different nature. In addition, it is exocellular, which facilitates its production.
- ⁇ -glucosidase BGII can be envisaged in all cases where one wishes to carry out the hydrolysis of ⁇ -D-glucosides in media containing glucose, such as for example:
- alkyl glucosides which can be used in particular as detergents.
- ⁇ -glucosidase BGII can be used in the form of a purified preparation, or else in the form of a culture medium containing said enzyme; this medium can be used in the raw state, or after any appropriate treatment having the effect of increasing its BGII content.
- EXAMPLE 1 PRODUCTION OF ⁇ -GLUCOSIDASE: The fungi A. niger 55465 and A. oryzae 12559 come from the collection of the Centraalbureau Voor Schimmel Cultures (CBS, Netherlands). The second strain of A. niger used comes from the laboratory collection. The mushrooms are stored on a "Potatoes Dextrose Agar" medium.
- the basic medium for the production of the enzyme contains the following compounds (% W / V): (NH 4 ) 2 HP0 4 : 0.3; (NH 4 ) 2 S0 4 : 0.8; KH 2 P0 4 : 0.1;
- the media containing the carbon sources to be tested (rutin, quercetin, cellobiose) are sterilized (120 ° C, 25 minutes) separately, then mixed with the base medium at a final concentration of 0.3% (P / V).
- the cultures, after sowing with the chosen fungus, are carried out at 30 ° C., with stirring (120 revolutions / minute). At different times of culture, samples are taken in order to monitor the production of the enzyme.
- the culture medium removed and first centrifuged (5000 g, 10 minutes, 5 ° C). The supernatant obtained, after dialysis, is used for the determination of the ⁇ -glucosidase activity.
- the determination of the ⁇ -glucosidase activity is carried out by incubation for 20 minutes at 40 ° C., of I volume of the enzymatic sample with 1 volume of p-nitrophenol ⁇ -D-glucoside (PNPG) (4 mM in 100 mM acetate buffer, pH 4.4).
- PNPG p-nitrophenol ⁇ -D-glucoside
- the amount of PNP (p-nitrophenol) released is estimated by adding 6 volumes of 0.1 M Na 2 C03, and followed by reading the absorbance at 400 nm.
- the enzymatic activity is expressed in nanokatals per ml (nkat / ml) of enzymatic solution.
- a nanokatal corresponds to the number of nanomoles of PNP released per second under the aforementioned conditions.
- BGII is produced by the three strains, the A. oryzae strain, however, having a higher yield.
- the culture medium (3 liters), obtained after A. oryzae on quercetin, then concentrated, has successively undergone two purification steps: exclusion chromatography and ion exchange chromatography.
- the culture medium (3 liters), harvested after culture of A. oryzae on quercetin, is first concentrated on an AMICON® cell (cutoff threshold 10 000). It is then loaded onto a column (1.6 x 90 cm) filled with ULTROGEL® AcA44 (IBF), and previously balanced with a 100 mM phosphate-citrate buffer, pH 7.0, at 4 ° C. The elution is carried out with the same buffer at a flow rate of 7 ml / hour. The assay for ⁇ -glucosidase activity is carried out and the proteins are estimated at 280 nm on the fractions collected. The fractions corresponding to the second peak of ⁇ -glucosidase (BGII) activity are grouped together.
- BGII was eluted at an NaCl concentration of 0.17 M, followed by BGI which was eluted at 0.21 M NaCl ( Figure 2)
- Proteins of known molecular mass are successively injected into the ULTROGEL® AcA44 column in order to calibrate the column: cytochrome C (12,500), chymotrypsin (25,000), ovalbumin (45,000), serum ovalbumin (68,000), lipoxygenase (100 000).
- the dead volume of the column is determined by the injection of a solution of Blue Dextran.
- the molecular mass of BGII. estimated by exclusion chromatography and using proteins from known molecular weights, is around 30,000
- BGI is excluded from the gel fractionation domain used, which indicates that it must have a molecular mass greater than 130,000. It should be noted that the molecular mass of most of the known fungal ⁇ -glucosidases is often greater than 80,000. Fairly low molecular weights, namely 48,000 for C. guilliermondii ⁇ -glucosidase and 41,000 for that of A. fumigatus have however been reported [WOODWARD and WISEMAN, Enzyme Microbiol. Technol., 4, 73-79. (1982)].
- the enzymatic solution is incubated for 20 minutes at 40 ° C. in a range of 10Q mM phosphate-citrate buffer of pH varying from 2.5 to 8, in the presence of PNPG.
- the enzymatic activity is assayed according to the protocol described above.
- the enzyme has an optimum pH of between 4.5 and 6.0 ( Figure 4), close to the values of known fungal ⁇ -glucosidases [GUNATA et al. , Progress in Flavor Precursor Studies; SCHREIER, P., WINTERHALTER, P., Eds, Allured: Wheaton (USA), 219-234, (1993)].
- the enzyme like the ⁇ -glucosidases of known fungal origin, retains approximately 10% of its maximum activity at pH 3.0.
- the pHi of BGII was determined by isoelectric focusing on agarose gel (gel thickness, 1 mM; 1% agarose, 12% sorbitol, pharmalyte 2.5-5.0).
- the device used is the “LKB 2117 Multiphor II Electrophoresis Unit”. After electrofocusing (1920 volts applied), the BGII was located on the gel using the substrate 4-methylumbelliferyl- ⁇ -D-glucoside.
- the pHi of the enzyme was estimated at 4.2 by comparing its migration with that of pHi markers.
- the activity measurements, using the PNPG as a substrate, are carried out as described above.
- glycosidases of filamentous fungi are distinguished by a very good stability at the acid pH of grape must (about 3.0), while those of S. cerevisiae, C. wickerhamii and grapes quickly lose their activity at this pH [GUNATA et al. , Progress in Flavor Precursor Studies; SCHREIER, P., WINTERHALTER, P., Eds, Allured: Wheaton (USA), 219-234, (1993); DELCROIX et al., Am. J. Enol. Vitic, 45, 3, p. 291-296, (1994)].
- the BGII preparation resulting from ion exchange chromatography can be maintained for 24 hours at 20 ° C., in a 100 mM phosphate-citrate buffer at each of pH 3.0, 6.0 and 7.0, in remaining stable and without any loss of activity.
- the reaction medium containing an enzymatic solution to be tested (BGI, BGII. Or ⁇ -glucosidase from A. niger purified from the enzyme preparation KLERZYME® (GIST-BROCADES, SECLIN, FRANCE), which hydrolyzes terpenic glycosides during vinification of dry wine [GUNATA et al., J. Inter. Sci. Vigne Vin, 24, 3, p. 133-143, (1990)] and which is used here for comparison) and a solution of PNPG to 4 mM is supplemented with a glucose solution or gluconolactone in different concentrations.
- the residual enzymatic activity is estimated after incubation of the mixture for 20 minutes at 40 ° C.
- the inhibition constant for glucose of the BGI, BGII and ⁇ -glucosidase activity of KLERZYME®, and the type of inhibition, are determined by the Lineweaver-Burk representation. RESULTS - Inhibition by glucose At the end of the exclusion chromatography,
- the BGI like practically all ⁇ -glucosidases of filamentous fungi [WOODWARD and
- the values of inhibition by gluco ⁇ e of BGII are of the same order as those obtained after the exclusion chromatography.
- the inhibition constants (Ki) for glucose from BGI activities. of BGII, and of ⁇ -glucosidase from KLERZYME® were respectively calculated with respect to PNPG according to the representation of LINEWEAVER BURK. Glucose behaves in all three cases like a competitive inhibitor.
- the inhibition constants are 3.2, 3.5, 953 mM respectively for the ⁇ -glucosidases of KLERZYME®, of BGI, and of BGII.
- Ki value as high as that obtained for BGII has never been reported.
- Significantly lower values were found respectively in ⁇ -glucosidase from grapes, sweet almonds and Candida wickerhamii, 170, 210, 230 mM [GUNATA et al., (1993) cited above].
- Gluconolactone produced from glucose by the action of glucose oxidase from fungi developed on grape berries, is known as an even more potent inhibitor than glucose, of the activity ⁇ -glucosidase [GUNATA et al., Progress in Flavor Precursor Studies, SCHREIR, P., WINTERHALTER, P., Eds, Allured: Wheaton (USA), 219-234, (1993)].
- the concentration of gluconolactone can reach up to 2 g / l in grape must obtained from the harvest attacked by fungi, such as Botrytis cinerea.
- the activity of the BGII enzyme vis-à-vis cellobiose, naringine, and ⁇ -D-glucosides of geraniol, nerol, linalol, benzyl alcohol, phenylethyl alcohol is studied in a buffered medium (acetate buffer , 100 mM, pH 4.4) incubated at 40 ° C. The final concentration of each substrate is 2 mM in the reaction medium.
- the sample is injected directly onto the column without prior treatment.
- the detection is made at 200 nm.
- BGII catalyzes the hydrolysis of the different substrates that have been tested, namely aryl- (PNPG), and alkyl glucosides (geraniol ⁇ -D-glucosides, nerol, linalol, benzyl alcohol, phenylethyl alcohol), and a diglucoside (cellobiose), and therefore behaves like the ⁇ -glucosidases of filamentous fungi [WOODWARD and WISEMAN , Microbiol enzyme. Technol., 4 p. 73-79, (1982)].
- a neutral must (white UGNI, pH 2.9, 90 g / l glucose), poor in terpene monoglucosides, but previously enriched in linalol ⁇ -D-glucosides, nerol , geraniol (0.15 mM each) was added either with BGII (0.6 nkat / ml) or with ⁇ -glucosidase from KLERZYME® (0.6 nkat / ml). The content of monoglucosides added to the must exceeds 10 times the contents encountered in the musts of the grape varieties richest in these compounds.
- the media were analyzed by HPLC after a week of incubation at 20 ° C. Under these conditions, the ⁇ -glucosidase from KLERZYME® had no effect on the substrates, while under the action of BGII, approximately 50% of the glycosides of nerol and geraniol and 90% of the linalol glucoside had disappeared. .
- naringin-7-rhamnoglucoside The hydrolysis of naringin (naringenin-7-rhamnoglucoside) was also studied by thin layer chromatography. It is known that complete hydrolysis of naringin requires the successive action of an ⁇ -rhamnosidase and a ⁇ -glucosidase. As expected, BGII alone therefore had no action on naringin.
- the reaction medium was then added with an ⁇ -rhamnosidase isolated from an enzymatic preparation (GUNATA et al. 1988), which cut the interosidic bond, and released the naringenin monoglucoside. This monoglucoside was then completely hydrolyzed by BGII.
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Abstract
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Priority Applications (4)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
AU65222/96A AU709427B2 (en) | 1995-07-06 | 1996-07-05 | Beta-glucosidase from filamentous fungi, and uses thereof |
NZ313210A NZ313210A (en) | 1995-07-06 | 1996-07-05 | Beta-glucosidase from filamentous fungi, and uses thereof |
EP96924944A EP0871717A1 (fr) | 1995-07-06 | 1996-07-05 | beta-GLUCOSIDASE DE CHAMPIGNONS FILAMENTEUX, ET SES UTILISATIONS |
US08/973,867 US6087131A (en) | 1995-07-06 | 1996-07-05 | β-glucosidase from filamentous fungi, and uses thereof |
Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
FR95/08185 | 1995-07-06 | ||
FR9508185A FR2736359B1 (fr) | 1995-07-06 | 1995-07-06 | Beta-glucosidase de champignons filamenteaux, et ses utilisations |
Publications (1)
Publication Number | Publication Date |
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WO1997002341A1 true WO1997002341A1 (fr) | 1997-01-23 |
Family
ID=9480750
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
PCT/FR1996/001054 WO1997002341A1 (fr) | 1995-07-06 | 1996-07-05 | β-GLUCOSIDASE DE CHAMPIGNONS FILAMENTEUX, ET SES UTILISATIONS |
Country Status (6)
Country | Link |
---|---|
US (1) | US6087131A (fr) |
EP (1) | EP0871717A1 (fr) |
AU (1) | AU709427B2 (fr) |
FR (1) | FR2736359B1 (fr) |
NZ (1) | NZ313210A (fr) |
WO (1) | WO1997002341A1 (fr) |
Cited By (3)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
FR2777908A1 (fr) * | 1998-04-24 | 1999-10-29 | Agronomique Inst Nat Rech | Clonage et expression du gene de la beta-glucosidase d'origine fongique bgii |
WO2002095014A2 (fr) * | 2001-05-18 | 2002-11-28 | Novozymes A/S | Polypeptides presentant une activite de cellobiase et polynucleotides codant pour de tels polypeptides |
CN102604916A (zh) * | 2002-09-10 | 2012-07-25 | 金克克国际有限公司 | 使用高浓度糖混合物诱导基因表达 |
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Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
BRPI0412279A (pt) * | 2003-07-02 | 2006-09-19 | Diversa Corp | glucanases, ácidos nucléicos codificando as mesmas e métodos para preparar e aplicar os mesmos |
EP1682656B1 (fr) * | 2003-10-28 | 2013-09-18 | Novozymes Inc. | Polypeptides presentant une activite beta-glucosidase et polynucleotides codant pour ceux-ci |
CA2861310A1 (fr) * | 2005-03-15 | 2006-09-28 | Bp Corporation North America Inc. | Cellulases, acides nucleiques codant pour ces cellulases, et procedes de production et d'utilisation de ces cellulases |
DK2444487T3 (en) | 2006-02-10 | 2018-05-28 | Bp Corp North America Inc | CELLULOLYTIC ENZYMES, NUCLEIC ACIDS, CODING THEM, AND PROCEDURES FOR THEIR PREPARATION AND USE |
AU2007356171B8 (en) * | 2006-08-04 | 2014-01-16 | Bp Corporation North America Inc. | Glucanases, nucleic acids encoding them, and methods for making and using them |
CN101652381B (zh) | 2007-01-30 | 2014-04-09 | 维莱尼姆公司 | 用于处理木质纤维素的酶、编码它们的核酸及其制备和应用方法 |
MX2011002142A (es) * | 2008-08-29 | 2011-04-26 | Iogen Energy Corp | Beta-glucosidasas modificadas con estabilidad mejorada. |
US8486683B2 (en) * | 2009-05-29 | 2013-07-16 | Iogen Energy Corporation | Beta-glucosidase enzymes |
CN110205351A (zh) * | 2019-05-23 | 2019-09-06 | 广东金骏康生物技术有限公司 | 一种糖基化柚皮素的制备方法及其应用 |
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1995
- 1995-07-06 FR FR9508185A patent/FR2736359B1/fr not_active Expired - Fee Related
-
1996
- 1996-07-05 US US08/973,867 patent/US6087131A/en not_active Expired - Fee Related
- 1996-07-05 WO PCT/FR1996/001054 patent/WO1997002341A1/fr not_active Application Discontinuation
- 1996-07-05 NZ NZ313210A patent/NZ313210A/en unknown
- 1996-07-05 AU AU65222/96A patent/AU709427B2/en not_active Ceased
- 1996-07-05 EP EP96924944A patent/EP0871717A1/fr not_active Withdrawn
Non-Patent Citations (7)
Title |
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A. DELCROIX ET AL: "glucosidase activities of three enological yeast strains during winemaking: effect on the terpenol content of muscat wine", AM. J. ENOL. VITIC., vol. 45, no. 3, 1994, pages 291 - 296, XP002000250 * |
CHEMICAL ABSTRACTS, vol. 122, no. 19, 8 May 1995, Columbus, Ohio, US; abstract no. 234051g, WANG QIN ET AL: "Catalytic properties of beta-glucosidase from Aspergillus niger" page 469; column r; XP002000253 * |
J. WOODWARD ET AL: "Fungal and other beta-D-glucosidases_their properties and applications", ENZYME MICROB. TECHNOL., vol. 4, March 1982 (1982-03-01), pages 73 - 79, XP002000252 * |
R.F.H. DEKKER ET AL: "Kinetic, inhibition, and stability properties of a commercial beta-D-Glucosidase (cellobiase) preparation from Aspergillus niger and its suitability in the hydrolysis of lignocellulose", BIOTECHNOLOGY AND BIOENGINEERING, vol. 28, 1986, NEW YORK US, pages 1438 - 1442, XP002000249 * |
TIANRAN CHANWU YANJIU YU KAIFA, vol. 6, no. 4, 1994, pages 36 - 39 * |
Z. GUNATA ET AL: "Action des glucodidases exogènes au cours de la vinification : libération de l'arome à partir de précurseurs glycosidiques", JOURNAL INTERNATIONAL DES SCIENCES DE LA VIGNE ET DU VIN, vol. 24, no. 3, 1990, pages 133 - 144, XP002000251 * |
Z. GUNATA ET AL: "Role of enzymes in the use of the flavour potential from grape glycosides in wine making", PROGRESS IN FLAVOUR PRECURSOR STUDIES. PROCEEDINGS OF THE INTERNATIONAL CONFERENCE MEETING. EDITED BY SCHREIER, PETER; WINTERHALER, PETER. PUBLISHED BY : ALLURED PUBLISHING CORPORATION, CAROL STREAM USA, 1993, 30 September 1992 (1992-09-30) - 2 October 1992 (1992-10-02), WÜRZBURG, GERMANY, pages 219 - 234, XP002019692 * |
Cited By (5)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
FR2777908A1 (fr) * | 1998-04-24 | 1999-10-29 | Agronomique Inst Nat Rech | Clonage et expression du gene de la beta-glucosidase d'origine fongique bgii |
WO1999055884A1 (fr) * | 1998-04-24 | 1999-11-04 | Institut National De La Recherche Agronomique | CLONAGE ET EXPRESSION DU GENE DE LA β-GLUCOSIDASE D'ASPERGILLUS ORYZAE BGII |
WO2002095014A2 (fr) * | 2001-05-18 | 2002-11-28 | Novozymes A/S | Polypeptides presentant une activite de cellobiase et polynucleotides codant pour de tels polypeptides |
WO2002095014A3 (fr) * | 2001-05-18 | 2003-12-24 | Novozymes As | Polypeptides presentant une activite de cellobiase et polynucleotides codant pour de tels polypeptides |
CN102604916A (zh) * | 2002-09-10 | 2012-07-25 | 金克克国际有限公司 | 使用高浓度糖混合物诱导基因表达 |
Also Published As
Publication number | Publication date |
---|---|
FR2736359B1 (fr) | 1997-10-03 |
FR2736359A1 (fr) | 1997-01-10 |
US6087131A (en) | 2000-07-11 |
EP0871717A1 (fr) | 1998-10-21 |
NZ313210A (en) | 1999-10-28 |
AU6522296A (en) | 1997-02-05 |
AU709427B2 (en) | 1999-08-26 |
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