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WO1992007947A1 - Melange a base d'oligosaccharide et procede de traitement ulterieur du melange - Google Patents

Melange a base d'oligosaccharide et procede de traitement ulterieur du melange Download PDF

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Publication number
WO1992007947A1
WO1992007947A1 PCT/FI1991/000240 FI9100240W WO9207947A1 WO 1992007947 A1 WO1992007947 A1 WO 1992007947A1 FI 9100240 W FI9100240 W FI 9100240W WO 9207947 A1 WO9207947 A1 WO 9207947A1
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WO
WIPO (PCT)
Prior art keywords
mixture
oligosaccharide mixture
glucoamylase
glucose
yeast
Prior art date
Application number
PCT/FI1991/000240
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English (en)
Inventor
Marianne Rossi
Yu-Yen Linko
Pekka Linko
Timo Vaara
Marja Turunen
Original Assignee
Oy Alko Ab
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
Filing date
Publication date
Application filed by Oy Alko Ab filed Critical Oy Alko Ab
Publication of WO1992007947A1 publication Critical patent/WO1992007947A1/fr

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Classifications

    • 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
    • C12P19/16—Preparation of compounds containing saccharide radicals produced by the action of an alpha-1, 6-glucosidase, e.g. amylose, debranched amylopectin
    • 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
    • C12P19/18—Preparation of compounds containing saccharide radicals produced by the action of a glycosyl transferase, e.g. alpha-, beta- or gamma-cyclodextrins

Definitions

  • the present invention concerns a procedure for after-treatment of an oligosaccharide mixture according to the patent application FI 904124, and a mixture obtained by means of said procedure.
  • glucoamylase for hydrolyzing starch, whereby starch breaks up to glu- cose.
  • Commercial glucoamylase preparations are mostly composed of several different amylases (in: Starch, Chemistry and Technology (1984), Eds. R.L. Whistler, J.N. BeMiller and E.F. Paschall, Academic Press Inc., London, England) .
  • glucoamylase is produced by moulds of genus Aspergillus, such as Aspergillus niger, Aspergil- lus awamori, and by some moulds of genus Rhizopus and Endomyces.
  • gluco ⁇ amylase and/or commercial yeast has been used in con- nection with producing neotrehalose and 2'- ⁇ -glucosyl- maltose, for removal of the hydrolysis products formed of starch, and free glucose.
  • the procedure constituting the object of the present invention in the after-treatment is used, differing from the procedures cited above, either solu ⁇ ble or immobilized glucoamylase and/or yeast. Since, moreover, the oligosaccharide mixture after-treatment method of patent application FI 904124, with glucoamy ⁇ lase and/or yeast, has not been heretofore described, the procedure of the invention is a completely novel after-treatment method.
  • glucoamylase is made to act on an oligosaccharide mixture as specified in patent application FI 904124, whereby the long-chain oligosaccharides are broken up to shorter units, and glucose is set free in the solu- tion.
  • the free glucose is eliminated with baking yeast from an oligosaccharide mixture according to patent application FI 904124 or from a glucoamylase-treated mixture. Proceeding in this manner, one obtains a novel oligosaccharide mixture which is lower in calories and less cariogenic.
  • the object of the invention is a procedure for after-treatment of an oligosaccharide mixture according to patent application FI 904124, and a mixture obtained by this procedure.
  • glucoamylase is made to act on an oligo ⁇ saccharide mixture according to patent application FI 904124, whereby the long-chain oligosaccharides, particularly those with DP (glucose polymerizing grade) higher than 5, are broken down to shorter units and glucose is set free in the solution.
  • the glucoamylase- treated oligosaccharide mixture contains in the first place oligosaccharides with DP between 3 and 5 (OSG3- OSG5).
  • the free glucose is eliminated with baking yeast from the oligosaccharide mixture according to patent application FI 904124 or from the glucoamylase-treated mixture, whereby an oligosaccharide mixture lower in calories and less cariogenic than the untreated oligo- saccharide mixture is obtained.
  • oligosaccharides with DP 3 to 5 can be used e.g. in the foodstuff industry as new raw materials because oligosaccharides with DP 3 to 5 are broken up very slowly, or not at all, by ⁇ amylase (e.g. in: Starch, Chemistry and Tech ⁇ nology (1984), Eds. R.L. Whistler, J.N. BeMiller and E.F. Paschall, Academic Press Inc., London, England).
  • the after-treatment may also be carried out with immobilized glucoamylase and/or yeast.
  • immobilized glucoamylase and/or yeast it is possible to achieve a continu ⁇ ous after-treatment procedure, by which 30 to 60% of the cost can be saved, compared with conventional tech- nique.
  • the product is obtained in rather pure condition, which even further lowers the after- treatment cost and, on the other hand, makes possible new applications of the product.
  • the fundamental idea of the invention consists of the fact that glucoamylase has been found to break up ⁇ -(l-4) and ⁇ -(1-6)-glycosidic bonds in starch, producing glucose from starch.
  • the oligosaccharide mixture of the patent application FI 904124 is starch- based, and the long glucose chains containing acceptor sugar (trehalose or cellobiose) can be broken up with glucoamylase to shorter units, the broken-up glucose chains decomposing further to glucose.
  • acceptor sugar trehalose or cellobiose
  • the oligosaccharide mixture of patent applica ⁇ tion FI 904124 will decompose to glucose and acceptor sugar.
  • the glucose that has been set free in the oli ⁇ gosaccharide mixture can be removed with baking yeast, which is known to use glucose in its metabolism.
  • the product thus obtained consists of acceptor sugar and an oligosaccharide mixture containing, among others, oli ⁇ gosaccharides with DP 3-5.
  • composition of the product mixtures was determined by liquid chromatography.
  • the method enabled the concentrations of oligosaccharides under DP 8 to be determined in that the concentration of any given oligosaccharide was calculated in accordance with the concentration of the reference standard (with DP 1 to 7) having the closest retention time. Confirmation of the results was made qualitatively with TLC.
  • Glucoamylase preparations of various origins can be used in the invention, such as commercial prepa ⁇ rations, for instance.
  • yeast e.g. Saccharomyces cerevisiae baking yeast may be used.
  • the concentration of the oligosaccharide mix- ture reacting with glucoamylase may be in the range from 5 to 60%.
  • the concentration may be high when solu ⁇ ble glucoamylase is used, while in the case of immobi ⁇ lized glucoamylase the favourable concentration range is 5 to 30%.
  • For glucose elimination either free or immobilized yeast cells may be used, and the concentra ⁇ tion of the oligosaccharide mixture may then be in the range of 5 to 60%.
  • the advantageous concentration range is 5 to 30%.
  • the favourable pH range of the oligosac ⁇ charide mixture to be after-treated is 5.5 to 7.5.
  • the reactions may be effected with glucoamylase at 10 to 70°C, advantageous temperature is 30 to 50°C.
  • advantageous temperature is 30 to 50°C.
  • yeast the temperature range may be 10 to 60°C, advan ⁇ tageous temperature is 30 to 45°C.
  • the reaction time is 24 hrs at the most, advantageous reac- tion time is 10 min. to 8 hrs, depending on the concen ⁇ tration of the glucoamylase or yeast used.
  • the longer the reaction time with glucoamylase the more of the OSG3-OSG5 oligosaccharides will the solution contain, compared with the untreated mixture.
  • the solution con ⁇ tains the greatest amount of 0SG3 oligosaccharide, next of OSG4 oligosaccharide, and so on, until at the turn- ing point of the reaction the contents, first of OSG5 saccharide, then of OSG4 decrease as the chains are broken up. Ultimately the concentration of OSG3 oligo ⁇ saccharide also begins to decline. The greater the quantity of oligosaccharides that are broken up the more glucose and acceptor sugar will the solution con ⁇ tain.
  • After-treatment with immobilized glucoamylase and/or yeast can be carried out either in batches or as a continuous column reaction. It is advisable, prior to continuous reaction, to filter the oligosaccharide mixture in order to remove any insoluble and unhydro- lyzable starch. Baking yeast immobilized in alginate binds to itself some of the oligosaccharide contents in the mixture being after-treated, for which reason the continuous system should be allowed to stabilize until the yeast beads are saturated with the oligosaccharide mixture. Using a long retention time in the column and low immobilized yeast concentration will result in favourable conditions for the after-treatment.
  • the oligosaccharide syrup may further be after-treated according to procedures known in the art, such as decolouring with active carbon and desalting with ion exchangers, whereafter the oligosaccharide syrup may be either cold-dried, powdered or concentrat ⁇ ed in vacuum.
  • Ethanol e.g. 70%
  • oligosaccharide mix ⁇ tures according to patent application FI 904124 can be modified in controlled manner, whereby mixtures are obtained in which the proportion of oligosaccharides with DP 3 to 5 has been advantageously altered.
  • this after-treatment it is possible with this after-treatment to achieve oligosaccharide mixtures lower in calories and less cariogenic than the untreated mixtures.
  • the yeast cells were bonded to sodium alginate in the form of beads (Linko, Y-Y., Weckstr ⁇ m, L. and Linko, P. (1980), Food Process Engineering, Vol. 2, p. 81-91).
  • Baking yeast, 16.0 g wet weight, (Oy Alko Ab, Rajamaki) was suspended in 10 ml distilled water and added to 50 g 8% sodium alginate (BDH, Poole, England) .
  • the mixture was extruded with the aid of nitrogen gas to beads of 0.6 mm diameter through needles into 0.5 M calcium chloride solution, in which the beads were left to mix for 60 min.
  • the beads were then washed with dis ⁇ tilled water, and the excess of water was removed.
  • the activity of the immobilized yeast was de ⁇ termined using for substrate, 2% glucose solution (in 50 mM imidazole buffer, pH 6.8). 1.0 g of the immobi ⁇ lized yeast were added to 5 g substrate and the reac ⁇ tion was allowed to proceed at 40°C for 30 min. The concentration of residual glucose was determined at room temperature by liquid chromatography (Zsadon, B., Otta, K.H., Tudos, F. and Szejtli, J. (1979), J. Chrom- atogr., 172. 490-492).
  • the elution rate in carbohydrate column was 0.9 ml/min, and the concentrations of the standards (with DP 1-7, including glucose, maltose, ..., maltoheptaose, cellobiose, trehalose) were 1-5 mg/1.
  • One unit of activity of the immobilized yeast beads is equivalent to 1 ⁇ mol glucose per min. used up under the above reaction conditions.
  • the activity of the immobilized yeast was found to be 7 U/g and the activity of free yeast cells under equivalent condi- tions of reaction, 33.3 U/g.
  • the activity yield of the immobilized yeast was found to be 100%.
  • the glucoamylase (Spezyme, Suomen Sokeri Oy, activity 340 GU/ml) was immobilized on Duolite ES 762 resin (Duolite International, Vitry, France) .
  • Duolite ES 762 resin Duolite International, Vitry, France
  • 50 mM imidazole buffer pH 6.8
  • 50 mM imidazole buffer pH 6.8
  • 50 mM imidazole buffer pH 6.8
  • the en ⁇ zyme solution was filtered off and 2.5% glutaric alde ⁇ hyde was added 2 ml per g resin for cross-linking. Shaking was continued for another 3 hrs at room temper ⁇ ature, whereafter the resin was washed with distilled water and filtered to moist constitution.
  • the activity of the immobilized glucoamylase was determined using for substrate, 2% starch solution (soluble starch in 50 mM imidazole buffer, pH 6.8).Im ⁇ mobilized glucoamylase was added 0.5 g to a solution containing 4.5 g substrate and 0.5 ml distilled water.
  • the concentration of the glucose thus formed was deter- mined by liquid chromatography (see Example 1).
  • the activity of the soluble glucoamylase was determined by adding suitably diluted enzyme 0.5 ml to 4.5 g sub ⁇ strate under equivalent conditions of reaction as above.
  • the unit of activity (U) of immobilized gluco ⁇ amylase corresponds to 1 ⁇ mol glucose produced in one minute under the above reaction conditions.
  • the activ ⁇ ity of the immobilized glucoamylase was found to be 3.6 U/g and that of the soluble enzyme, 378 U/ml.
  • the grade of activity of the immobilized glucoamylase was found to be 4.3%.
  • Oligosaccharide mixtures according to patent application FI 904124 were after-treated with either soluble or immobilized glucoamylase preparation accord ⁇ ing to Example 2.
  • soluble glucoamylase To the oligosaccharide mixture, of which the composition is presented in Table 1 (treha ⁇ lose oligosaccharides, dry matter content of the mix- ture 50%), was added soluble glucoamylase, either 1.1 U per g of mixture (Test 1) or 3.3 U per g of mixture (Test 2).
  • Immobilized glucoamylase was added 0.11 U per g of mixture (Test 3).
  • the batch reactions were allowed to proceed at 40°C under shaking for 3 hrs (Test 1), 5 hrs (Test 2) and 1.75 hrs (Test 3).
  • the compositions of the products were determined by liquid chromatography (see Example 1), and they are given in Table 1.
  • a cellobiose oligosaccharide mixture was simi ⁇ larly after-treated, its composition being presented in Table 2 (dry matter content 30%).
  • Soluble glucoamylase was added 0.67 U per g of mixture (Test 4) and immobi ⁇ lized glucoamylase, 0.22 U per g of mixture (Test 5).
  • the batch reactions were allowed to proceed at 40°C under shaking for 3 hrs (Test 4) and 5 hrs (Test 5).
  • the compositions of the products were determined by liquid chromatography (see Example 1), and they are given in Table 2.
  • the concentration of OSG3-OSG5 oligosacchar ⁇ ides could be increased by the glucoamylase treatment in all tests.
  • the untreated oligosaccharide mixture presented in Table 1 had OSG3-OSG5 concentration 21.5 g/100 g, while the OSG3-OSG5 concentrations after glucoamylase treatment were 22.0-26.3 g/100 g.
  • Espe ⁇ cially in Test 2 the concentration of OSG3 oligosaccha- ride increased 85%, compared with the untreated mix ⁇ ture.
  • the untreated oligosaccharide mixture presented in Table 2 had OSG3-OSG5 concentration 11.2 g/100 g, while the OSG3-OSG5 concentrations after glucoamylase treatment were 12.3-14.3 g/100 g.
  • oligosaccharide mixture as in Test 1 pre- sented in Example 3 was after-treated with free yeast cells as in Example 1, in a batch reaction, and an oligosaccharide mixture as in Example 3, with immobi ⁇ lized yeast cells as in Example 1, in a continuous re ⁇ action.
  • the aim was to reduce the glucose concentration in the mixture.
  • the oligosaccharide mixture of Test 3 was after-treated with immobilized yeast in a continuous column reaction at 40°C. Prior to glucose removal, the oligosaccharide mixture of Test 3 was diluted 1:10 with water, and filtered, whereafter the dry matter content of the solution was 5%. 20 g immobilized yeast (activ ⁇ ity 7 U/g) were added into the column (1.8 cm diameter and 14 cm height) , and the flow rate in the column was 0.8 ml/min. Collection of eluate was commenced upon stabilization of the column reaction. The composition of the eluate was determined by liquid chromatography (see Example 1) and is presented in Table 3.
  • Fig. 1 displays the liquid chromatographic elution chromatogram of the oligosac ⁇ charide mixture of Test 3, after immobilized yeast treatment.

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  • Organic Chemistry (AREA)
  • Chemical & Material Sciences (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Engineering & Computer Science (AREA)
  • Zoology (AREA)
  • Wood Science & Technology (AREA)
  • Health & Medical Sciences (AREA)
  • Chemical Kinetics & Catalysis (AREA)
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  • Bioinformatics & Cheminformatics (AREA)
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  • General Health & Medical Sciences (AREA)
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  • Preparation Of Compounds By Using Micro-Organisms (AREA)
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Abstract

Procédé de traitement ultérieur d'un mélange à base d'oligosaccaride, selon lequel de la glucoamylase et/ou de la levure est amenée à agir sur un mélange à base d'oligosaccharide obtenu lorsque l'on fait agir de la cyclomatodextrine-glucanotransférase (CGTase, E.C. 2.4.1.19) sur de l'amidon en présence d'un sucre accepteur. Selon ce procédé, un nouveau mélange à base d'oligosaccharide, à teneur réduite en calories et moins cariogène que précédemment, est obtenu.
PCT/FI1991/000240 1990-11-01 1991-08-08 Melange a base d'oligosaccharide et procede de traitement ulterieur du melange WO1992007947A1 (fr)

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
FI905402A FI905402A7 (fi) 1990-11-01 1990-11-01 Oligosakkaridiseos ja menetelmä sen jälkikäsittelyksi
FI905402 1990-11-01

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Cited By (7)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
EP0691407A1 (fr) * 1994-06-27 1996-01-10 Kabushiki Kaisha Hayashibara Seibutsu Kagaku Kenkyujo Saccharide non réductant, sa production et son utilisation
US5576303A (en) * 1993-03-16 1996-11-19 Kabushiki Kaisha Hayashibara Seibutsu Kagaku Kenkyujo Energy-supplementing saccharide source and its uses
US5578584A (en) * 1993-03-24 1996-11-26 Matsutani Chemical Industry Co., Ltd. Feed containing galacto-oligosaccharides for domestic fowls
WO2007059955A3 (fr) * 2005-11-23 2007-09-27 Pro Natura Ges Fuer Gesunde Er Agent permettant de réduire la teneur en calories utilisable d'aliments et destiné à la réduction thérapeutique du poids, à utiliser notammentdans le cas d'adiposité (obésité)
US8231924B2 (en) 2004-08-20 2012-07-31 Cargill, Incorporated Ingredient systems comprising trehalose, food products containing trehalose, and methods of making same
US8231925B2 (en) 2004-08-20 2012-07-31 Cargill, Incorporated Ingredient systems comprising trehalose, food products containing trehalose, and methods of making same
US10568942B2 (en) 2005-11-16 2020-02-25 Pro Natura Gesellschaft für gesunde Ernährung mbH Agent for use in the case of fructose intolerance

Citations (5)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US4477568A (en) * 1981-09-24 1984-10-16 Proefstation voor Aardappelverweking-TNO en Cooperatieve Verkoop en Produktievereniging van Aardappelmeel en Derivaten AVERE B.A. Process for the manufacture of cyclodextrin
EP0164933A2 (fr) * 1984-06-05 1985-12-18 Cpc International Inc. Procédé de transformation enzymatique
GB2165549A (en) * 1984-10-12 1986-04-16 Agricult Forestry & Fishers Branched cyclodextrins
EP0252525A2 (fr) * 1986-07-11 1988-01-13 Wako Pure Chemical Industries Ltd Dosage de l'alpha amylase utilisant des oligosaccharides modifiées et leur procédé de production
WO1989007148A1 (fr) * 1988-01-29 1989-08-10 Bioeurope Procede de preparation enzymatique d'oligodextranes utiles dans la fabrication de substituts du sucre, et nouveaux oligodextranes

Patent Citations (5)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US4477568A (en) * 1981-09-24 1984-10-16 Proefstation voor Aardappelverweking-TNO en Cooperatieve Verkoop en Produktievereniging van Aardappelmeel en Derivaten AVERE B.A. Process for the manufacture of cyclodextrin
EP0164933A2 (fr) * 1984-06-05 1985-12-18 Cpc International Inc. Procédé de transformation enzymatique
GB2165549A (en) * 1984-10-12 1986-04-16 Agricult Forestry & Fishers Branched cyclodextrins
EP0252525A2 (fr) * 1986-07-11 1988-01-13 Wako Pure Chemical Industries Ltd Dosage de l'alpha amylase utilisant des oligosaccharides modifiées et leur procédé de production
WO1989007148A1 (fr) * 1988-01-29 1989-08-10 Bioeurope Procede de preparation enzymatique d'oligodextranes utiles dans la fabrication de substituts du sucre, et nouveaux oligodextranes

Non-Patent Citations (3)

* Cited by examiner, † Cited by third party
Title
CHEMICAL ABSTRACTS, Volume 109, No. 3, 18 July 1988, (Columbus, Ohio, US), see page 655, abstract 23312m; & JP,A,63 017 895 (Preparation of new gluco-oligosaccharide derivatives and their use for determining alfa-amylase activity), 25 January 1988. *
CHEMICAL ABSTRACTS, Volume 114, No. 15, 15 April 1991, (Columbus, Ohio, US), see abstract 141647a; & JP,A,2 255 095 (Effective production of gamma-cyclodextrin and/or alfa-glucosylglycyrrhizin with cyclodextrin glucanotransferase), 15 October 1990. *
DIALOG INFORMATION SERVICES, file 351, WPI, 81-91, Dialog Acc. No. 007662427, ((NORQ) NORINSHO), "Neotrehalose and centose prepn. - by treating starch substrate with cyclodextrin - synthetase"; GLUCOSYL MALTOSE; & JP,A,63 216 492, 08-09-1988, 8842. *

Cited By (8)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US5576303A (en) * 1993-03-16 1996-11-19 Kabushiki Kaisha Hayashibara Seibutsu Kagaku Kenkyujo Energy-supplementing saccharide source and its uses
US5578584A (en) * 1993-03-24 1996-11-26 Matsutani Chemical Industry Co., Ltd. Feed containing galacto-oligosaccharides for domestic fowls
US5919668A (en) * 1994-06-02 1999-07-06 Kabushiki Kaisha Hayashibara Seibutsu Kagaku Kenkyujo Non-reducing saccharide and its production and use
EP0691407A1 (fr) * 1994-06-27 1996-01-10 Kabushiki Kaisha Hayashibara Seibutsu Kagaku Kenkyujo Saccharide non réductant, sa production et son utilisation
US8231924B2 (en) 2004-08-20 2012-07-31 Cargill, Incorporated Ingredient systems comprising trehalose, food products containing trehalose, and methods of making same
US8231925B2 (en) 2004-08-20 2012-07-31 Cargill, Incorporated Ingredient systems comprising trehalose, food products containing trehalose, and methods of making same
US10568942B2 (en) 2005-11-16 2020-02-25 Pro Natura Gesellschaft für gesunde Ernährung mbH Agent for use in the case of fructose intolerance
WO2007059955A3 (fr) * 2005-11-23 2007-09-27 Pro Natura Ges Fuer Gesunde Er Agent permettant de réduire la teneur en calories utilisable d'aliments et destiné à la réduction thérapeutique du poids, à utiliser notammentdans le cas d'adiposité (obésité)

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FI905402A0 (fi) 1990-11-01
AU8319491A (en) 1992-05-26
FI905402L (fi) 1992-05-02
FI905402A7 (fi) 1992-05-02

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