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WO1992003565A1 - Melange d'oligosaccharides et procede de fabrication - Google Patents

Melange d'oligosaccharides et procede de fabrication Download PDF

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Publication number
WO1992003565A1
WO1992003565A1 PCT/FI1991/000239 FI9100239W WO9203565A1 WO 1992003565 A1 WO1992003565 A1 WO 1992003565A1 FI 9100239 W FI9100239 W FI 9100239W WO 9203565 A1 WO9203565 A1 WO 9203565A1
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WO
WIPO (PCT)
Prior art keywords
starch
cgtase
trehalose
acceptor
oligosaccharides
Prior art date
Application number
PCT/FI1991/000239
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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 WO1992003565A1 publication Critical patent/WO1992003565A1/fr

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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
    • C12P19/18—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 starch-based oligosaccharide mixture containing acceptor sugar, and a procedure for manufacturing same.
  • Oligosaccharides containing trehalose and cel ⁇ lobiose are linear molecules in which one or several glucose units are adjoined to acceptor sugar (trehalose or cellobiose) .
  • acceptor sugar trehalose or cellobiose
  • CGTase cyclomaltodextrin-glucanotransferase
  • Oligosaccharides can be applied as new raw materials in the foodstuff, animal feed and medical industry, and in chemical industry. To this purpose certain oligosaccharides have already been launched on the market, e.g. starch-based products such as maltose, maltotriose, maltotetraose, isomaltose, panose, etc. Furthermore, lactose-based oligosaccharides and sugar alcohols have been produced, such as maltitol, and sac ⁇ charose-based products, such as 'coupling sugar', fruc- tooligosaccharides, palatinose, etc., which have been reported in: Alternative sweeteners (1986), edited by L.O. Nabors and R.C.
  • oligosaccharides are often low in calories, their sweetness is milder than that of saccharose, and they are either less cariogenic than saccharose or not cari- ogenic at all. In addition to these properties, oligo ⁇ saccharides have also good technical characteristics and positive effects both physiologically and in view of health.
  • fructooligo- saccharides A procedure for manufacturing fructooligo- saccharides has been disclosed e.g. in the British Patent No. 2,179,946, in which fructosyltransferase is made to act on saccharose. Palatinose, or isomaltulose, is produced from saccharose with glucosyltransferase, lactose-based oligosaccharides such as 6-galactosyl lactose are produced from lactose with ⁇ -galactosidase.
  • K. Ajisaka and H. Fujimoto (1989) Ameri ⁇ can Society Meeting, Sept. 10-15, Miami Beach, a proce- dure for manufacturing trisaccharide containing treha ⁇ lose, from glucose and trehalose with R. niveus gluco- amylase, has been disclosed.
  • Patent No. 2,019,406 in both of which the enzyme is made to act on starch or dextrin in the presence of either saccharose or fructose, whereby as product are formed oligosaccharides of 'coupling sugar* type.
  • J. Biochem., 79 ./ 641-648 J. Biochem., 79 ./ 641-648, is disclosed the manufacturing from dextrin or starch, with CGTase, of oligosaccharides containing xylose and sorbose. Determination of the acceptor specificity of CGTase from various acceptor sugars and from cyclodex- trin is described in scientific magazines (D.
  • starch is used for substrate and cellobiose and/or trehalose for acceptor. No such production method has been described heretofore.
  • a novel, unique oligosaccharide mixture which is usable as a new raw material e.g. in the foodstuff and animal feed indus ⁇ tries.
  • the object of the invention is an oligosaccha ⁇ ride mixture containing trehalose and cellobiose as acceptor sugar, and a procedure for manufacturing same.
  • cyclomaltodextrin-glucanotransferase (CGTase; E.C. 2.4.1.19) is made to act on starch in the presence of acceptor sugar (trehalose or cellobiose), whereby oligosaccharides are formed which in their sugar composition contain trehalose and cellobiose.
  • the basic idea of the invention consists in that CGTase has been found to produce oligosaccharides from a suitable acceptor sugar and starch, in suitable conditions. It is possible in the procedure of the in ⁇ vention, by varying the conditions of reaction, to achieve oligosaccharide mixtures of novel type in which the oligosaccharides have DP numbers starting with 3 and up to 7 at least.
  • the reaction model of the proce ⁇ dure for producing an oligosaccharide mixture, on which the invention reads, can be assumed to be as follows. when cellobiose ( ⁇ -glu-(l-4)- ⁇ -glu) or trehalose ( ⁇ - glu-(l-l)- ⁇ -glu) is used for acceptor.
  • acceptor trehalose or cellobiose (di- saccharide)
  • the trehalose-containing oligosaccharide 0SG3 has the fol ⁇ lowing structure: 0- ⁇ -D-glu-(l-4)-0- ⁇ -D-glu-(l-l)- ⁇ -D- glu, that is, a glucoside molecule is attached to tre ⁇ halose with an ⁇ -(l-4)-glycosidic bond.
  • the oligosac ⁇ charides with DP higher than 3 are hard to analyse by nmr technique, owing to their complex structure. It has, however, been found in enzymatic structural analy- sis that the glucose molecule(s) are linked with the acceptor sugar in conformity with the above model.
  • Oligosaccharides according to the invention can be used e.g. in the foodstuff industry as new raw materials, because ⁇ -amylase breaks up very slowly, or not at all, oligosaccharides with DP between 3 and 5 (OSG3-OSG5) (e.g. in: Starch, Chemistry and Technology (1984) edited by R.L. Whistler, J.N. BeMiller and E.F. Paschall, Academic Press Inc., London, England, p. 93- 102) .
  • the oligosaccharide mixture obtained as product may furthermore contain the acceptor sugars trehalose or cellobiose, which are also used as single sugars for raw materials of the foodstuff industry.
  • the proportion in the product mixture of oligosaccharides having DP 3- 5 can be modified by means of dry matter and enzyme concentration, relative mass proportion of starch and acceptor sugar, and reaction time.
  • compositions of the product mixtures were determined by liquid chromatography.
  • the method enabled the concentrations of oligosaccharides with DP less than 8 to be determined in that the concentration of any given oligosaccharide was calculated in accordance with the concentration of whichever standard (DP from 1 to 7) had the most closely equal retention time. Con ⁇ firmation of the results was made qualitatively with TLC.
  • the CGTase required in the present invention is produced by cultivating a microorganism producing the respective enzyme, e.g. certain bacteria of genus Bacillus, in a culture solution containing a carbon and nitrogen source, minerals and vitamins (M. Makela, Bio- technical production of cyclodextrins (1990), Depart- ment of Biochemistry, University of Turku, Finland) .
  • the CGTase thereby formed is recovered using procedures of prior art, such as centrifuging the culture solu ⁇ tion, or filtering.
  • the crude enzyme saved in this manner may be purified and concentrated e.g. by salting out, gel filtration and/or by ion exchange chromatog ⁇ raphy or affinity chromatography.
  • starch materials of various origins can be used, e.g. those derived from cereals such as barley starch, or from root crops, such as potato starch.
  • the starch may also be pretreated e.g. by acid hydrolysis and/or enzymatically so that the dextrose equivalent of the liquefied starch thus formed is in the range from 0.5 to 20.
  • enzymatic hydroly ⁇ sis of starch one may use e.g. ⁇ -amylase or it is also possible to add the production enzyme, or CGTase, di ⁇ rectly to the starch, in which case pretreatment is unnecessary.
  • the advantageous DE number of the starch is about 1.
  • the total concentration of starch reacting with CGTase and acceptor sugar should be within 5-60%.
  • Advantageous concentration is 30-40% for production of cellobiose saccharides, and 40-50% for production of trehalose saccharides, whereby the relatively greatest amount of short-chain oligosaccharides will be formed in the mixture. Particularly in production of trehalose oligosaccharides the concentration should be high.
  • Sub- strate and acceptor may be dissolved either in water or in buffer, e.g. in 50 mM i idazole buffer pH 6.8, in 50 mM acetate buffer pH 5.5 or in 50 mM glycine-NaOH buffer pH 9.0.
  • Favourable pH range for the reaction is 6.5-7.0.
  • the reaction may be carried out at 50-80°C, with reaction time 2 days at the most.
  • Favourable tem ⁇ perature for the reaction is 60°C and reaction time, 20 to 48 hrs, depending on the CGTase concentration.
  • the relative mass proportion of starch and acceptor sugar should be within 0.5-4 in the solution.
  • Favourable pro- portion of starch and acceptor is 1:1, whereby OSG3- OSG5 oligosaccharides will be formed in the mixture most of all.
  • OSG3- OSG5 oligosaccharides When the starch quantity exceeds that of acceptor, long-chain oligosaccharides are formed most, in proportion.
  • short-chain oligosacchar ⁇ ides among others the OSG3 oligosaccharide, are formed relatively most.
  • the CGTase concentration in the reac ⁇ tion should be within 30-350 U per g of starch.
  • the favourable CGTase concentration is affected, among others, by concentration in that the higher the concen ⁇ tration of the solution the higher should the enzyme concentration be in the reaction. High enzyme concen ⁇ tration also shortens the reaction time.
  • Oligosaccharide-production enzyme or CGTase, (isolated from a Bacillus circulans strain, activity 7600 U/ml, Oy Alko Ab) was added 30 U/g to a mixture containing starch as stated in Table 1, in 50 mM imid- azole buffer pH 6.8, to which had been added 1.5 mM CaCl 2 .
  • the CGTase was allowed to act at 85°C for 30 min. with simultaneous agitation, whereafter in the starch (DE 1) was dissolved cellobiose (Sigma, U.S.A.) as stated in Table 1, and the solution was tempered to 60°C reaction temperature.
  • the reaction was started by adding to the so- lution 50 U CGTase per g of starch, and the reaction was allowed to proceed 48 hrs at 60°C, agitating at the same time.
  • the compositions of the products were deter ⁇ mined at room temperature by liquid chromatography (Zsadon B., Otta K.H., Tudos F. and Szejtli J. (1979), J. Chromatogr., 172, 490-492).
  • the elution rate in car ⁇ bohydrate column was 0.9 ml/min and the standards (e.g.
  • Example 1 (see Example 1) was added 30 U/g to a mixture contain ⁇ ing starch, as stated in Table 2, in buffer as in Example 1.
  • the CGTase was allowed to act for 30 min, at 85°C, with agitation, whereafter in the starch (DE 1) was dissolved ⁇ , ⁇ -trehalose (Sigma, U.S.A.) as stated in Table 2, and the solution was tempered to the reac ⁇ tion temperature, 60°C.
  • the reaction was started by adding CGTase 150 U per g of starch, and the reaction was allowed to proceed 48 hrs at 60°C under agitation.
  • the composi ⁇ tions of the products were determined by liquid chroma- tography (see Example 1) .
  • the concentrations of OSG3-OSG7 oligosaccha ⁇ rides in the products after 48 hrs reaction time are stated in Table 2.
  • CGTase (see Example 1) was added 30 U/g to a mixture containing starch in the mass proportion stated in Table 3, so that the ultimate concentration after acceptor addition in the solution would be 30 g/100 g.
  • the starch had been dissolved in imidazole buffer as in Example 1.
  • the CGTase was allowed to act for 30 min, at 85°C, with agitation, whereafter in the starch (DE 1) was dissolved either trehalose or cellobiose as stated in Table 3 (ultimate concentration 30 g/100 g) , and the solution was tempered to 60°C reaction temperature.
  • the reaction was started by adding CGTase 50 U per g of starch, and the reaction was allowed to pro- ceed 48 hrs at 60°C under agitation.
  • the compositions of the products were determined by liquid chromatogra ⁇ phy (see Example 1).
  • the concentrations of OSG3-OSG7 oligosaccha ⁇ rides in the products after 48 hrs reaction time are stated in Table 3.
  • the total quantities of oligosaccha ⁇ rides OSG3-OSG5 were, with the cellobiose saccharides, 13.1 g/100 g (mass proportion 1:4) and 14.4 g/100 g (1:2), and with trehalose saccharides 6.9 g/100 g in either case (mass proportions 1:2.3 and 1:1.2).
  • the proportion of the OSG3 oligosaccharide was highest when the acceptor concentration in the solution was high.
  • Trehalose oligosaccharides were produced in the manner described in Example 2, in the reaction being used 50 g starch (DE 1) and 50 g trehalose dis ⁇ solved in 200 g imidazole buffer (dry matter content 50%). The reaction was started by adding CGTase (see Example 1) 150 and 210 U per g of starch, and the reac- tion temperature was 60°C.
  • Fig. 2 the yield of oligosaccharides and the consumption of treha ⁇ lose (g/100 g) are plotted over time (48 hrs, CGTase concentration 210 U/g) .
  • the concentrations of OSG3-OSG5 oligosaccha ⁇ rides after 48 hrs reaction time are presented in Table 4.
  • the total of OSG3-OSG5 oligosaccharides in the pro ⁇ duct was measured to be 20.0 g/100 g (40.0% of the dry matter content, CGTase 150 U/g) and 22.7 g/100 g (45.4% of the dry matter content, CGTase 210 U/g).
  • Example 1 The production solution of Example 1, with 30% dry matter content, was diluted with water to 4.72% dry matter content and centrifuged, to remove the dry mat ⁇ ter. To the solution was added 135.5 U/ml ⁇ -amylase (isolated from a Bacillus subtilis strain, activity 1355 U/mg, Sigma, U.S.A.) and the reaction was allowed to proceed 24 hrs at 60°C, with agitation.
  • ⁇ -amylase isolated from a Bacillus subtilis strain, activity 1355 U/mg, Sigma, U.S.A.
  • the composi ⁇ tion of the product was determined by liquid chromatog- raphy (see Example 1), and measurement showed the total content of OSG3-OSG5 oligosaccharides in the product to be 14.2 g/100 g (OSG3: 7.3 OSG4: 4.2 g/100 g, OSG5: 2.7 g/100 g).
  • ⁇ -amylase broke off 16% oligosaccharide and 25% OSG5 oligosaccharide from the product of Example 1, while on the other hand the content of OSG3 oligosac ⁇ charide increased 22%.
  • Trehalose oligosaccharides were produced in the manner described in Example 2, in the reaction being used 15 g starch (DE 1) and 13.6 g trehalose dis- solved in 200 g imidazole buffer (dry matter content 28.6%).
  • the reaction was started by adding CGTase (see Example 1) 50 U per g of starch, and the reaction tem ⁇ perature was 60°C.
  • the reaction was allowed to proceed for 48 hrs, whereafter the composition of the product was determined by liquid chromatography (see Exam ⁇ ple 1).
  • OSG3- OSG5 oligosaccharides were 6.6 g/100 g (OSG3: 1.9 g/100 g, OSG4: 2.3 g/100 g, OSG5: 2.4 g/100 g, total 23.1% of the dry matter content).
  • the production solution was diluted with water to 6% dry matter content and centrifuged, to remove the dry matter.
  • the composition of the product was determined by liquid chromatography (see Example 1), and measurement showed the total quan ⁇ tity of OSG3-OSG5 oligosaccharides in the product to be 10.7 g/100 g (OSG3: 5.8 OSG4: 3.3 g/100 g, OSG5: 1.6 g/100 g) .
  • OSG3 5.8
  • OSG4 3.3 g/100 g
  • OSG5 1.6 g/100 g
  • ⁇ -amylase broke off 33% 0SG5 oligosaccharide from the product, while on the other hand the content of OSG3 oligosaccharide was tripled.
  • Trehalose oligosaccharides were produced in the manner described in Example 2, but the starch was first hydrolyzed with ⁇ -amylase (BAN 120 L, activity 120 KNU/g, Novo, Denmark). Amylase was added 0.3 and 0.9 KNU/g to a mixture containing 16 g starch in imid ⁇ azole buffer (see Example 2). The amylase was allowed to act 30 min. at 85°C, with stirring, whereafter in the starch (DE 5 and DE 16) was dissolved 16 g treha ⁇ lose (dry matter content of solution 32%) and the solu ⁇ tion was tempered to reaction temperature, 60°C.
  • ⁇ -amylase BAN 120 L, activity 120 KNU/g, Novo, Denmark.
  • the reaction was started by adding to the solution CGTase (see Example 1) 120 U per g of starch, and the reaction was allowed to proceed 48 hrs at 60°C, with stirring.
  • the composition of the products was de ⁇ termined by liquid chromatography (see Example 1) and by TLC on silicagel plates (running solution: acetone- 1-butanol-water 11:9:5; staining solution: aniline 2 ml, diphenylamine 2 g, acetone 100 ml, and 80% phos ⁇ phoric acid 15 ml; after plate staining, 30 min. heat ⁇ ing at 105°C) .
  • the total quantity of OSG3-OSG5 oligosaccha- rides in the product was found, in either case, to be 11.5 which was 35.9% of the dry matter content.
  • the product compositions were also analysed by TLC, which differentiates the produced oligosaccharides from the hydrolysis products formed in the pretreatment of the starch, such as maltose, maltotriose, maltotetraose, etc.
  • TLC the product solutions contained very small quantities of hydrolysis products formed in the pretreatmen ; their concentrations varied within 0.1 to 2.5 g/100 g, depending on the DE number of the solution.
  • the oligosaccharide contents of the product were found by measurement to be: OSG3: 4.4 g/100 g, 0SG4: 3.9 g/100 g, 0SG5: 3.2 g/100 g, and with starch having DE 16: 0SG3: 4.6 g/100 g, OSG4: 4.0 g/100 g, OSG5: 2.9 g/100 g.
  • CGTase (see Example 1) was added 30 U/g to a mixture containing 2 g starch in water or in 50 mM ace- tate, imidazole or glycine-NaOH buffer, to which had been added 1.5 mM CaCl 2 .
  • the buffers had pH 5.5, 6.8 and 9.0, respectively.
  • CGTase was allowed to act 30 min, at 85°C, with stirring, whereafter in the starch (DE 1) was dissolved 3 g trehalose (dry matter content of solution 40%) and the solution was tempered to reaction temperature 60°C.
  • CGTase was bonded with covalent bonds to Eupergit C beads (Rohm Pharma, Federal Republic of Germany) in that to 0.5 g of the beads (dry matter mass) was added 2 ml CGTase (isolated from Bacillus circulans strain, activity 265 U/ml, Oy Alko Ab) . The enzyme was left to be bonded for 20 hours at room tem ⁇ perature, shaking at the same time, whereafter the beads were washed with imidazole buffer according to Example 2.
  • soluble CGTase was added 30 U/g to a mixture containing 0.5 g starch and 4 g buffer as in Example 1.
  • the CGTase was allowed to act 30 min. at 85°C, with stirring, whereafter in the starch (DE 1) was dissolved 0.5 g trehalose (dry matter content of solution 20%), and the solution was tempered to reaction temperature 60°C.
  • the reaction was started by adding to the solution immobilized CGTase 0.5 g (dry matter mass, activity 424 U/g) , and the reaction was allowed to pro ⁇ ceed 21 hrs at 60°C, shaking at the same time.
  • the com- position of the product was determined by liquid chro ⁇ matography (see Example 2) . Measurements gave for the total OSG3-OSG5 oligosaccharide quantity in the pro ⁇ duct: 7.5 g/100 g (OSG3: 3.2 OSG4 2.4 g/100 g, and OSG5: 1.9 g/100 g) , which is 37.5% of the dry matter content.

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Abstract

Procédé de fabrication d'un mélange d'oligosaccharides, selon lequel de la cyclomaltodextrine-glucanotransférase (CGTase; E.C. 2.4.1.19) agit sur de l'amidon en présence d'un sucre accepteur (le tréhalose ou la cellobiose), de manière à produire des oligosaccharides contenant du tréhalose et de la cellobiose et présentant une composition unique de sucre.
PCT/FI1991/000239 1990-08-20 1991-08-08 Melange d'oligosaccharides et procede de fabrication WO1992003565A1 (fr)

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
FI904124A FI904124L (fi) 1990-08-20 1990-08-20 Oligosackaridblandning och foerfarande foer dess framstaellning.
FI904124 1990-08-20

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WO1992003565A1 true WO1992003565A1 (fr) 1992-03-05

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Cited By (16)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
EP0606753A3 (fr) * 1992-12-28 1995-06-14 Hayashibara Biochem Lab Enzyme de formation de saccharides non réductrices, et leur préparation et utilisations.
EP0690130A1 (fr) * 1994-06-27 1996-01-03 Kabushiki Kaisha Hayashibara Seibutsu Kagaku Kenkyujo Composition de saccharides avec réductibilité réduite, sa préparation et son utilisation
EP0691407A1 (fr) * 1994-06-27 1996-01-10 Kabushiki Kaisha Hayashibara Seibutsu Kagaku Kenkyujo Saccharide non réductant, sa production et son utilisation
US5538883A (en) * 1993-07-20 1996-07-23 Kabushiki Kaisha Hayashibara Seibutsu Kagaku Kenkyujo Maltose-trehalose converting enzyme
EP0636632A3 (fr) * 1993-06-28 1996-10-09 Hayashibara Biochem Lab Oligosaccharides non-réductrices, leur préparation et leur utilisation.
US5576303A (en) * 1993-03-16 1996-11-19 Kabushiki Kaisha Hayashibara Seibutsu Kagaku Kenkyujo Energy-supplementing saccharide source and its uses
EP0688867A3 (fr) * 1994-06-24 1996-12-18 Hayashibara Biochem Lab Enzyme thermostable de formation de saccharides non réducteurs, sa préparation et son utilisation
US5677442A (en) * 1992-12-28 1997-10-14 Kabushiki Kaisha Hayashibara Seibutsu Kagaku Kenkyujo Method of crystallizing trehalose without using organic solvent
US5747300A (en) * 1994-07-19 1998-05-05 Kabushiki Kaisha Hayashibara Seibutsu Kaguku Kenkyujo Trehalose and its production and use
US5908767A (en) * 1994-06-02 1999-06-01 Kabushiki Kaisha Hayashibara Seibutsu Kagaku Kenkyujo Non-reducing saccharide and its production and use
US5912330A (en) * 1994-03-01 1999-06-15 Kabushiki Kaisha Hayashibara Seibutsu Kagaku Kenkyujo Crystalline maltosyl glucoside, and its production and use
KR100401350B1 (ko) * 1995-02-10 2003-12-18 가부시끼가이샤 하야시바라 세이부쓰 가가꾸 겐꾸조 비환원성당질,그제조방법및용도
CN100347183C (zh) * 1993-09-30 2007-11-07 株式会社林原生物化学研究所 非还原性糖类生成酶及其制备和应用
EP2402454A1 (fr) 2010-06-30 2012-01-04 Süd-Chemie AG Production de cellobiose à partir de biomasse
US8231925B2 (en) 2004-08-20 2012-07-31 Cargill, Incorporated Ingredient systems comprising trehalose, food products containing trehalose, and methods of making same
US8231924B2 (en) 2004-08-20 2012-07-31 Cargill, Incorporated Ingredient systems comprising trehalose, food products containing trehalose, and methods of making same

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US4254227A (en) * 1978-03-09 1981-03-03 Kabushiki Kaisha Hayashibara Seibutsu Kagaku Kenkyujo Processes for producing syrups of syrup solids containing fructose-terminated oligosaccharides
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

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CHEMICAL ABSTRACTS, Volume 104, No. 13, 31 March 1986, (Columbus, Ohio, US), NAKAMURA, SANEHISA et al., "Preparation of syrup of sucrose-containing oligosaccharides", see page 574, abstract 107812j; & RYUKYU DAIGAKU NOGAKUBU GAKUJUTSU HOKOKU 1984, 31, 43-50. *
CHEMICAL ABSTRACTS, Volume 112, No. 7, 12 February 1990, (Columbus, Ohio, US), see page 591, abstract 53775u; & JP,A,1 179 698 "Manufacture of malto-oligosucroses from starches and sucrose with cyclodextrin glucanotransferase using ultrafiltration membranes", 17 July 1989. *
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Cited By (33)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US6017899A (en) * 1992-12-28 2000-01-25 Kabushiki Kaisha Hayashibara Seibutsu Kagaku Kenkyujo Non-reducing saccharide-forming enzyme, its preparation and uses
US5716838A (en) * 1992-12-28 1998-02-10 Kabushiki Kaisha Hayashibara Seibutsu Kagaku Kenkyujo Non-reducing saccharide-forming enzyme, its preparation and uses
EP0606753A3 (fr) * 1992-12-28 1995-06-14 Hayashibara Biochem Lab Enzyme de formation de saccharides non réductrices, et leur préparation et utilisations.
US5922580A (en) * 1992-12-28 1999-07-13 Kabushiki Kaisha Hayashibara Seibutsu Kagaku Kenkyujo Non-reducing saccharide-forming enzyme, its preparation and uses
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US8231925B2 (en) 2004-08-20 2012-07-31 Cargill, Incorporated Ingredient systems comprising trehalose, food products containing trehalose, and methods of making same
US8231924B2 (en) 2004-08-20 2012-07-31 Cargill, Incorporated Ingredient systems comprising trehalose, food products containing trehalose, and methods of making same
EP2402454A1 (fr) 2010-06-30 2012-01-04 Süd-Chemie AG Production de cellobiose à partir de biomasse
WO2012001102A1 (fr) 2010-06-30 2012-01-05 Süd-Chemie AG Production de cellobiose à partir d'une biomasse

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