CN106811493A - The preparation method of glucose 1- phosphoric acid - Google Patents
The preparation method of glucose 1- phosphoric acid Download PDFInfo
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- CN106811493A CN106811493A CN201510892112.7A CN201510892112A CN106811493A CN 106811493 A CN106811493 A CN 106811493A CN 201510892112 A CN201510892112 A CN 201510892112A CN 106811493 A CN106811493 A CN 106811493A
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Abstract
The invention discloses a kind of preparation method of glucose 1- phosphoric acid, belong to the enzymatic preparation field of glucose 1- phosphoric acid.The preparation method of glucose 1- phosphoric acid disclosed in this invention in a multienzymatic reaction system, glucose 1- phosphoric acid is converted a substrate into by acellular multienzyme efficient catalytic with the derivative of starch or starch as substrate；By process optimization, addition can promote amylolytic enzyme and the enzyme using accessory substance maltose to the present invention, so as to set up multienzymatic reaction system, be obviously improved the transformation efficiency of raw material and the yield of glucose 1- phosphoric acid.The inventive method feed stock conversion is high, and glucose 1- phosphoric acid yields are high, and step is simple and direct, and low production cost, effect on environment is small, is capable of achieving the large-scale production of glucose 1- phosphoric acid.
Description
Technical field
The present invention relates to the preparation method of glucose 1- phosphoric acid, more particularly to the method that starch and starch derivatives are converted into glucose 1- phosphoric acid for acellular many enzymatics, belong to the enzymatic production field of glucose 1- phosphoric acid.
Background technology
In organism, glucose 1- phosphoric acid (G 1-P) is to be catalyzed glycogen by glucosan phosphorylase, what the polysaccharide such as starch or maltodextrin and inorganic phosphate reactant salt were produced, it is first metabolin of gluconeogenesis approach, can be in phosphoglucomutase (PGM, EC 5.4.2.2) in the presence of generate G-6-P, into glycolysis or other metabolic pathways.Used as one kind activation glucose, G 1-P are in compounded saccharifying compound（Such as glycolipid, oligosaccharides, ribotide）Synthesis in be a kind of important precursor.Additionally, the compound can be also used for synthesizing artificial starch, electric power, and high yield pulp1 is produced to produce hydrogen by biological sugar battery.It is reported that G 1-P have anti-inflammatory and immunosuppressive therapy effect, its calcium salt has antitumaous effect, therefore, G 1-P are also worth with potential medical applications.So far, the application of glucose 1- phosphoric acid is not excavated fully yet, and this may be because of its too high production cost.
Because glucose 1- phosphoric acid has polarity very high, it is difficult to pass through complete cell membrane, glucose 1- phosphoric acid is catalyzed what corresponding disaccharides, oligosaccharides or polysaccharide were obtained typically by polysaccharide phospholylase.However, the simple method using polysaccharide phospholylase catalytic production glucose 1- phosphoric acid is with many not enough in the past.Such as, with disaccharides（Sucrose, trehalose or cellobiose）During as substrate, the price of disaccharides may be far above starch first, and by taking sucrose as an example, the theoretical maximum yield of its glucose 1- phosphoric acid calculated with glucose only has 50%, while along with the generation of fructose separation costs can be caused very high in production process.Although the cost of maltodextrin and starch is lower than disaccharides, but α -1 in substrate, the presence of 6 glycosidic bonds causes the glucosan phosphorylase can not fully to be reacted with substrate, maltotetraose or longer oligosaccharides are tended in the substrate selection of glucosan phosphorylase simultaneously, maltose and glucose cannot function as the substrate of glucosan phosphorylase, these reasons can all cause during using maltodextrin or starch as substrate, and product yield is low.Such as Weinhausel in nineteen ninety-five using 40 g/L maltodextrins as substrate, using deriving fromCorynebacterium callunaeGlucosan phosphorylase catalytic production glucose 1- phosphoric acid yield be 65 mM, conversion ratio is only 49%（The conversion ratio is mass transitions rate of the DEXTROSE ANHYDROUS 1- disodium hydrogen phosphates relative to starch, similarly hereinafter）, Bae in 2005 using 50 g/L soluble starches as substrate, using deriving fromThermus
caldophilusThe yield of GK24 glucosan phosphorylases production glucose 1- phosphoric acid is 132 mM, and conversion ratio is 80%.
The content of the invention
The technical problems to be solved by the invention are to provide a kind of enzymatic method for transformation of glucose 1- phosphoric acid, the method that glucose 1- phosphoric acid is produced by the derivative of acellular multienzyme catalytic starch and starch, the advantages of the method has glucose 1- phosphoric acid yield and high conversion rate, low production cost.
In order to solve the above technical problems, the technical solution used in the present invention is：
The present invention discloses a kind of preparation method of glucose 1- phosphoric acid first, comprises the following steps：
（1）With starch or starch derivatives as substrate, branching enzyme, glucosan phosphorylase are added（α-Glucan
Phosphorylase, EC 2.4.1.1）, glucanotransferase（4-a-glucanotransferase, EC 2.4.1.25）Or maltose phosphorylase（maltose
Phosphorylase, EC 2.4.1.8）Multienzymatic reaction system is set up, enzymic catalytic reaction is carried out；（2）Product is separated, is purified, obtained final product.
Wherein, step（1）The concentration of the substrate is 10 g/L；The debranching enzyme enzyme is isoamylase（Isoamylase, EC
3.2.1.68）Or Pullulanase（Pullulanase, EC 3.2.1.41）In any one or two kinds, the consumption of the glucosan phosphorylase is 0.05
U/mL, the maltose phosphorylase（Maltose phosphorylase, EC 2.4.1.8）Or glucanotransferase（EC 2.4.1.25）Consumption be 1 U/mL, the condition of the enzymic catalytic reaction is reacted 2-100 hours at 20-90 DEG C；Preferably, reacted 40 hours at 70 DEG C.
It is furthermore preferred that the concentration of the substrate is 10 g/L；The consumption of the glucosan phosphorylase is 5U/mL, and the consumption of the starch debranching enzyme is 1U/mL, and the consumption of the maltose phosphorylase or glucanotransferase is 1U/mL；
The enzymic catalytic reaction reacts 2-100 hours at 20-100 DEG C；Preferably, the enzymic catalytic reaction reacts 40 hours at 20-90 DEG C；Most preferably, the enzymic catalytic reaction reacts 40 hours at 70 DEG C.
The multienzymatic reaction system also contains following composition：Phosphate buffer, divalence magnesium ion；Preferably, the consumption of each composition is：The mM of phosphate 200, the mM of divalence magnesium ion 5；Wherein, the buffer solution is preferably phosphate buffer, it is furthermore preferred that the pH value 7.2 of buffer solution.
After reaction terminates, remaining starch residue will be low bifurcated starch, can now add a small amount of alpha amylase（EC
3.2.1.1）Promote the hydrolysis of starch residue, further improve the yield of glucose 1- phosphoric acid.The consumption of preferred alpha amylase is 0.1 U/ml.
The present invention with starch or starch derivatives as substrate, using glucosan phosphorylase as reaction core enzyme, by adding branching enzyme, glucanotransferase（EC 2.4.1.25）Or maltose phosphorylase（Maltose phosphorylase, EC
2.4.1.8）The glucose 1- phosphatase reaction systems of high yield pulp1 are set up, and high yield pulp1 can substantially reduce the separation costs of final glucose 1- phosphoric acid.
Because starch is the mixture of amylose and amylopectin.Side chain in amylopectin be with α -1, what 6 glycosidic bonds were connected with main chain, and glucosan phosphorylase can not decomposing alpha -1,6 glycosidic bonds.In order to improve the conversion ratio of glucose 1- phosphoric acid, the present invention is added in multienzymatic reaction system being capable of α -1, the debranching enzyme enzyme-isoamylase or Pullulanase of 6 glycosidic bonds in starch-splitting.Because the final product of glucosan phosphorylase hydrolysis starch is maltose, in order to utilize maltose, the present invention is added also in reaction system（4-a-glucanotransferase, EC 2.4.1.25）, the enzyme can be by the oligosaccharide of short chain oligosaccharide of the polymerization as long-chain, and the oligosaccharide of the long-chain can be re-used by glucosan phosphorylase such that it is able to improves the utilization rate of starch.Maltose is decomposed into Cori ester and glucose；Herein, glucanotransferase can be replaced partly by maltose phosphorylase.
Starch of the present invention and starch derivatives include non-hydrolysis starch, any one or more in boiling starch, amylodextrin, maltodextrin, malt polysaccharide or maltose.
Any one of multienzymatic reaction system of the present invention enzyme can also be replaced by enzyme of any one with equal function, preferably by the mutant enzyme with equal function that protein engineering house of correction is obtained.
By Starch Conversion in glucose 1- phosphoric acid tests, in a reaction system, with soluble starch as raw material, to add glucosan phosphorylase, the conversion ratio of final glucose 1- phosphoric acid is 67% for external many enzymatics of the invention.Isoamylase, glucanotransferase are it is possible to additionally incorporate in above-mentioned reaction system, while improving the consumption of glucosan phosphorylase, the conversion ratio of final glucose 1- phosphoric acid reaches 114%, and conversion ratio is significantly improved.
Technical solution of the present invention compared with prior art, has the advantages that：
The present invention, with starch and their derivative as raw material, glucose 1- phosphoric acid is catalytically conveted to by external multienzyme in a multienzymatic reaction system, and by process optimization, addition can promote amylolytic enzyme and utilize accessory substance（Maltose）Enzyme, significantly improve transformation efficiency, high yield pulp1 reduction glucose 1- phosphoric acid separation costs.The inventive method has simplicity, and raw material availability is high, glucose 1- phosphoric acid yields are high, low production cost, the advantages of, it is possible to achieve the large-scale production of glucose 1- phosphoric acid.
The term that the present invention relates to and definition
Unless otherwise defined, all technologies otherwise used herein and scientific terminology all have generally understand identical implication with those skilled in the art.
Term " enzymic catalytic reaction " means the chemical reaction carried out under biocatalyst-enzyme effect.
Term " glucose polymer " means the non-hydrolysis starch that glucose molecule is polymerized.
Term " glucose oligomers " means starch, amylodextrin, malt polysaccharide, maltose of partial hydrolysis etc..
Involved conversion ratio is glucose 1- disodium hydrogen phosphates in text（It is anhydrous）Relative to the mass transitions rate of starch（w/w*100%）
Brief description of the drawings
Fig. 1 is the schematic diagram of acellular many enzymatic pathways 1 of converted starch generation glucose 1- phosphoric acid；Wherein, IA, isoamylase；PA, Pullulanase；α GP, glucosan phosphorylase；4GT, glucanotransferase；
Fig. 2 is the schematic diagram of acellular many enzymatic pathways 2 of converted starch generation glucose 1- phosphoric acid；Wherein, IA, isoamylase；PA, Pullulanase；α GP, glucosan phosphorylase；MP, maltose phosphorylase.
Fig. 3 is that SDS-PAGE detects 3 key enzymes；Wherein, the 1st row, isoamylase；2nd row, glucosan phosphorylase；3rd row, glucanotransferase.
Fig. 4 is to analyze glucose 1- phosphoric acid using HPLC；Wherein, Fig. 3 is to distinguish glucose 1- phosphoric acid, glucose, phosphoric acid with HPLC modes.
Fig. 5 is that, with soluble starch as substrate, by the product after enzymatic reaction, arrow meaning represents the characteristic peak of glucose 1- phosphoric acid using HPLC detections.
Fig. 6 is that, with maltodextrin as substrate, by the product after enzymatic reaction, arrow meaning represents the characteristic peak of glucose 1- phosphoric acid using HPLC detections.
Fig. 7 is the production curve of the combination production glucose 1- phosphoric acid of different enzymes.Wherein, IA, isoamylase；α GP, glucosan phosphorylase；4GT, glucanotransferase.
Specific embodiment
Further describe the present invention with reference to specific embodiment, advantages of the present invention and feature will be with description and apparent.It should be understood that the embodiment is only exemplary, any limitation is not constituted to the scope of the present invention.It will be understood by those skilled in the art that the details of technical solution of the present invention and form can be modified or replaced without departing from the spirit and scope of the invention, but these modifications or replacement each fall within protection scope of the present invention.
Experiment material
Soluble starch, soluble starch, ACROS Products, production code member：424490020；
Cornstarch, corn starch, Sigma purchases, production code member：S4126-2KG
Maltodextrin, ALDRICH Products, production code member：419672；
PET20b carriers, Novagen, Madison, WI, USA；
Bacillus coli expression bacterium BL21 (DE3), Invitrogen, Carlsbad, CA, USA；
Most of enzyme in the present invention（Except glucanotransferase）Can be commercially available in Sigma companies；But can all be obtained by prokaryote gene expression according to gene engineering method；
Maltose phosphorylase can be bought from Sigma companies, and production code member is M8284；
Alpha amylase is bought from Sigma companies, and production code member is 10065;
Glucose（HK）Kit is determined, Sigma companies buy, and production code member is GAHK20-1KT.
Experimental example
1
Starch Conversion is glucose by external many enzymatics
1-
Phosphoric acid, improves Starch Conversion rate
By an external multienzyme catalyst system and catalyzing by Starch Conversion be glucose 1- phosphoric acid（Fig. 1）.These key enzymes include：（1）Branching enzyme IA；(2) glucosan phosphorylase（α GP, EC 2.4.1.1）, Cori ester is discharged from starch；（3）Glucanotransferase（4-a-glucanotransferase, EC
2.4.1.25）.
Because starch is that have branched chain, it is simple using glucosan phosphorylase can not completely by Starch Hydrolysis, because glucosan phosphorylase can only act on α-Isosorbide-5-Nitrae glycosidic bond, and branched chain be with α -1, what 6 glycosidic bonds were connected with main chain.This needs to add isoamylase（Isoamylase, EC 3.2.1.68）Hydrolyzing alpha -1,6 glycosidic bonds.Because the minimum substrate of glucosan phosphorylase is maltotriose, in order to lift the utilization ratio of maltodextrin, glucanotransferase is added, the enzyme can be by the oligosaccharide of short chain oligosaccharide of the polymerization as long-chain, so as to further lift the utilization ratio of starch.
In the present invention, isoamylase is derived fromSulfolobus tokodaii, numbering of the gene on KEGG is ST0928, and the genomic DNA of the bacterial strain is German Albert-Ludwigs-Universit t
Georg Fuchs professor's friendship of Freiburg is provided；Glucosan phosphorylase is derived fromThermotoga maritima, numbering of the gene on KEGG is TM1168；Glucanotransferase is derived fromThermococcus litoralis, numbering of the gene on KEGG is OCC10078.Above genomic DNA all can be from the official website of ATCC（www.atcc.org）Upper acquisition, gene can be obtained from corresponding genomic DNA with primer by PCR, and by Simple Cloning（You, C., et al. (2012). "Simple Cloning via Direct
Transformation of PCR Product (DNA Multimer) to Escherichia coli and Bacillus
subtilis." Appl. Environ. Microbiol. 78(5): 1593-1595.）Method be cloned into pET20b carriers (Novagen,
Madison, WI, USA) in, obtain corresponding expression vector pET20b-StIA, pET20b-TmaGP, pET20b-Ti4GF.These three plasmids are all converted to Bacillus coli expression bacterium BL21 (DE3)
In (Invitrogen, Carlsbad, CA), and protein expression and purifying are carried out, the result of protein purification is as shown in Figure 2.
Reaction is carried out in three 0.75 milliliter of reaction system respectively, and reaction system one contains 200
The phosphate buffer of mM（pH 7.2）, 10
G/L soluble starches, the divalence magnesium ion of 5 mM, the glucosan phosphorylase of 1U/ml；Contain the phosphate buffer of 200 mM in reaction system two（pH
7.2）, 10 g/ soluble starches, the divalence magnesium ion of 5 mM, the isoamylase of 1 U/ml, the glucosan phosphorylase of 1 U/ml；Contain the phosphate buffer of 200 mM in reaction system three（pH
7.2）, 10 g/L soluble starches, the divalence magnesium ion of 5 mM, the isoamylase of 1 U/ml, the glucosan phosphorylase of 1 U/ml, the glucanotransferase of 1 U/ml.Reaction carries out catalytic reaction at 60 DEG C, reacts 40 hours.
According to the difference of retention time, HPLC can be used to distinguish glucose 1- phosphoric acid, glucose, phosphoric acid in reaction solution；The mobile phase of HPLC is the dilute sulfuric acid of 5 mM.
Glucose 1- phosphoric acid can be used phosphoglucomutase coupling G 6 PD to determine the increase of NADH.Specific method is：Contain 10 mM Mg in 450 μ L reaction systems2+
, 20 U/mL phosphoglucomutases（PGM）, glucose 1- phosphoric acid testing samples, 400 μ L glucoses (HK) measure kit measurement liquid, 37 DEG C are reacted 20 min, and the increase of NADH is detected under 340 nm.
After reaction terminates, the glucose 1- phosphoric acid in first reaction system（Fig. 4）Final concentration be 3.7g/L, conversion ratio is 37%；Glucose 1- phosphoric acid in second reaction system（Fig. 4）Final concentration be 5.2 g/L, conversion ratio is 52 %；Glucose 1- phosphoric acid in 3rd reaction system（Fig. 4）Final concentration of 8.2 g/L, conversion ratio is 82%.
Experimental example
2
Starch Conversion is glucose by external many enzymatics
1-
Phosphoric acid
Isoamylase, glucosan phosphorylase, the preparation of glucanotransferase are with experimental example 1.
The phosphate buffer containing 200 mM in one 0.75 milliliter of reaction system（pH 7.2）, the divalence magnesium ion of 5 mM, the glucosan phosphorylase of 0.05 U/mL, the isoamylase of 1 U/mL, and 1 U/mL glucanotransferase, the soluble starch of 10 g/L carries out catalytic reaction at 40 DEG C, reacts 40 hours.
After reaction terminates, the final concentration of final glucose 1- phosphoric acid is 2.2 g/L, and conversion ratio is 22 %.
Experimental example
3
Starch Conversion is glucose by external many enzymatics
1-
Phosphoric acid
Isoamylase, glucosan phosphorylase, the preparation of glucanotransferase are with experimental example 1.
The phosphate buffer containing 200 mM in one 0.75 milliliter of reaction system（pH 7.2）, the divalence magnesium ion of 5 mM, the glucosan phosphorylase of 0.05 U/mL, the isoamylase of 1 U/mL, and 1 U/mL glucanotransferase, the soluble starch of 10 g/L carries out catalytic reaction at 80 DEG C, reacts 40 hours.
After reaction terminates, the final concentration of final glucose 1- phosphoric acid is 12.1 g/L, and conversion ratio is 121%.
Experimental example
4
The enzyme that glucose changes is promoted by process optimization and addition, by Starch Conversion is glucose using external many enzymatics
1-
Phosphoric acid
Glucosan phosphorylase, the preparation of glucanotransferase are with experimental example 1；Pullulanase（Pullulanase, EC
3.2.1.41）From the purchase of Sigma companies, production code member is P1067；Maltose phosphorylase is bought from Sigma companies, and production code member is M8284.
Because the Pullulanase bought from sigma companies can not be in high temperature（80oC）Lower reaction, therefore first 37oC Pullulanase processing soluble starch, then adds other enzymes, then 80oC reacts.
The phosphate buffer containing 200 mM in one 0.75 milliliter of reaction system（pH 7.2）, the divalence magnesium ion of 5 mM, the Pullulanase of 1 U/mL, the soluble starch of 10 g/L, catalytic reaction is carried out at 37 DEG C, and the glucosan phosphorylase of 5 U/mL is added after 10 hours of reaction, the maltose phosphorylase of 1 U/mL, catalytic reaction is carried out at 80 DEG C, reacts 40 hours.Final glucose 1- phosphoric acid（Fig. 4）Final concentration of 11.7g/L, conversion ratio reached 117%.
Then add a small amount of alpha amylase to promote the hydrolysis of residue starch in reaction system, improve the yield of glucose 1- phosphoric acid, the consumption of alpha amylase is 0.1
U/ml, reaction is first 37oC reacts 6 hours, continues thereafter with 80oC reacts 24 hours, final glucose 1- phosphoric acid（Fig. 4）Final concentration of 120 g/L, conversion ratio reached 120 %.
Experimental example
6
Maltodextrin is converted into glucose by external many enzymatics
1-
Phosphoric acid
Isoamylase, glucosan phosphorylase, with experimental example 1, maltose phosphorylase is bought from Sigma companies, and production code member is M8284 for the preparation of glucanotransferase；
Contain 200 in one 0.75 milliliter of reaction system
The phosphate buffer of mM（pH 7.2）, the divalence magnesium ion of 5 mM, the glucosan phosphorylase of 5 U/mL, the isoamylase of 1 U/mL, the glucanotransferase of 1 U/mL, the maltodextrin of 10 g/L（ALDRICH Products, production code member 419672）, catalytic reaction is carried out at 80 DEG C, react 40 hours.Final glucose 1- phosphoric acid（Fig. 5）Final concentration of 121 g/L, conversion ratio reached 121 %.
Experimental example
7
The non-hydrolysed corn starch of high concentration is converted into glucose by external many enzymatics
1-
Phosphoric acid
Isoamylase, glucosan phosphorylase, with experimental example 1, maltose phosphorylase is bought from Sigma companies, and production code member is M8284 for the preparation of glucanotransferase；
The phosphate buffer containing 1 M in one 0.75 milliliter of reaction system（pH 7.2）, the divalence magnesium ion of 5 mM, the glucosan phosphorylase of 10 U/mL, the isoamylase of 1 U/mL, the glucanotransferase of 2 U/mL, the cornstarch of 50 g/L carries out catalytic reaction at 70 DEG C, reacts 40 hours.Final glucose 1- phosphoric acid（Fig. 7）Final concentration of 60.8 g/L, conversion ratio reached 122%.
Claims (5)
1. a kind of preparation method of glucose 1- phosphoric acid, it is characterised in that comprise the following steps：
（1）With starch or starch derivatives as substrate, add glucosan phosphorylase to set up multienzymatic reaction system, carry out enzymic catalytic reaction；（2）Product is separated, is purified, obtained final product.
2. according to the preparation method described in claim 1, it is characterised in that：Also contain starch debranching enzyme in the multienzymatic reaction system, glucanotransferase, wherein glucanotransferase can be by maltose phosphorylase partial replacements, and the starch debranching enzyme is any one in isoamylase or Pullulanase or two kinds.
3. according to the preparation method described in claim 2, it is characterised in that：It is also possible to contain alpha amylase in the multienzymatic reaction system.
4. according to the preparation method described in claim 1, it is characterised in that：Step（1）The starch derivatives includes non-hydrolysis starch, any one or more in boiling starch, soluble starch, amylodextrin, maltodextrin, malt polysaccharide.
5. according to the preparation method described in claim 1 or 4, it is characterised in that the multienzymatic reaction system also contains following component：Phosphate buffer and divalence magnesium ion.
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Cited By (4)
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| US10138506B2 (en) | 2015-10-02 | 2018-11-27 | Bonumose Llc | Enzymatic production of D-tagatose |
| CN109706200A (en) * | 2017-10-26 | 2019-05-03 | 中国科学院天津工业生物技术研究所 | A method of preparing laminaribiose |
| CN110438100A (en) * | 2019-08-02 | 2019-11-12 | 中国科学院天津工业生物技术研究所 | A kind of method of biocatalysis synthetic glycerine glucoside |
| CN110819667A (en) * | 2018-08-08 | 2020-02-21 | 中国科学院天津工业生物技术研究所 | Method for preparing laminaribiose by starch conversion |
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Cited By (7)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US10138506B2 (en) | 2015-10-02 | 2018-11-27 | Bonumose Llc | Enzymatic production of D-tagatose |
| US10533202B2 (en) | 2015-10-02 | 2020-01-14 | Bonumose Llc | Enzymatic production of D-tagatose |
| US11034988B2 (en) | 2015-10-02 | 2021-06-15 | Bonumose, Inc. | Enzymatic production of D-tagatose |
| CN109706200A (en) * | 2017-10-26 | 2019-05-03 | 中国科学院天津工业生物技术研究所 | A method of preparing laminaribiose |
| CN110819667A (en) * | 2018-08-08 | 2020-02-21 | 中国科学院天津工业生物技术研究所 | Method for preparing laminaribiose by starch conversion |
| CN110438100A (en) * | 2019-08-02 | 2019-11-12 | 中国科学院天津工业生物技术研究所 | A kind of method of biocatalysis synthetic glycerine glucoside |
| CN110438100B (en) * | 2019-08-02 | 2022-08-09 | 中国科学院天津工业生物技术研究所 | Method for synthesizing glycerol glucoside through biocatalysis |
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Application publication date: 20170609 |