CN114958796A - Glycosylation method of curcumin - Google Patents

Glycosylation method of curcumin Download PDF

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CN114958796A
CN114958796A CN202210731651.2A CN202210731651A CN114958796A CN 114958796 A CN114958796 A CN 114958796A CN 202210731651 A CN202210731651 A CN 202210731651A CN 114958796 A CN114958796 A CN 114958796A
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curcumin
leu
gly
thr
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陈志超
杜喜林
樊冰
李庆廷
强耀锋
张鹏
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Shanghai Longyin Biotechnology Co ltd
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    • C12N9/1051—Hexosyltransferases (2.4.1)
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    • C12P19/44—Preparation of O-glycosides, e.g. glucosides
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    • C12Y204/00—Glycosyltransferases (2.4)
    • C12Y204/01—Hexosyltransferases (2.4.1)
    • C12Y204/01007—Sucrose phosphorylase (2.4.1.7)
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Abstract

The invention discloses a glycosylation method of curcumin, belonging to the technical field of biology. The amino acid sequence of the sucrose phosphatase gtfA is shown as a sequence 1. The sucrose phosphatase was cloned into Lactobacillus reuteri. The invention provides a high-efficiency turmeric glycosylation enzymatic reaction technology.

Description

Glycosylation method of curcumin
Technical Field
The invention belongs to the technical field of biology, and particularly relates to a curcumin glycosylation method.
Background
Curcumin (curculin) is a natural polyphenol plant compound which can be used as both medicine and food and is extracted from the rhizome of curcuma zedoary and curcuma longa of traditional Chinese medicines. Curcumin is also used in the united states to color pastry, mustard, curry and dairy products as well as rice, meat and fish dishes. In addition to these uses, curcumin also has good pharmacological properties, such as antioxidant, anticancer, anti-inflammatory and anti-fibrinolytic effects. Therefore, it has long been recognized as a potential health-promoting natural compound that can prevent heart disease and has hepatoprotective and nephroprotective activities. Over the past several decades, extensive studies have demonstrated the pharmacological mechanisms of curcumin, such as inhibition of experimental allergic encephalomyelitis to treat multiple central sclerosis, and as a sarcoplasmic/endoplasmic reticulum calcium pump against cystic fibrosis.
However, curcumin has very low water solubility, which results in poor pharmacokinetic/pharmacodynamic (PK/PD) properties, and low bioavailability, which prevents its further use. Therefore, improving the water solubility of curcumin has become an urgent technical problem in economic value. In the prior art, the water content of curcumin can be improved through a nano/microcapsule embedding mode, but the problem of bioavailability cannot be really solved by a dispersion method of a hydrophilic carrier (DOI: 10.1016/j.molstrac.2020.129774).
In the prior art, glycosylation is considered to be an effective means for effectively improving the water solubility and bioavailability of curcumin. Therefore, the efficient and low-cost glycosylation technical means is a key technology for obtaining the glycosylated curcumin. GR Vijayakumar discloses a technical scheme for glycosidation of curcumin by using amyloglucosidase in the prior art, however, the catalytic efficiency of the enzyme is low, and the molar conversion rate (glycosylation rate) of glycosylation can only reach 48 percent at most (DOI: 10.1108/02632770710753307). Y Kaminaga discloses a technical scheme for biocatalysis of curcumin glycosylation by using suspension cells of the roots of the catharanthus roseus, however, the glycosylation rate of curcumin is only 32 percent, and the yield is only 2.5 mu mol/g (DOI: 10.1016/S0014-5793 (03)) 01265-1.
Disclosure of Invention
The invention aims to provide a curcumin glycosylation method. To solve the above-mentioned problems of the prior art.
The purpose of the invention is realized by the following technical scheme.
A sucrose phosphatase gtfA for curcumin glycosylation has an amino acid sequence shown in sequence 1, and is cloned to Lactobacillus reuteri.
A method for glycosylation of curcumin comprises using sucrose phosphatase gtfA as catalyst, and obtaining glycosylated curcumin by enzymatic glycosyl transfer reaction in the presence of glycosyl donor.
Furthermore, the amino acid sequence of the sucrose phosphatase gtfA is shown as a sequence 1.
Furthermore, the sucrose phosphatase can be expressed by recombinant bacteria of expression hosts such as escherichia coli, pichia pastoris, saccharomyces cerevisiae, corynebacterium glutamicum and the like.
Further, the glycosyl donor is one of sucrose, maltose, 1-phosphate-glucose and 6-phosphate-glucose.
Preferably, the glycosyl donor is sucrose or 1-phospho-glucose.
Preferably, the enzymatic glycosyl transfer reaction is carried out under reaction conditions of pH 6.0-7.5 and temperature 35-45 ℃.
Further, the reaction condition of the enzymatic glycosyl transfer reaction is to add a surfactant as a solubilizer.
Preferably, the surfactant is sophorolipid.
Sucrose phosphatase (also known as sucrose: phospho α -D glucosyltransferase; EC 2.4.1.7) catalyzes the reversible conversion of sucrose (α -D-glucopyranosyl-1, 2- β -D-fructofuranoside) and phosphate to α -D-glucopyranosyl-1-phosphate (Glc1P) and D-fructose. The KEGG database indicates that sucrose phosphatase is involved in the breakdown and synthesis of sucrose. Sucrose phosphorylase is known in the art to catalyze three types of reactions between phosphate and glucose groups, including hydrolysis and synthesis of phosphate, and hydrolysis and transglycosylation of sugar groups. Arsenate can replace phosphate as a substrate for the glucose-based acceptor. Sucrose phosphatases have also been reported to be useful for glycosylation of polyphenols, including catechin and (-) -epigallocatechin.
The invention provides a high-efficiency turmeric glycosylation enzymatic reaction technology.
Detailed Description
The technical features of the present invention will be further described with reference to specific embodiments.
Example 1: expression of recombinant sucrose phosphatase A
The sucrose phosphatase A sequence 1) is subjected to codon optimization according to the codon bias of escherichia coli, and the optimized gene sequence is shown as a sequence 2. The sucrose phosphatase is derived from Lactobacillus reuteri (Lactobacillus reuteri) and is artificially optimized. The codon-optimized sucrose phosphatase A gene sequence was synthesized and subcloned into E.coli expression vector pET30a (+) (the gene synthesis and subcloning process was committed to Jinzhi corporation, Suzhou, pET30a (+) is a published commercial E.coli expression vector). The recombinant plasmid pET30a-A carrying the sucrose phosphatase A gene was transformed into the E.coli BL21(DE3) host by the same company, and screened overnight on LB-resistant solid medium containing chloramphenicol (34. mu.g/mL). And selecting single colonies of the positive clones, and respectively selecting the single colonies to shake flasks for expression of the recombinase. The shake flask induction expression of the recombinase adopts LB culture medium (peptone 10g/L, yeast powder 5g/L, sodium chloride 10g/L), the positive clone strain collected by the LB resistance solid culture medium is inoculated into a shake flask, and then cultured at 37 ℃ until the turbidity OD600 is 0.6-1.0, and then the induced recombinant sucrose phosphatase A expression (the final concentration in the shake flask is 0.4mM) of IPTG (isopropyl thiogalactoside) is added, and simultaneously, the temperature is reduced to 25 ℃ for culture for 8-14 h. The activity of sucrose phosphatase A enzyme was detected by using a sucrose phosphate synthase activity detection kit (manufactured by Shanghai Ji to Biochemical technologies, Ltd.) according to the instruction, and the clone top1 having the highest enzyme activity was selected as an expression strain of the recombinase.
The top1 clone was used as an expression strain, and enzyme production was performed in a 10L fermentor. The fermentation tank culture adopts fermentation medium (peptone 10g/L, yeast powder 5g/L, sodium chloride 8g/L, glycerol 10g/L, magnesium sulfate 1g/L, potassium dihydrogen phosphate 1g/L, dipotassium hydrogen phosphate 2g/L), feed is 30% glycerol, and ammonia water is used for controlling pH to be 7.0. After inoculating the fermentation tank, culturing at 37 ℃ for 5h, starting feeding, starting inducing when OD600 is 20, adding IPTG with final concentration of 0.4mM, cooling to 25 ℃, culturing, fermenting for 22h, and discharging. Then, the cells were collected by centrifugation as crude sucrose phosphatase A.
Example 2: expression of sucrose phosphatase A catalyzes curcumin glycosylation
The reaction was carried out using 1. mu.M phosphate buffer as a reaction system containing 30mg/mL of a glycosyl donor, 10mg/mL of the crude sucrose phosphatase gtfA prepared in example 1, 1mg/mL of sophorolipid (Boston Biotech., Ltd.), 0.5mmol/L of curcumin, followed by catalyzing the enzymatic reaction at 37 ℃ for 12 hours with dynamic shaking. The glycosylation donors added in the reaction are shown in table 1.
Before and after the reaction, the content of curcumin and its glycosylated derivatives was measured by HPLC external standard method, the analysis conditions of HPLC were that the column used Cosmosil 5C18-ARII column, 4.6U150mm, Nacalai Tesque, and the mobile phase used the following gradient elution of methanol with water: from 0 to 14 minutes, methanol ratio increased from 40% to 80%; the methanol ratio is increased from 80% to 100% in 14 to 15 minutes, and the isocratic elution with 100% methanol is maintained in 15 to 20 minutes. The flow rate was 1.0 ml/min. The elution was monitored at 423nm on a DAD detector. The amount of product was calculated based on the calibration curve prepared using each curcuminoside.
TABLE 1 glycosylated curcumin product content after different glycosyl donor reactions
Figure BDA0003714125120000051
Example 3: transglycosylation of other sucrose phosphatases
Sucrose phosphatases from other strains were expressed according to the procedure of example 1, including those from the strain Ruminococcus calillidus, AmyAc sucrose phosphatase (NCBI Reference Sequence: WP-022410484.1), gtfA sucrose phosphatase from the strain Lactobacillus crispatus (NCBI Reference Sequence: WP-060461996.1), sucrose phosphatase from Paenibacillus sp.A3 (NCBI Reference Sequence: WP-054973973.1), and sucrose phosphatase from Marinobacter flavimaris (NCBI Reference Sequence: WP-104270647.1). The gene sequences and amino acid sequences of all enzymes can be queried and obtained publicly from the NCBI database (https:// www.ncbi.nlm.nih.gov /) by means of the NCBI Reference Sequence number. Then, the sucrose phosphatase recombinant enzymes from different sources are subjected to the glycosyl transfer test of Curcumin according to the method described in the embodiment example 2, however, the production of Curcumin 4 '-O-glucoside or Curcumin 4' 4-O-diglucoside or other glycosyl Curcumin is not detected by all 4 recombinant enzymes, so that the sugar phosphatases from the 4 other strains do not have the glycosyl transfer capability of Curcumin as a receptor.
Figure BDA0003714125120000071
Figure BDA0003714125120000081
Figure BDA0003714125120000091
Sequence listing
<110> Shanghai dragon Yin Biotech Co., Ltd
<120> a method for glycosylation of curcumin
<160> 2
<170> SIPOSequenceListing 1.0
<210> 1
<211> 485
<212> PRT
<213> Lactobacillus reuteri (Lactobacillus reuteri)
<400> 1
Met Pro Ile Leu Ala Gly Ala Met Leu Ile Thr Thr Ser Ala Ser Met
1 5 10 15
Gly Leu Ala Ile Leu Gly Thr His Gly Val Leu Leu Ala Thr Ile Gly
20 25 30
Ala Ala Ile Gly Gly Val His Leu Leu Pro Pro Pro Pro Ser Thr Gly
35 40 45
Ala Ala Gly Pro Ala Pro Thr Ala Thr Ala Val Val Ala Ser Ala Pro
50 55 60
Gly Ala Thr Ala Ala Val Gly Ala Leu Gly Gly Ala Thr Thr Leu Met
65 70 75 80
Pro Ala Pro Met Ile Ala His Ile Ser Leu Leu Ser Gly Met Thr Gly
85 90 95
Ala Pro Leu Leu Leu His Ala Ala Ser Leu Thr Ala Ala Pro Pro Ile
100 105 110
Ala Thr Gly Leu Pro Thr Gly Leu Ala Gly Leu Ala Ala Pro Thr Gly
115 120 125
Gly Ala Val Ala Leu Ile Thr Leu Ala Leu Ala Leu Ala Pro Leu Gly
130 135 140
Gly Ile Thr Pro Ala Ala Gly Thr Thr Gly Ala Leu Thr Ala Thr Pro
145 150 155 160
Gly Gly Gly Gly Ile Ala Ile Ala Val Leu Ser Leu Val Ala Ala Gly
165 170 175
Pro Pro Leu Gly Thr Leu Ile Ala Met Val Leu His Gly Ala Ala Met
180 185 190
Ile Ala Leu Ala Ala Pro Ala Thr Ala Ile Leu Leu Val Gly Thr Ala
195 200 205
Ala Pro Pro Val Gly Pro Gly Ile Thr Ala Leu Leu Ala Gly Val Gly
210 215 220
Ala Ile Leu Ala Pro Thr Leu Ala Ile Ile Leu Pro Gly Ile His Gly
225 230 235 240
His Thr Thr Ile Pro Gly Leu Ile Ser Gly His Ala Pro Pro Ile Thr
245 250 255
Ala Pro Thr Leu Pro Met Thr Thr Leu Thr Thr Leu Thr Ser Gly Leu
260 265 270
Thr Ala Ala Leu Ala Leu Thr Leu Leu Met Ser Pro Met Leu Gly Pro
275 280 285
Thr Thr Leu Ala Thr His Ala Gly Ile Gly Val Val Ala Ala Leu Ala
290 295 300
Ile Leu Thr Ala Ala Gly Ile Gly Thr Ala Ser Ala Gly Leu Thr Leu
305 310 315 320
Val Gly Ala Ala Val Leu Ala Leu Thr Ser Ser Ala Gly Thr Ala Ala
325 330 335
Leu Ala Ile Thr Gly Ile Ala Ser Thr Thr Thr Ser Ala Leu Gly Ala
340 345 350
Ala Ala Leu Ala Thr Leu Leu Ser Ala Ala Pro Gly Val Pro Ala Pro
355 360 365
Gly Ile Pro Met Val Thr Thr Val Gly Leu Leu Ala Gly Ser Ala Ala
370 375 380
Leu Gly Leu Leu Gly Leu Thr Leu Gly Gly Ala Ala Ile Ala Ala His
385 390 395 400
Thr Thr Thr Leu Gly Gly Val Ala Gly Gly Val Gly Ala Pro Val Val
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Leu Ala Leu Leu Ala Leu Leu Ala Thr Ala Ala Leu Pro Ala Ala Pro
420 425 430
Ala Leu Ala Gly Ser Ile Gly Val Leu Thr Pro Thr Gly Thr Thr Ile
435 440 445
Leu Val Thr Ala Leu Ala Leu Ala Gly Leu Ala Val Ala Val Leu Ala
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Ala Ala Ala Ala Ala Leu Thr Pro Thr Ile Thr Ala Ala Gly Gly Leu
465 470 475 480
Val Met Gly Gly Leu
485
<210> 2
<211> 1455
<212> DNA
<213> Lactobacillus reuteri (Lactobacillus reuteri)
<400> 2
atgccgatca aaaacgaagc catgctgatt acgtacagcg attctatggg taaaaacatc 60
aaagaaactc atgaagtgct gaagaactac atcggtgatg cgattggtgg tgtgcacctg 120
ctgccgttct tcccgtctac cggtgaccgt ggcttcgcac cgtatcgtta cgacgttgtt 180
gacagcgcct tcggcaactg ggatgatgtt gaagctctgg gtgaagatta ctacctgatg 240
ttcgacttca tgatcaacca catctctaaa aaaagcgaaa tgtatcagga ttttaagaaa 300
aaacacgatg actctaaata taacgatttc ttcattcgtt gggaaaaatt ttgggaaaaa 360
gccggcaaaa accgcccgac ccaggaagac gtagacctga tctataaacg caaagacaaa 420
gccccgaaac aggaaatcac cttcgatgat ggtactacgg aaaacctgtg gaacactttc 480
ggtgaagaac agattgatat taacgttaag tccaaagtag cgaacgaatt ttttaaagaa 540
acgctgattg atatggttaa acacggtgct gatatgatcc gtctggatgc cttcgcgtat 600
gctattaaaa aagtcggcac caacgacttc tttgttgaac ctgaaatctg ggacctgctg 660
aacgaggttc aagacatcct ggcaccgtac aaagcaatca tcctgccgga gatccacgaa 720
cactacacta ttccgcagaa aatcagccag cacgatttct tcatctacga ttttaccctg 780
cctatgacca ccctgtacac tctgtacagc ggtaaaacca accgcctggc taaatggctg 840
aaaatgtctc cgatgaaaca gtttaccact ctggataccc acgacggcat cggtgtggtt 900
gatgcgaagg acattctgac cgacgacgaa atcgaatacg cttctaacga gctgtataaa 960
gttggtgcca atgtgaaacg taaatattcc tctgctgaat acaacaacct ggacatctac 1020
cagattaact ctacctacta ctctgctctg ggcgatgacg ataaagcata tctgctgtcc 1080
cgtgcattcc aggtgttcgc accgggtatt ccgatggttt actacgtagg tctgctggct 1140
ggttctaacg acctggagct gctggaaaaa accaaagagg gccgtaacat caaccgtcac 1200
tattacacca aagaagaagt tgcgcaagag gttcaacgcc cggtggtcaa aaacctgctg 1260
gatctgctgg cgtggcgtaa caaattcgcc gcctttgatc tggatggctc tatcgaagtg 1320
aagactccga ccgaaactac tattaaagtc acccgtaaag acaaggatgg taaaaacgtc 1380
gcggtgctgg atgctgatgc ggccaacaaa acgttcacta tcaccgcgaa tggcgagaaa 1440
gttatggaac agaaa 1455

Claims (9)

1. A sucrose phosphatase gtfA useful for curcumin glycosylation characterized by: the amino acid sequence is shown in sequence 1.
2. The sucrose phosphatase gtfA useful for curcumin glycosylation according to claim 1, characterized in that: the sucrose phosphatase was cloned into Lactobacillus reuteri.
3. A method of glycosylating curcumin, characterized by: using sucrose phosphatase gtfA as catalyst, and obtaining glycosylated curcumin by enzymatic glycosyl transfer reaction in the presence of glycosyl donor.
4. A method of glycosylating curcumin as claimed in claim 3, wherein: the sucrose phosphatase can be a recombinant bacterium expressed by an expression host of escherichia coli, pichia pastoris, saccharomyces cerevisiae and corynebacterium glutamicum.
5. A method of glycosylating curcumin as claimed in claim 3, wherein: the glycosyl donor is one of sucrose, maltose, 1-phosphate-glucose and 6-phosphate-glucose.
6. A method of glycosylating curcumin as claimed in claim 5, wherein: the glycosyl donor is sucrose or 1-phosphate-glucose.
7. A method of glycosylating curcumin as claimed in claim 3, wherein: the reaction conditions of the enzymatic glycosyl transfer reaction are that the reaction pH is 6.0-7.5 and the temperature is 35-45 ℃.
8. A method of glycosylating curcumin as claimed in claim 3, wherein: the reaction condition of the enzymatic glycosyl transfer reaction is to add a surfactant as a solubilizer.
9. The method of glycosylating curcumin of claim 8, wherein: the surfactant is sophorolipid.
CN202210731651.2A 2022-06-26 2022-06-26 Glycosylation method of curcumin Pending CN114958796A (en)

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