CN108330154B - Application of esterase EstP00714 in catalytic resolution of racemic linalyl acetate to obtain (S) -linalool - Google Patents

Application of esterase EstP00714 in catalytic resolution of racemic linalyl acetate to obtain (S) -linalool Download PDF

Info

Publication number
CN108330154B
CN108330154B CN201810078725.0A CN201810078725A CN108330154B CN 108330154 B CN108330154 B CN 108330154B CN 201810078725 A CN201810078725 A CN 201810078725A CN 108330154 B CN108330154 B CN 108330154B
Authority
CN
China
Prior art keywords
esterase
estp00714
racemic
linalyl acetate
linalool
Prior art date
Legal status (The legal status 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 status listed.)
Expired - Fee Related
Application number
CN201810078725.0A
Other languages
Chinese (zh)
Other versions
CN108330154A (en
Inventor
胡云峰
公颜慧
马三梅
王永飞
许永楷
张云
孙爱君
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
South China Sea Institute of Oceanology of CAS
Original Assignee
South China Sea Institute of Oceanology of CAS
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 South China Sea Institute of Oceanology of CAS filed Critical South China Sea Institute of Oceanology of CAS
Priority to CN201810078725.0A priority Critical patent/CN108330154B/en
Publication of CN108330154A publication Critical patent/CN108330154A/en
Application granted granted Critical
Publication of CN108330154B publication Critical patent/CN108330154B/en
Expired - Fee Related legal-status Critical Current
Anticipated expiration legal-status Critical

Links

Images

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
    • C12P41/00—Processes using enzymes or microorganisms to separate optical isomers from a racemic mixture
    • C12P41/003—Processes using enzymes or microorganisms to separate optical isomers from a racemic mixture by ester formation, lactone formation or the inverse reactions
    • C12P41/004—Processes using enzymes or microorganisms to separate optical isomers from a racemic mixture by ester formation, lactone formation or the inverse reactions by esterification of alcohol- or thiol groups in the enantiomers or the inverse reaction
    • 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
    • C12P7/00—Preparation of oxygen-containing organic compounds
    • C12P7/02—Preparation of oxygen-containing organic compounds containing a hydroxy group
    • C12P7/04—Preparation of oxygen-containing organic compounds containing a hydroxy group acyclic

Landscapes

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

Abstract

The invention discloses application of esterase EstP00714 in catalytic resolution of racemic linalyl acetate to obtain (S) -linalool. The invention uses esterase EstP00714 as a catalyst, obtains (S) -linalool with an enantiomeric excess value of more than 96 percent by optimizing a reaction system and reaction conditions, and the conversion rate reaches 55 percent. Compared with the traditional chemical resolution, the method has the advantages of mild reaction conditions, no pollution and high enantiomeric excess value. Can be used in the fields of biological medicine, cosmetics, fine chemical engineering and the like, and has great application value.

Description

Application of esterase EstP00714 in catalytic resolution of racemic linalyl acetate to obtain (S) -linalool
The technical field is as follows:
the invention belongs to the fields of biochemical engineering and biotechnology, and particularly relates to application of esterase EstP00714 in catalytic resolution of racemic linalyl acetate to obtain (S) -linalool.
Background art:
esterases (EC 3.1.1.1) are widely found in animals, plants and microorganisms and are a class of enzymes that catalyze hydrolysis or the formation of ester bonds, the substrates for which are usually esters with less than ten carbon atoms in the aliphatic chain. The esterase belongs to an alpha/beta sheet hydrolase superfamily, a catalytic center consists of serine, aspartic acid/glutamic acid and histidine, and a conserved sequence is a pentapeptide (GXSXG) sequence near the serine. Esterase can catalyze various chemical reactions such as hydrolysis, esterification, transesterification and the like, is an important industrial biocatalyst, and is widely applied to the fields of fine chemical engineering, washing, medicines, food, papermaking, leather processing, textile, wastewater treatment, feed industry and the like. From the catalytic property, the esterase has high chemoselectivity and stereoselectivity, and the reaction does not need coenzyme, has mild reaction condition and less byproducts. Another significant feature of esterases in production applications is their ability to function in heterogeneous systems (i.e., oil-water interfaces) or in the organic phase. In the aqueous phase, esterases generally catalyze hydrolysis reactions, while in the organic phase, esterases catalyze esterification and transesterification reactions. The method for preparing the novel drug intermediate or removing the non-effective components of the drug racemate by the biotransformation of microbial esterase is an important chiral technology, has very wide application prospect, can provide a new platform for synthesizing chiral drugs, and provides a new method for preparing optical pure compounds in large quantities. The enzymatic method for selectively resolving the racemate compound has the advantages of high stereospecificity, less side reaction, high yield, good optical purity of the product and mild reaction conditions, so the method is a widely accepted resolving method.
The invention content is as follows:
the invention aims to provide application of esterase EstP00714 in catalytic resolution of racemic linalyl acetate to obtain (S) -linalool.
The esterase EstP00714 (the amino acid sequence of the esterase is shown in SEQ ID NO. 2) and the coding gene EstP00714 (the nucleotide sequence of the esterase is shown in SEQ ID NO. 1) are developed from a strain of pseudomonas pseudomonad antipruralis HUP007, a recombinant expression vector containing the esterase gene EstP00714 and a genetic engineering bacterium are constructed, and the esterase EstP00714 is obtained after the genetic engineering bacterium is cultured and can be applied to catalyzing ester hydrolysis reaction.
The esterase EstP00714 disclosed by the invention is applied to catalytic resolution of racemic linalyl acetate to obtain (S) -linalool, and the amino acid sequence of the esterase EstP00714 is shown as SEQ ID No. 2.
Preferably, the catalytic resolution of racemic linalyl acetate to (S) -linalool is carried out in the presence of an organic solvent and/or a surfactant.
The organic solvent is preferably ethanol.
The surfactant is preferably sodium tripolyphosphate.
The reaction system for obtaining (S) -linalool by catalytically resolving racemic linalyl acetate is preferably as follows: comprises 20mg/mL esterase EstP00714, 50mM substrate racemic linalyl acetate, 10% volume fraction ethanol and 5g/L sodium tripolyphosphate, and the balance pH6PBS buffer.
The reaction temperature for obtaining (S) -linalool by catalytically resolving racemic linalyl acetate is 30 ℃, and the reaction time is 2 hours.
The esterase gene Estp00714 of the invention is derived from Pseudomonas aeruginosa antitumoralisHUP007 (stored in the south China sea research institute of academy of sciences). The amino acid sequence of the esterase EstP00714 is shown as SEQ ID NO.2, the nucleotide sequence of the coding gene EstP00714 is shown as SEQ ID NO.1, and the esterase EstP00714 is disclosed in the patent application number: 201610605466.3, title of the invention: in a patent application of esterase EstP00714 and a coding gene and application thereof, a preparation method of the esterase EstP00714 is disclosed in the patent, so that esterase EstP00714 enzyme powder (namely purified esterase EstP00714) can be obtained.
The invention uses esterase EstP00714 as a catalyst, obtains (S) -linalool with an enantiomeric excess value of more than 96 percent by optimizing a reaction system and reaction conditions, and the conversion rate reaches 55 percent. Compared with the traditional chemical resolution, the method has the advantages of mild reaction conditions, no pollution and high enantiomeric excess value. Can be used in the fields of biological medicine, cosmetics, fine chemical engineering and the like, and has great application value.
Description of the drawings:
FIG. 1 shows the effect of substrate concentration on the resolution of racemic linalyl acetate by esterase EstP 00714.
FIG. 2 shows the effect of enzyme concentration on the resolution of racemic linalyl acetate by esterase EstP 00714.
FIG. 3 shows the effect of reaction time on the resolution of racemic linalyl acetate by esterase EstP 00714.
FIG. 4 is a gas chromatogram of racemic linalyl acetate before reaction; wherein, 1 represents racemic linalyl acetate.
FIG. 5 is a gas chromatogram of (. + -.) -linalool; wherein R represents (R) -linalool and S represents (S) -linalool.
FIG. 6 is a gas chromatogram of racemic linalyl acetate and the product linalool after the reaction; wherein R represents (R) -linalool, S represents (S) -linalool, and 1 represents linalyl acetate.
The specific implementation mode is as follows:
the following examples are further illustrative of the present invention and are not intended to be limiting thereof.
The esterase gene Estp00714 is derived from Pseudomonas atrophaeus HUP007, which is stored in the south China sea research institute laboratory. The amino acid sequence of the esterase EstP00714 is shown as SEQ ID NO.2, the nucleotide sequence of the coding gene EstP00714 is shown as SEQ ID NO.1, and the esterase EstP00714 is disclosed in the patent application number: 201610605466.3, title of the invention: in a patent application of esterase EstP00714 and a coding gene and application thereof, a preparation method of the esterase EstP00714 is disclosed in the patent, so that purified esterase EstP00714 (namely esterase EstP00714 enzyme powder) can be obtained.
Example 1: esterase EstP00714 resolution of racemic linalyl acetate
1.1 Effect of reaction pH and temperature on the resolution of racemic linalyl acetate by esterase EstP00714
The reaction system with different pH values is 0.5mL, and comprises 10mg esterase EstP00714 enzyme powder, 50mM substrate racemic linalyl acetate, and the balance of reaction buffer solutions with different pH values; the reaction was carried out for 2h at different temperatures. GC measures the stereoselectivity of esterase EstP00714 for resolving racemic linalyl acetate, and the enantiomeric excess value (e.e.) and the conversion rate (C) of the product are calculated according to the peak area, and the results are shown in Table 1.
Equation 1:
Figure BDA0001560359310000041
equation 2:
Figure BDA0001560359310000042
in the formula: a. theSAnd ARRespectively represent the peak areas of (S) -linalool and (R) -linalool, A0And A represents the peak areas of linalyl acetate before and after the reaction.
The conversion (C) increases with increasing pH between pH6.0 and 10.0, but the e.e. decreases with increasing pH. The highest e.e.92% was obtained at pH 6.0. Thus, the esterase EstP00714 has the optimum pH value of 6.0 for resolving racemic linalyl acetate.
C increases and then decreases with increasing temperature, and the e.e. decrease is not significant between 25-35 ℃. The C decreases significantly when the temperature is higher than 35 ℃, which is associated with the high temperature affecting the activity of the enzyme. The maximum conversion of 55% was achieved at 30 ℃ and the e.e. reached 94%. Thus, the esterase EstP00714 has an optimum temperature of 30 ℃ for resolving racemic linalyl acetate.
TABLE 1 Effect of reaction pH and temperature on the resolution of racemic linalyl acetate by esterase EstP00714
Figure BDA0001560359310000043
Figure BDA0001560359310000051
aThe expression PBS buffer is used herein to indicate,brepresents a Tris/HCl buffer
1.2 Effect of organic solvent on resolution of racemic linalyl acetate by esterase EstP00714
The reaction system is 0.5mL, and comprises 10mg esterase EstP00714 enzyme powder, 50mM substrate racemic linalyl acetate, 10% volume fraction, 30% organic solvent and the balance of PBS buffer solution with the pH value of 6.0; using no organic solvent as a reference; the reaction is carried out for 2h at 30 ℃, and the results are shown in Table 2 by detecting with a gas chromatography chiral column.
TABLE 2 Effect of organic solvents on the resolution of racemic linalyl acetate by esterase EstP00714
Figure BDA0001560359310000052
It can be seen from Table 2 that the stereoselectivity of esterase EstP00714 was slightly improved in the presence of most of the organic solvent, but the conversion was reduced to a different extent in the alkanes. Although the e.e. reaches 98% in the presence of 10% by volume of isooctane, n-hexane and toluene, the relative decrease of C is more obvious. In ethanol with a volume fraction of 10%, both e.e. and C were increased to 97% and 52%, respectively. Ethanol was therefore used as a co-solvent in subsequent experiments.
1.3 Effect of surfactants on the resolution of racemic linalyl acetate by esterase EstP00714
Under optimized conditions (30 ℃, pH6.0PBS buffer solution), the reaction system is 0.5mL, and comprises 10mg esterase EstP00714 enzyme powder, 50mM substrate racemic linalyl acetate, ethanol with the final concentration of 10% by volume fraction, 1g/L, 5g/L and 10g/L of surfactants (sodium tripolyphosphate, Tween-20, Tween-80 and TritonX-100), and the balance pH6.0PBS buffer solution; after 2h reaction at 30 ℃ with no surfactant added as a control, samples were used for GC detection, and the results are shown in Table 3. As can be seen from Table 3, compared with the control, 4 surfactants had no significant effect on the e.e. resolution of racemic linalyl acetate by esterase EstP00714, and 5g/L sodium tripolyphosphate could increase the conversion rate to 54%, so 5g/L sodium tripolyphosphate was added in the subsequent experiments.
TABLE 3 Effect of surfactants on the resolution of racemic linalyl acetate by esterase EstP00714
Figure BDA0001560359310000061
1.4 Effect of substrate concentration on the resolution of racemic linalyl acetate by esterase EstP00714
Under optimized conditions (30 ℃, pH6.0PBS buffer solution), the reaction system is 0.5mL, and comprises 10mg esterase EstP00714 enzyme powder, 10-100mM substrate racemic linalyl acetate, 10% volume fraction ethanol, 5g/L sodium tripolyphosphate and the balance of pH6.0PBS buffer solution; after 2h reaction at 30 ℃ the samples were used for GC detection and the results are shown in FIG. 1. As can be seen from fig. 1, the conversion C gradually decreases as the substrate concentration increases, the e.e. slowly increases. Indicating that higher concentrations of substrate inhibit the enzymatic reaction and decrease the conversion. At substrate concentrations >50mM, e.e. is essentially unchanged, so that the optimum substrate concentration for the resolution of racemic linalyl acetate by esterase EstP00714 is 50mM, with 96% and 50% for e.e. and C, respectively.
1.5 Effect of enzyme concentration on the resolution of racemic linalyl acetate by esterase EstP00714
Under optimized conditions (30 ℃, pH6.0PBS buffer solution), the reaction system is 0.5mL, and comprises 5-35mg esterase EstP00714 enzyme powder, 50mM substrate racemic linalyl acetate, ethanol with the volume fraction of 10%, 5g/L sodium tripolyphosphate and the balance of pH6.0PBS buffer solution; GC detection after 2h reaction at 30 ℃ gave the results shown in FIG. 2. As can be seen from fig. 2, the e.e. and conversion do not vary much with increasing enzyme concentration. At an enzyme concentration of 20mg/mL, the e.e. and conversion were 96% and 53%, respectively.
1.6 Effect of reaction time on resolution of racemic linalyl acetate by esterase EstP00714
Under optimized conditions (30 ℃, pH6.0PBS buffer solution), the reaction system is 0.5mL, and comprises 10mg esterase EstP00714 enzyme powder, 50mM substrate racemic linalyl acetate, 10% volume fraction of ethanol, 5g/L sodium tripolyphosphate and the balance of pH6.0PBS buffer solution; reacting at 30 ℃, taking out 500 mu L of the mixture every 1h, extracting the mixture by using ethyl acetate, removing water by using anhydrous sodium sulfate, adding L-methyl lactate as an internal standard, and detecting the mixture by using a gas chromatography chiral column. The results of the resolution of racemic linalyl acetate by esterase EstP00714 at different reaction times are shown in FIG. 3.
As can be seen from fig. 3, C gradually increased with time, and over the 2h reaction, the e.e. and conversion reached substantially the highest, 96% and 55%, respectively. After 2h, neither the conversion nor the e.e. change was significant. FIGS. 4, 5 and 6 are gas chromatograms of racemic linalyl acetate, (±) -linalool before reaction and linalyl acetate and linalool after reaction, respectively.
Sequence listing
<110> Nanhai ocean institute of Chinese academy of sciences
Application of <120> esterase EstP00714 in catalytic resolution of racemic linalyl acetate to obtain (S) -linalool
<160>2
<170>SIPOSequenceListing 1.0
<210>1
<211>1146
<212>DNA
<213> Pseudomonas HUP007 (Pseudonocardia antipruralis HUP007)
<400>1
gtgcagatcc agggtcacta tgagctgaag ttcgaggcgg tgcgcgatgc cttcgccgcg 60
ttgttcgagg atccccagga acgtggtgcc gcattgtgca tccaggttgg cggcgagacc 120
gtggtcgacc tgtgggccgg cagcgccgac aaggacggcc gcgaggcctg gcacagcgat 180
accatcgcca acctgttctc ctgcaccaag accttcaccg ccgtcaccgc cctgcaactg 240
gtgggcgagg gcaagctggc cctcgatgcg ccggtggcgc gctactggcc ggagttcgcc 300
caggccggca aggagcaggt caccctgcgc cagttgctca gccaccgcgc cggcctgccg 360
gccatccgcg agctgctgcc ggccgaggcg ctgtacgact ggcaagccat ggttgatgcc 420
ctggccgccg aagcgccctg gtggacaccc ggaagcgaac acggttacgc ggcgatcacc 480
tatggctggc tgatcggtga gctgatccgc cgcgccgacg gtcgcggccc gggcgactcg 540
atcgtggctc gcaccgcccg gccattgggg ttggatttcc atgtcggcct ggccgacgac 600
gagttccacc gcgtggcgca tatcgcccgc ggcaagggca accccggcga tgccgcggcc 660
cagcgcctgc tgcaggtcac catgcgcgag cccgaggccc tgtcgacccg ggccttcacc 720
aacccgccgg cgatcctcac cagcaccaac aagcccgaat ggcggcgcat gcagcagcca 780
gcggccaatg gccacggcaa cgcccgcagc ctggcgggct tctatgccgg cctgctcgac 840
ggcagcctgc tggagtccga gctgctcgac gaactgaccc gcgagcacag cctcggccag 900
gaccgcaccc tgttgaccca gacccgcttc ggcctgggct gcatgctcga ccagccagaa 960
gtggccaacg ccactttcgg ccttggcgcg cgggcgttcg gccatcccgg cgcgggcggc 1020
tcggtcggct ttgccgaccc cgaacacgac gtggcctttg gcttcgtcac caataccctg 1080
ggcccctatg tgctgatgga cccgcgcgct caacgcctgg tgcgtgtcct tggcagttgc 1140
ctttga 1146
<210>2
<211>381
<212>PRT
<213> Pseudomonas HUP007 (Pseudonocardia antipruralis HUP007)
<400>2
Val Gln Ile Gln Gly His Tyr Glu Leu Lys Phe Glu Ala Val Arg Asp
1 5 10 15
Ala Phe Ala Ala Leu Phe Glu Asp Pro Gln Glu Arg Gly Ala Ala Leu
20 25 30
Cys Ile Gln Val Gly Gly Glu Thr Val Val Asp Leu Trp Ala Gly Ser
35 40 45
Ala Asp Lys Asp Gly Arg Glu Ala Trp His Ser Asp Thr Ile Ala Asn
50 55 60
Leu Phe Ser Cys Thr Lys Thr Phe Thr Ala Val Thr Ala Leu Gln Leu
65 70 75 80
Val Gly Glu Gly Lys Leu Ala Leu Asp Ala Pro Val Ala Arg Tyr Trp
85 90 95
Pro Glu Phe Ala Gln Ala Gly Lys Glu Gln Val Thr Leu Arg Gln Leu
100 105 110
Leu Ser His Arg Ala Gly Leu Pro Ala Ile Arg Glu Leu Leu Pro Ala
115 120 125
Glu Ala Leu Tyr Asp Trp Gln Ala Met Val Asp Ala Leu Ala Ala Glu
130 135 140
Ala Pro Trp Trp Thr Pro Gly Ser Glu His Gly Tyr Ala Ala Ile Thr
145 150155 160
Tyr Gly Trp Leu Ile Gly Glu Leu Ile Arg Arg Ala Asp Gly Arg Gly
165 170 175
Pro Gly Asp Ser Ile Val Ala Arg Thr Ala Arg Pro Leu Gly Leu Asp
180 185 190
Phe His Val Gly Leu Ala Asp Asp Glu Phe His Arg Val Ala His Ile
195 200 205
Ala Arg Gly Lys Gly Asn Pro Gly Asp Ala Ala Ala Gln Arg Leu Leu
210 215 220
Gln Val Thr Met Arg Glu Pro Glu Ala Leu Ser Thr Arg Ala Phe Thr
225 230 235 240
Asn Pro Pro Ala Ile Leu Thr Ser Thr Asn Lys Pro Glu Trp Arg Arg
245 250 255
Met Gln Gln Pro Ala Ala Asn Gly His Gly Asn Ala Arg Ser Leu Ala
260 265 270
Gly Phe Tyr Ala Gly Leu Leu Asp Gly Ser Leu Leu Glu Ser Glu Leu
275 280 285
Leu Asp Glu Leu Thr Arg Glu His Ser Leu Gly Gln Asp Arg Thr Leu
290 295 300
Leu Thr Gln Thr Arg Phe Gly Leu Gly Cys Met Leu Asp Gln Pro Glu
305 310 315320
Val Ala Asn Ala Thr Phe Gly Leu Gly Ala Arg Ala Phe Gly His Pro
325 330 335
Gly Ala Gly Gly Ser Val Gly Phe Ala Asp Pro Glu His Asp Val Ala
340 345 350
Phe Gly Phe Val Thr Asn Thr Leu Gly Pro Tyr Val Leu Met Asp Pro
355 360 365
Arg Ala Gln Arg Leu Val Arg Val Leu Gly Ser Cys Leu
370 375 380

Claims (6)

1. The esterase EstP00714 is applied to catalytic resolution of racemic linalyl acetate to obtain (S) -linalool, and the amino acid sequence of the esterase EstP00714 is shown as SEQ ID No. 2.
2. The use according to claim 1, wherein said catalytic resolution of racemic linalyl acetate to (S) -linalool is carried out in the presence of an organic solvent and/or a surfactant.
3. The use according to claim 2, wherein the organic solvent is ethanol.
4. Use according to claim 2 or 3, wherein the surfactant is sodium tripolyphosphate.
5. The use according to claim 4, wherein the reaction system for catalytically resolving racemic linalyl acetate to obtain (S) -linalool is: comprises 20mg/mL esterase EstP00714, 50mM substrate racemic linalyl acetate, 10% volume fraction ethanol and 5g/L sodium tripolyphosphate, and the balance of PBS buffer with the pH of 6.
6. The use according to claim 5, wherein the catalytic resolution of racemic linalyl acetate to give (S) -linalool is carried out at 30 ℃ and for 2 h.
CN201810078725.0A 2018-01-26 2018-01-26 Application of esterase EstP00714 in catalytic resolution of racemic linalyl acetate to obtain (S) -linalool Expired - Fee Related CN108330154B (en)

Priority Applications (1)

Application Number Priority Date Filing Date Title
CN201810078725.0A CN108330154B (en) 2018-01-26 2018-01-26 Application of esterase EstP00714 in catalytic resolution of racemic linalyl acetate to obtain (S) -linalool

Applications Claiming Priority (1)

Application Number Priority Date Filing Date Title
CN201810078725.0A CN108330154B (en) 2018-01-26 2018-01-26 Application of esterase EstP00714 in catalytic resolution of racemic linalyl acetate to obtain (S) -linalool

Publications (2)

Publication Number Publication Date
CN108330154A CN108330154A (en) 2018-07-27
CN108330154B true CN108330154B (en) 2020-08-18

Family

ID=62925939

Family Applications (1)

Application Number Title Priority Date Filing Date
CN201810078725.0A Expired - Fee Related CN108330154B (en) 2018-01-26 2018-01-26 Application of esterase EstP00714 in catalytic resolution of racemic linalyl acetate to obtain (S) -linalool

Country Status (1)

Country Link
CN (1) CN108330154B (en)

Citations (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2003031609A1 (en) * 2001-10-09 2003-04-17 Degussa Ag Esterase esta of rhodococcus sp.
CN106119224A (en) * 2016-07-27 2016-11-16 中国科学院南海海洋研究所 A kind of esterase EstP00714 and encoding gene thereof and application

Patent Citations (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2003031609A1 (en) * 2001-10-09 2003-04-17 Degussa Ag Esterase esta of rhodococcus sp.
CN106119224A (en) * 2016-07-27 2016-11-16 中国科学院南海海洋研究所 A kind of esterase EstP00714 and encoding gene thereof and application

Non-Patent Citations (1)

* Cited by examiner, † Cited by third party
Title
一个新颖南极微生物酯酶EST112-2的功能鉴定和在手性叔醇(S)-芳樟醇制备中的应用（英文）;邓盾等;《有机化学》;20180118;第38卷(第5期);第1187-1192页 *

Also Published As

Publication number Publication date
CN108330154A (en) 2018-07-27

Similar Documents

Publication Publication Date Title
CN111094557A (en) Alcohol dehydrogenase mutant and application thereof in synthesis of diaryl chiral alcohol
CN109628544B (en) Application of lipase in resolution of N-acetyl-DL-methionine methyl ester
US9970043B2 (en) Process for producing optically active 2-alkyl-1,1,3-trialkoxycarbonylpropane
CN105969837B (en) Method for preparing (S) -styrene oxide by enzyme method
CN108330154B (en) Application of esterase EstP00714 in catalytic resolution of racemic linalyl acetate to obtain (S) -linalool
CN109652470B (en) Application of lipase in resolution of (R, S) -methyl mandelate
CN108048317B (en) Continuous synthesis system and continuous synthesis method of unnatural amino acid
US5457051A (en) Enantioselective hydrolysis of ketoprofen esters by beauveria bassiana and enzymes derived therefrom
WO2007026860A1 (en) METHOD FOR PRODUCTION OF OPTICALLY ACTIVE α-HYDROXYCARBOXYLIC ACID
Nakamura et al. Production of (R)-3-chloro-1, 2-propanediol from prochiral 1, 3-dichloro-2-propanol by Corynebacterium sp. strain N-1074
CN106119224B (en) Esterase EstP00714 and coding gene and application thereof
JP5266875B2 (en) Process for producing optically active organic carboxylic acid from organic carboxylic acid ester
JP2010532992A (en) Microbial kinetic resolution of ethyl 3,4-epoxybutyrate
EP0529085A1 (en) Process for producing optically active 3-chloro-1-phenyl-1-propanol and derivative thereof
CN110438194B (en) Application of lipase in preparation of D-tropine methyl ester
Singh et al. Enantioselective transesterification of (RS)-1-chloro-3-(3, 4-difluorophenoxy)-2-propanol using Pseudomonas aeruginosa lipases
CN109943618A (en) A kind of application of recombinant lipase in fractionation (R, S)-α-ethyl -2- oxygen -1- methyl pyrrolidineacetate
EP1433857B1 (en) Process for producing monomer
CN111057736B (en) Application of lipase in splitting BOC-DL-proline methyl ester
CN110257350B (en) Aldehyde ketone reductase BmAKR1, mutant and application thereof
CN103409402A (en) Aldolase mutant
JP2005117905A (en) Method for producing optically active 1-benzyl-3-pyrrolidinol
CN110358804B (en) Enzyme method production process of R-3-amino n-butanol
KR20230010934A (en) Enantioselectivity Improved Candida antarctica Lipase B Variants
AU645543B2 (en) Pharmaceuticals

Legal Events

Date Code Title Description
PB01 Publication
PB01 Publication
SE01 Entry into force of request for substantive examination
SE01 Entry into force of request for substantive examination
CB02 Change of applicant information

Address after: No.1119 Haibin Road, Nansha District, Guangzhou City, Guangdong Province

Applicant after: SOUTH CHINA SEA INSTITUTE OF OCEANOLOGY, CHINESE ACADEMY OF SCIENCES

Address before: 510301 No. 164 West Xingang Road, Guangdong, Guangzhou

Applicant before: SOUTH CHINA SEA INSTITUTE OF OCEANOLOGY, CHINESE ACADEMY OF SCIENCES

CB02 Change of applicant information
GR01 Patent grant
GR01 Patent grant
CF01 Termination of patent right due to non-payment of annual fee

Granted publication date: 20200818

CF01 Termination of patent right due to non-payment of annual fee