CN117070506B - Carbon tube nano catalyst for immobilizing iridium complex and enzyme, preparation method and application thereof - Google Patents
Carbon tube nano catalyst for immobilizing iridium complex and enzyme, preparation method and application thereof Download PDFInfo
- Publication number
- CN117070506B CN117070506B CN202311321687.4A CN202311321687A CN117070506B CN 117070506 B CN117070506 B CN 117070506B CN 202311321687 A CN202311321687 A CN 202311321687A CN 117070506 B CN117070506 B CN 117070506B
- Authority
- CN
- China
- Prior art keywords
- cnt
- iridium complex
- adh
- catalyst
- enzyme
- 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.)
- Active
Links
- 229910052741 iridium Inorganic materials 0.000 title claims abstract description 70
- GKOZUEZYRPOHIO-UHFFFAOYSA-N iridium atom Chemical compound [Ir] GKOZUEZYRPOHIO-UHFFFAOYSA-N 0.000 title claims abstract description 70
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 title claims abstract description 59
- 102000004190 Enzymes Human genes 0.000 title claims abstract description 52
- 108090000790 Enzymes Proteins 0.000 title claims abstract description 52
- 229910052799 carbon Inorganic materials 0.000 title claims abstract description 33
- 239000011943 nanocatalyst Substances 0.000 title claims abstract description 33
- 230000003100 immobilizing effect Effects 0.000 title claims abstract description 14
- 238000002360 preparation method Methods 0.000 title abstract description 11
- WVDDGKGOMKODPV-UHFFFAOYSA-N hydroxymethyl benzene Natural products OCC1=CC=CC=C1 WVDDGKGOMKODPV-UHFFFAOYSA-N 0.000 claims abstract description 132
- 102000007698 Alcohol dehydrogenase Human genes 0.000 claims abstract description 90
- HUMNYLRZRPPJDN-UHFFFAOYSA-N benzenecarboxaldehyde Natural products O=CC1=CC=CC=C1 HUMNYLRZRPPJDN-UHFFFAOYSA-N 0.000 claims abstract description 82
- 239000003054 catalyst Substances 0.000 claims abstract description 58
- QNGNSVIICDLXHT-UHFFFAOYSA-N para-ethylbenzaldehyde Natural products CCC1=CC=C(C=O)C=C1 QNGNSVIICDLXHT-UHFFFAOYSA-N 0.000 claims abstract description 42
- 108010021809 Alcohol dehydrogenase Proteins 0.000 claims abstract description 38
- 239000000463 material Substances 0.000 claims abstract description 30
- -1 glutaraldehyde activated carbon nanotube Chemical class 0.000 claims abstract description 24
- BBEAQIROQSPTKN-UHFFFAOYSA-N pyrene Chemical compound C1=CC=C2C=CC3=CC=CC4=CC=C1C2=C43 BBEAQIROQSPTKN-UHFFFAOYSA-N 0.000 claims abstract description 18
- GVEPBJHOBDJJJI-UHFFFAOYSA-N fluoranthrene Natural products C1=CC(C2=CC=CC=C22)=C3C2=CC=CC3=C1 GVEPBJHOBDJJJI-UHFFFAOYSA-N 0.000 claims abstract description 9
- BDAGIHXWWSANSR-UHFFFAOYSA-M Formate Chemical compound [O-]C=O BDAGIHXWWSANSR-UHFFFAOYSA-M 0.000 claims abstract description 7
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 claims description 24
- 239000002041 carbon nanotube Substances 0.000 claims description 23
- 229910021393 carbon nanotube Inorganic materials 0.000 claims description 23
- 238000006243 chemical reaction Methods 0.000 claims description 21
- 230000035484 reaction time Effects 0.000 claims description 17
- 239000007864 aqueous solution Substances 0.000 claims description 16
- 238000000034 method Methods 0.000 claims description 14
- 239000000243 solution Substances 0.000 claims description 12
- SXRSQZLOMIGNAQ-UHFFFAOYSA-N Glutaraldehyde Chemical compound O=CCCCC=O SXRSQZLOMIGNAQ-UHFFFAOYSA-N 0.000 claims description 8
- 239000012876 carrier material Substances 0.000 claims description 8
- 150000002503 iridium Chemical class 0.000 claims description 8
- 239000008055 phosphate buffer solution Substances 0.000 claims description 8
- ZMXDDKWLCZADIW-UHFFFAOYSA-N N,N-Dimethylformamide Chemical compound CN(C)C=O ZMXDDKWLCZADIW-UHFFFAOYSA-N 0.000 claims description 7
- 238000005406 washing Methods 0.000 claims description 7
- 240000004808 Saccharomyces cerevisiae Species 0.000 claims description 5
- 235000014680 Saccharomyces cerevisiae Nutrition 0.000 claims description 5
- 150000003935 benzaldehydes Chemical class 0.000 claims description 5
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 5
- 238000001035 drying Methods 0.000 claims description 4
- 239000002904 solvent Substances 0.000 claims description 3
- 238000009210 therapy by ultrasound Methods 0.000 claims description 3
- 239000003795 chemical substances by application Substances 0.000 claims description 2
- 238000004140 cleaning Methods 0.000 claims description 2
- 239000003622 immobilized catalyst Substances 0.000 claims 1
- 235000019445 benzyl alcohol Nutrition 0.000 abstract description 43
- 239000005515 coenzyme Substances 0.000 abstract description 17
- 150000004696 coordination complex Chemical class 0.000 abstract description 12
- 230000002779 inactivation Effects 0.000 abstract description 9
- 238000006555 catalytic reaction Methods 0.000 abstract description 7
- 230000002195 synergetic effect Effects 0.000 abstract description 4
- 229930027945 nicotinamide-adenine dinucleotide Natural products 0.000 description 32
- BAWFJGJZGIEFAR-NNYOXOHSSA-N NAD zwitterion Chemical compound NC(=O)C1=CC=C[N+]([C@H]2[C@@H]([C@H](O)[C@@H](COP([O-])(=O)OP(O)(=O)OC[C@@H]3[C@H]([C@@H](O)[C@@H](O3)N3C4=NC=NC(N)=C4N=C3)O)O2)O)=C1 BAWFJGJZGIEFAR-NNYOXOHSSA-N 0.000 description 31
- 229950006238 nadide Drugs 0.000 description 31
- BOPGDPNILDQYTO-NNYOXOHSSA-N nicotinamide-adenine dinucleotide Chemical compound C1=CCC(C(=O)N)=CN1[C@H]1[C@H](O)[C@H](O)[C@@H](COP(O)(=O)OP(O)(=O)OC[C@@H]2[C@H]([C@@H](O)[C@@H](O2)N2C3=NC=NC(N)=C3N=C2)O)O1 BOPGDPNILDQYTO-NNYOXOHSSA-N 0.000 description 31
- 230000003197 catalytic effect Effects 0.000 description 30
- 238000005984 hydrogenation reaction Methods 0.000 description 28
- 238000011069 regeneration method Methods 0.000 description 12
- 230000008929 regeneration Effects 0.000 description 10
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 9
- 230000000694 effects Effects 0.000 description 9
- 229910052751 metal Inorganic materials 0.000 description 9
- 239000002184 metal Substances 0.000 description 9
- HLBBKKJFGFRGMU-UHFFFAOYSA-M sodium formate Chemical compound [Na+].[O-]C=O HLBBKKJFGFRGMU-UHFFFAOYSA-M 0.000 description 7
- 235000019254 sodium formate Nutrition 0.000 description 7
- 239000004280 Sodium formate Substances 0.000 description 5
- 238000009903 catalytic hydrogenation reaction Methods 0.000 description 5
- IBBMAWULFFBRKK-UHFFFAOYSA-N picolinamide Chemical compound NC(=O)C1=CC=CC=N1 IBBMAWULFFBRKK-UHFFFAOYSA-N 0.000 description 5
- 125000001725 pyrenyl group Chemical group 0.000 description 5
- IKHGUXGNUITLKF-UHFFFAOYSA-N Acetaldehyde Chemical compound CC=O IKHGUXGNUITLKF-UHFFFAOYSA-N 0.000 description 4
- 238000004128 high performance liquid chromatography Methods 0.000 description 4
- 230000007246 mechanism Effects 0.000 description 4
- 230000004048 modification Effects 0.000 description 4
- 238000012986 modification Methods 0.000 description 4
- 238000011160 research Methods 0.000 description 4
- UJPKMTDFFUTLGM-UHFFFAOYSA-N 1-aminoethanol Chemical compound CC(N)O UJPKMTDFFUTLGM-UHFFFAOYSA-N 0.000 description 3
- 238000004833 X-ray photoelectron spectroscopy Methods 0.000 description 3
- 238000002835 absorbance Methods 0.000 description 3
- 230000008878 coupling Effects 0.000 description 3
- 238000010168 coupling process Methods 0.000 description 3
- 238000005859 coupling reaction Methods 0.000 description 3
- 238000010586 diagram Methods 0.000 description 3
- 230000002255 enzymatic effect Effects 0.000 description 3
- 238000004519 manufacturing process Methods 0.000 description 3
- 230000008569 process Effects 0.000 description 3
- 238000004064 recycling Methods 0.000 description 3
- 238000001179 sorption measurement Methods 0.000 description 3
- 241000894007 species Species 0.000 description 3
- 238000001228 spectrum Methods 0.000 description 3
- KWOLFJPFCHCOCG-UHFFFAOYSA-N Acetophenone Chemical compound CC(=O)C1=CC=CC=C1 KWOLFJPFCHCOCG-UHFFFAOYSA-N 0.000 description 2
- CURLTUGMZLYLDI-UHFFFAOYSA-N Carbon dioxide Chemical compound O=C=O CURLTUGMZLYLDI-UHFFFAOYSA-N 0.000 description 2
- 101710088194 Dehydrogenase Proteins 0.000 description 2
- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 description 2
- 150000001408 amides Chemical class 0.000 description 2
- 238000012512 characterization method Methods 0.000 description 2
- 239000012295 chemical reaction liquid Substances 0.000 description 2
- 238000009833 condensation Methods 0.000 description 2
- 230000005494 condensation Effects 0.000 description 2
- 230000009849 deactivation Effects 0.000 description 2
- 238000006356 dehydrogenation reaction Methods 0.000 description 2
- 239000008367 deionised water Substances 0.000 description 2
- 229910021641 deionized water Inorganic materials 0.000 description 2
- 238000006911 enzymatic reaction Methods 0.000 description 2
- 239000001257 hydrogen Substances 0.000 description 2
- 229910052739 hydrogen Inorganic materials 0.000 description 2
- 239000000203 mixture Substances 0.000 description 2
- 239000002086 nanomaterial Substances 0.000 description 2
- 125000002524 organometallic group Chemical group 0.000 description 2
- WVDDGKGOMKODPV-ZQBYOMGUSA-N phenyl(114C)methanol Chemical compound O[14CH2]C1=CC=CC=C1 WVDDGKGOMKODPV-ZQBYOMGUSA-N 0.000 description 2
- 238000011084 recovery Methods 0.000 description 2
- 238000004626 scanning electron microscopy Methods 0.000 description 2
- 238000012360 testing method Methods 0.000 description 2
- 238000001291 vacuum drying Methods 0.000 description 2
- 238000005303 weighing Methods 0.000 description 2
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 1
- 108010050375 Glucose 1-Dehydrogenase Proteins 0.000 description 1
- UFHFLCQGNIYNRP-UHFFFAOYSA-N Hydrogen Chemical compound [H][H] UFHFLCQGNIYNRP-UHFFFAOYSA-N 0.000 description 1
- 239000004201 L-cysteine Substances 0.000 description 1
- 235000013878 L-cysteine Nutrition 0.000 description 1
- 238000000026 X-ray photoelectron spectrum Methods 0.000 description 1
- 238000000862 absorption spectrum Methods 0.000 description 1
- 230000004913 activation Effects 0.000 description 1
- 150000001299 aldehydes Chemical group 0.000 description 1
- 125000003277 amino group Chemical group 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
- 230000008901 benefit Effects 0.000 description 1
- 150000001721 carbon Chemical class 0.000 description 1
- 239000001569 carbon dioxide Substances 0.000 description 1
- 229910002092 carbon dioxide Inorganic materials 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 238000006482 condensation reaction Methods 0.000 description 1
- 125000004122 cyclic group Chemical group 0.000 description 1
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 1
- 235000018417 cysteine Nutrition 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 239000008103 glucose Substances 0.000 description 1
- 229960002989 glutamic acid Drugs 0.000 description 1
- 239000002638 heterogeneous catalyst Substances 0.000 description 1
- 239000002815 homogeneous catalyst Substances 0.000 description 1
- 150000002431 hydrogen Chemical class 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- 238000000338 in vitro Methods 0.000 description 1
- 238000001727 in vivo Methods 0.000 description 1
- 230000000415 inactivating effect Effects 0.000 description 1
- 230000003993 interaction Effects 0.000 description 1
- 238000011835 investigation Methods 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 239000011259 mixed solution Substances 0.000 description 1
- 229910052757 nitrogen Inorganic materials 0.000 description 1
- 125000004433 nitrogen atom Chemical group N* 0.000 description 1
- UYWQUFXKFGHYNT-UHFFFAOYSA-N phenylmethyl ester of formic acid Natural products O=COCC1=CC=CC=C1 UYWQUFXKFGHYNT-UHFFFAOYSA-N 0.000 description 1
- 239000008363 phosphate buffer Substances 0.000 description 1
- 230000001699 photocatalysis Effects 0.000 description 1
- 230000004962 physiological condition Effects 0.000 description 1
- 125000005575 polycyclic aromatic hydrocarbon group Chemical group 0.000 description 1
- 238000006116 polymerization reaction Methods 0.000 description 1
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
- 125000005581 pyrene group Chemical group 0.000 description 1
- 150000003283 rhodium Chemical class 0.000 description 1
- 229910052703 rhodium Inorganic materials 0.000 description 1
- 239000010948 rhodium Substances 0.000 description 1
- MHOVAHRLVXNVSD-UHFFFAOYSA-N rhodium atom Chemical compound [Rh] MHOVAHRLVXNVSD-UHFFFAOYSA-N 0.000 description 1
- 150000003303 ruthenium Chemical class 0.000 description 1
- 239000012266 salt solution Substances 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 238000012546 transfer Methods 0.000 description 1
- 230000003313 weakening effect Effects 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N11/00—Carrier-bound or immobilised enzymes; Carrier-bound or immobilised microbial cells; Preparation thereof
- C12N11/14—Enzymes or microbial cells immobilised on or in an inorganic carrier
-
- B—PERFORMING OPERATIONS; TRANSPORTING
- B01—PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
- B01J—CHEMICAL OR PHYSICAL PROCESSES, e.g. CATALYSIS OR COLLOID CHEMISTRY; THEIR RELEVANT APPARATUS
- B01J31/00—Catalysts comprising hydrides, coordination complexes or organic compounds
- B01J31/16—Catalysts comprising hydrides, coordination complexes or organic compounds containing coordination complexes
- B01J31/1616—Coordination complexes, e.g. organometallic complexes, immobilised on an inorganic support, e.g. ship-in-a-bottle type catalysts
- B01J31/1625—Coordination complexes, e.g. organometallic complexes, immobilised on an inorganic support, e.g. ship-in-a-bottle type catalysts immobilised by covalent linkages, i.e. pendant complexes with optional linking groups
-
- B—PERFORMING OPERATIONS; TRANSPORTING
- B01—PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
- B01J—CHEMICAL OR PHYSICAL PROCESSES, e.g. CATALYSIS OR COLLOID CHEMISTRY; THEIR RELEVANT APPARATUS
- B01J31/00—Catalysts comprising hydrides, coordination complexes or organic compounds
- B01J31/16—Catalysts comprising hydrides, coordination complexes or organic compounds containing coordination complexes
- B01J31/18—Catalysts comprising hydrides, coordination complexes or organic compounds containing coordination complexes containing nitrogen, phosphorus, arsenic or antimony as complexing atoms, e.g. in pyridine ligands, or in resonance therewith, e.g. in isocyanide ligands C=N-R or as complexed central atoms
- B01J31/1805—Catalysts comprising hydrides, coordination complexes or organic compounds containing coordination complexes containing nitrogen, phosphorus, arsenic or antimony as complexing atoms, e.g. in pyridine ligands, or in resonance therewith, e.g. in isocyanide ligands C=N-R or as complexed central atoms the ligands containing nitrogen
- B01J31/181—Cyclic ligands, including e.g. non-condensed polycyclic ligands, comprising at least one complexing nitrogen atom as ring member, e.g. pyridine
- B01J31/1815—Cyclic ligands, including e.g. non-condensed polycyclic ligands, comprising at least one complexing nitrogen atom as ring member, e.g. pyridine with more than one complexing nitrogen atom, e.g. bipyridyl, 2-aminopyridine
-
- B—PERFORMING OPERATIONS; TRANSPORTING
- B01—PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
- B01J—CHEMICAL OR PHYSICAL PROCESSES, e.g. CATALYSIS OR COLLOID CHEMISTRY; THEIR RELEVANT APPARATUS
- B01J31/00—Catalysts comprising hydrides, coordination complexes or organic compounds
- B01J31/16—Catalysts comprising hydrides, coordination complexes or organic compounds containing coordination complexes
- B01J31/22—Organic complexes
- B01J31/2282—Unsaturated compounds used as ligands
- B01J31/2295—Cyclic compounds, e.g. cyclopentadienyls
-
- B—PERFORMING OPERATIONS; TRANSPORTING
- B01—PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
- B01J—CHEMICAL OR PHYSICAL PROCESSES, e.g. CATALYSIS OR COLLOID CHEMISTRY; THEIR RELEVANT APPARATUS
- B01J31/00—Catalysts comprising hydrides, coordination complexes or organic compounds
- B01J31/40—Regeneration or reactivation
- B01J31/4015—Regeneration or reactivation of catalysts containing metals
- B01J31/4023—Regeneration or reactivation of catalysts containing metals containing iron group metals, noble metals or copper
- B01J31/4038—Regeneration or reactivation of catalysts containing metals containing iron group metals, noble metals or copper containing noble metals
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/0004—Oxidoreductases (1.)
- C12N9/0006—Oxidoreductases (1.) acting on CH-OH groups as donors (1.1)
-
- 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
- C12P7/22—Preparation of oxygen-containing organic compounds containing a hydroxy group aromatic
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y101/00—Oxidoreductases acting on the CH-OH group of donors (1.1)
- C12Y101/01—Oxidoreductases acting on the CH-OH group of donors (1.1) with NAD+ or NADP+ as acceptor (1.1.1)
- C12Y101/01001—Alcohol dehydrogenase (1.1.1.1)
-
- B—PERFORMING OPERATIONS; TRANSPORTING
- B01—PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
- B01J—CHEMICAL OR PHYSICAL PROCESSES, e.g. CATALYSIS OR COLLOID CHEMISTRY; THEIR RELEVANT APPARATUS
- B01J2531/00—Additional information regarding catalytic systems classified in B01J31/00
- B01J2531/80—Complexes comprising metals of Group VIII as the central metal
- B01J2531/82—Metals of the platinum group
- B01J2531/827—Iridium
Landscapes
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Engineering & Computer Science (AREA)
- Life Sciences & Earth Sciences (AREA)
- Wood Science & Technology (AREA)
- Health & Medical Sciences (AREA)
- Zoology (AREA)
- Genetics & Genomics (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Inorganic Chemistry (AREA)
- Materials Engineering (AREA)
- Biochemistry (AREA)
- General Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Microbiology (AREA)
- Biotechnology (AREA)
- Biomedical Technology (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- General Chemical & Material Sciences (AREA)
- Catalysts (AREA)
Abstract
The invention discloses a carbon tube nano catalyst for immobilizing iridium complex and enzyme, a preparation method and application thereof. Relates to the technical field of organic metal complex and biological enzyme synergistic catalysis. It comprises glutaraldehyde activated carbon nanotube material CHO-CNT; also comprises alcohol dehydrogenase ADH and pyrene functionalized iridium complex which are respectively fixed on the surface of glutaraldehyde activated carbon nanotube material CHO-CNT. The catalyst can effectively solve the problem of mutual inactivation between the iridium complex and the alcohol dehydrogenase; the prepared catalyst is prepared by formate and oxidized coenzyme NAD + In the presence of the catalyst, the benzaldehyde compound can be efficiently catalyzed to be hydrogenated to generate the corresponding benzyl alcohol compound.
Description
Technical Field
The invention relates to the technical field of collaborative catalysis of organometallic complexes and biological enzymes, in particular to a carbon tube nano-catalyst for immobilizing iridium complexes and enzymes. The invention also relates to a preparation method and an application method of the carbon tube nano-catalyst for immobilizing the iridium complex and the enzyme.
Background
Due to the great biological significance and high production cost, the efficient recycling of the reduced nicotinamide adenine dinucleotide NADH has been a research hot spot in the bioconversion process. In direct enzymatic hydrogenation reactions, stoichiometric amounts of NADH are required to provide the necessary hydrogen source, resulting in excessive production costs that prevent the use of enzymatic hydrogenation reactions. In an in vivo environment, however, continuous cyclic regeneration of NADH can be achieved by a multi-enzyme cascade, e.g., glucose dehydrogenase can continuously produce NADH by consuming large amounts of glucose. In an in vitro environment, the regeneration method of NADH mainly comprises chemical regeneration, homogeneous catalytic regeneration, electrochemical regeneration, photocatalytic regeneration and heterogeneous catalytic regeneration. However, these regeneration methods are still inefficient compared to enzyme regeneration, which is still the method of choice for most applications. In these non-enzymatic processes, NADH regeneration studies based on homogeneous metal complex catalysts have achieved satisfactory results in recent years, providing a powerful guarantee for the co-catalysis of metal catalysts with enzymes.
Currently, homogeneous metal complex catalysts for NADH regeneration mainly include ruthenium complexes, rhodium complexes, iridium complexes, and the like. The rhodium and iridium complex has higher stability, catalytic efficiency and stereoselectivity for NADH regeneration. The metal complex-enzyme co-catalytic system constructed by combining the homogeneous metal complex and various biological enzymes has been successfully applied to the aspects of acetophenone chiral hydrogenation, L-glutamic acid preparation and the like. However, although the metal complex-enzyme co-catalytic system has good application potential, the problems of high cost, poor recovery performance and mutual inactivation between the organometallic complex and the enzyme in the catalytic system are not solved in the prior researches. The homogeneous metal complex catalyst and the corresponding biological enzyme are fixed on the surface of the carrier material, so that the enzyme and the metal complex of the homogeneous system are converted into heterogeneous catalyst, and the problems of high cost and poor recoverability of the catalytic system can be solved. The mutual inactivation problem of the metal complex and the enzyme is mainly caused by complete coordination of the metal organic complex and the active site of the enzyme and the wrapping effect of the supermolecular enzyme protein on the small molecular metal complex. At present, effective means for solving the problem of mutual inactivation between a metal complex and an enzyme in a metal complex-enzyme co-catalytic system are still lacking.
Disclosure of Invention
The invention aims to solve the technical problems of high cost, poor recovery performance and mutual inactivation between an organic metal complex and an enzyme in a metal complex-enzyme co-catalytic system.
The technical scheme of the invention is as follows:
the carbon tube nano catalyst for immobilizing iridium complex and enzyme comprises glutaraldehyde activated carbon nano tube material CHO-CNT; the iridium complex is characterized by further comprising alcohol dehydrogenase ADH and pyrene functionalized iridium complexes which are respectively fixed on the surface of the glutaraldehyde activated carbon nanotube material CHO-CNT;
the structural formula of the carbon nanotube material CHO-CNT is as follows:
；
the pyrene functionalized iridium complex has the following structural formula:
。
the alcohol dehydrogenase ADH is preferably an alcohol dehydrogenase from Saccharomyces cerevisiae.
The preparation method of the carbon tube nano catalyst for immobilizing iridium complex and enzyme comprises the following steps:
step (1): adding an amino-functionalized carbon nanotube carrier material into glutaraldehyde aqueous solution, oscillating and incubating, centrifuging to remove excessive glutaraldehyde, cleaning, and then redispersing into the aqueous solution to obtain glutaraldehyde-activated carbon nanotube material aqueous solution;
step (2): dissolving a pyrene functionalized iridium complex in an N, N dimethylformamide solvent, adding the solution into the glutaraldehyde activated carbon nanotube material aqueous solution prepared in the step (1), performing ultrasonic treatment, centrifuging, washing with ethanol, and drying to obtain an iridium complex loaded carbon nanotube material Ir@CNT;
step (3): adding the iridium complex loaded carbon nanotube material Ir@CNT prepared in the step (2) into a phosphate buffer solution, then adding alcohol dehydrogenase ADH, centrifuging, washing with water and drying after the oscillating reaction is finished, thus obtaining the iridium complex and enzyme immobilized carbon nanotube nano catalyst Ir@CNT@ADH.
According to the application method of the carbon tube nano catalyst for immobilizing the iridium complex and the enzyme, under the condition that formate and benzaldehyde coexist, the catalyst is used for catalyzing benzaldehyde compounds to be converted into corresponding benzyl alcohol compounds.
In the application method of the carbon tube nano catalyst for immobilizing iridium complex and enzyme, the preferable reaction conditions are as follows: the reaction time is 24 hours, the reaction pH is 6.5, and the reaction system NAD + The concentration was 0.5 mM,Ir@CNT@ADH at 1.0 mg/mL.
The invention has the beneficial effects that:
the catalyst obtained by the method has the following technical advantages: the iridium complex has high catalytic hydrogenation efficiency and can efficiently catalyze and oxidize coenzyme NAD + Hydroconversion to reduced coenzyme NADH; the combined catalysis between the iridium complex catalyst and the alcohol dehydrogenase can be effectively utilized to catalyze the conversion of benzaldehyde compounds into corresponding benzyl alcohol compounds; effectively improves the recoverability of the iridium complex catalyst and the ethanol dehydrogenase.
Second, studies have found that NAD immobilized on the electrode surface + The molecule can effectively prevent two NADs + Redox sites caused by electrochemical polymerization between the two. Based on this, the present invention adopts amino-functionalized carbon nanotubes (NH 2 -CNT) as carrier material, and fixing pyrene functionalized metallic iridium complex and biological enzyme on NH respectively by two different mild coupling modes of pi-pi adsorption and aldehyde-ammonia condensation reaction after glutaraldehyde activation 2 The CNT surface is prepared into a carbon tube nano catalyst immobilized with iridium complex and enzyme, which successfully solves the problem of recoverability of two high-valence homogeneous catalysts and greatly weakens the problem of mutual inactivation of metal complex and enzyme, and the catalyst of the invention is in aqueous solutionHas better dispersibility and stability, and contributes to wider application of a metal complex-enzyme co-catalytic system in the future.
Thirdly, the carbon tube nano catalyst for immobilizing the iridium complex and the enzyme provided by the invention can realize recycling of the catalyst through simple centrifugal separation, and can effectively solve the problem that the iridium complex and the alcohol dehydrogenase are mutually inactivated in a homogeneous system.
Fourth, the iridium complex and enzyme immobilized carbon tube nano-catalyst provided by the invention can efficiently catalyze and oxidize coenzyme NAD in the presence of formate + Hydroconversion to reduced coenzyme NADH; under the condition of the coexistence of formate and benzaldehyde, the method can efficiently catalyze the conversion of benzaldehyde compounds into corresponding benzyl alcohol compounds.
Drawings
FIG. 1 is a schematic diagram of the structure of a carbon tube nanocatalyst Ir@CNT@ADH of the iridium complex and enzyme immobilized in the invention;
FIG. 2 is a schematic diagram of the preparation steps of the iridium complex and enzyme immobilized carbon tube nanocatalyst Ir@CNT@ADH of the invention;
FIG. 3 is a schematic representation of the structural characterization of a scanning electron microscope A) and X-ray photoelectron spectroscopy B), C) and D) of a carbon tube nano-catalyst Ir@CNT@ADH of the iridium complex and enzyme immobilized in the invention;
FIG. 4 is a schematic representation of the ultraviolet-visible absorption spectrum analysis structure of the iridium complex and enzyme immobilized carbon tube nanocatalyst Ir@CNT@ADH of the invention;
FIG. 5 is a schematic diagram of a catalytic mechanism for preparing benzyl alcohol by catalyzing benzaldehyde hydrogenation by using a carbon tube nano catalyst Ir@CNT@ADH of the immobilized iridium complex and enzyme;
FIG. 6 is an optimized graph of conditions for preparing benzyl alcohol by catalyzing benzaldehyde hydrogenation with Ir@CNT@ADH, which is a carbon tube nano catalyst for immobilizing iridium complex and enzyme. Wherein A) is the yield comparison of the catalyst Ir@CNT@ADH and Ir@CNT@benzaldehyde hydrogenation to prepare benzyl alcohol under the condition of different reaction time; b) Is oxidized nicotinamide adenine dinucleotide NAD + The concentration of (2) has an influence on the yield of benzyl alcohol prepared by catalyzing benzaldehyde hydrogenation by Ir@CNT@ADH; c) Is of different pHUnder the condition, the yield of benzyl alcohol prepared by catalyzing benzaldehyde hydrogenation by using a catalyst Ir@CNT@ADH is compared; d) The yield of benzyl alcohol prepared by catalyzing benzaldehyde hydrogenation with the catalyst Ir@CNT@ADH is compared with the catalyst Ir@CNT@ADH at different dosage.
Detailed Description
The invention is described in detail below with reference to the drawings and the specific embodiments.
Example one composition example of the iridium complex and enzyme immobilized carbon tube nanocatalyst Ir@CNT@ADH of the invention.
The invention provides a carbon tube nano catalyst structure for immobilizing iridium complex and enzyme, which mainly comprises three parts of glutaraldehyde activated carbon nano tube material (CHO-CNT), iridium complex and Alcohol Dehydrogenase (ADH). Wherein glutaraldehyde-activated carbon nanotube material (CHO-CNT) has an outer diameter of 8.0-15.0 nm and a length of about 50.0 μm; the iridium complex is pyrenyl functionalized pyridine amide iridium complex; the Alcohol Dehydrogenase (ADH) is an alcohol dehydrogenase derived from Saccharomyces cerevisiae. Iridium complex and Alcohol Dehydrogenase (ADH) are respectively fixed on the surface of glutaraldehyde activated carbon nanotube material (CHO-CNT) through two different mild coupling modes of pi-pi adsorption and aldehyde-ammonia condensation, and the specific structure is shown in figure 1.
The glutaraldehyde-activated carbon nanotube material (CHO-CNT) has the structural formula:
。
the pyrenyl functionalized pyridine amide iridium complex has the following structural formula:
。
the Alcohol Dehydrogenase (ADH) is preferably derived from Saccharomyces cerevisiae.
Further, the pyrenyl functionalized pyridine amide iridium complex realizes the firm modification of the pyrenyl functionalized pyridine amide iridium complex on the surface of the glutaraldehyde activated carbon nanotube material through the firm pi-pi conjugated electron interaction between a pyrene functional group in the structure and the polycyclic aromatic hydrocarbon structure of the glutaraldehyde activated carbon nanotube material; the alcohol dehydrogenase reacts with aldehyde functional groups in glutaraldehyde activated carbon nano tube materials through the amino terminal to form stable imine bonds, so that stable modification of the alcohol dehydrogenase on the surface of the carbon nano tube is realized.
Example two, preparation example of carbon tube nanocatalyst Ir@CNT@ADH supporting iridium complex and enzyme.
In the preparation method, pyrenyl functionalized pyridine amide iridium complex (Ir) and Alcohol Dehydrogenase (ADH) are respectively fixed on the surface of glutaraldehyde activated carbon nanotube material (CHO-CNT) through two different mild coupling modes of pi-pi adsorption and aldehyde-ammonia condensation. As shown in fig. 2, the preparation method of the carbon tube nano catalyst Ir@CNT@ADH of the iridium complex and enzyme immobilized according to the invention comprises the following steps:
step 1. Weighing the amino-functionalized carbon nanotube carrier material (NH) 2 -CNT) 100.0. 100.0 mg into a glutaraldehyde aqueous solution with a mass concentration of 20.0% of 10.0 mL, incubating the reaction solution at 25 ℃ for 10.0 hours with shaking, centrifuging to remove excess glutaraldehyde, washing with deionized water three times, and redispersing into a deionized water solution of 10.0. 10.0 mL to obtain a glutaraldehyde-activated carbon nanotube material (CHO-CNT) aqueous solution;
step 2, weighing pyrene functionalized iridium complex 1.0 mg, dissolving in 2.0 mLN, N dimethylformamide solvent, adding into prepared glutaraldehyde activated carbon nanomaterial (CHO-CNT) aqueous solution, carrying out ultrasonic treatment for 5-60 minutes, centrifuging, washing with ethanol for 3-5 times, and carrying out vacuum drying to obtain iridium complex loaded carbon nanomaterial Ir@CNTs 90.0 mg;
step 3. The above-mentioned dried iridium complex-supported carbon nanotube material Ir@CNTs 50.0. 50.0 mg was weighed and added to a 2.0. 2.0 mL phosphate buffer solution (0.1M, pH=7.4), followed by adding 0.5. 0.5 mg Alcohol Dehydrogenase (ADH), and the mixture was reacted at 25℃for 5.0 hours with shaking. After the reaction is finished, the mixed solution is subjected to centrifugation, water washing and vacuum drying to obtain the carbon tube nano catalyst Ir@CNT@ADH 45.0 mg for immobilizing the iridium complex and the enzyme.
The structure characterization of the prepared iridium complex and enzyme immobilized carbon tube nano catalyst Ir@CNT@ADH.
The invention adopts Scanning Electron Microscopy (SEM) and X-ray photoelectron spectroscopy (XPS) to characterize the prepared catalyst Ir@CNT@ADH. As shown in fig. 3 a), it can be observed from the SEM spectrum of the catalyst ir@cnt@adh that the catalyst ir@cnt@adh maintained the tubular morphology of the carbon nanotube material with a diameter of about 10 nm. This observation shows that ir@cnt@adh retains the structure of the carbon nanotubes, ensuring a high surface area for efficient catalytic activity. The XPS spectrum Ir 4f nuclear energy level of the catalyst Ir@CNT@ADH shows Ir 4f at 62.7 eV and 65.7 eV, respectively 7/2 And Ir 4f 5/2 Two characteristic peaks (B in fig. 3)); and Ir 4f 7/2 And Ir 4f 5/2 The peak area ratio of (2) is about 4:3, and the energy difference between the two peaks is calculated to be 3.0 eV, which is consistent with the energy level spectrum of the standard Ir 4f core. As shown in fig. 3C), significant Cl 2p was observed at 198.4 eV and 200.2 eV 3/2 Peaks, which may be due to metal-bound Cl species (Ir-Cl), indicate successful modification of iridium complexes at the carbon nanotube material surface; the N1s nuclear energy spectrum of ir@cnt@adh shows two distinct nitrogen atom characteristic peaks 397.8 eV and 399.5 eV, belonging to the metal binding N species and the amide N species (D in fig. 3), respectively, and at 397.8 eV and 399.5 eV the area ratio of the peaks is about 1:34, indicating the presence of a large number of amino groups on the carbon nanotube surface. These results confirm that iridium complexes are successfully modified on the surface of carbon nanotubes.
To further characterize the modification of the alcohol dehydrogenase on the surface of the catalyst Ir@CNT@ADH, the catalyst contains NAD + And ethanol in PBS solution with ir@cnt or ir@cnt@adh as catalysts, the catalytic activity of ir@cnt@adh surface ADH in the presence and absence of the iridium complex inactivating agent cysteine Cys was examined, respectively (fig. 4). When ir@cnt was used as catalyst, almost no NADH signal was observed at 340 nm, indicating that ir@cnt was not catalytically active for alcohol dehydrogenation. Whereas with Ir@CNT@ADH as catalyst, a significant NADH characteristic UV-visible absorbance peak was detected at 340 nm, at a value of 0.12. This result demonstrates that ADH was successfully modified at the surface of carbon nanotubes. In addition, when L-cysteine (Cys) is present in the Ir@CNT@ADH reaction solutionAt this time, the absorbance value of NADH increased to 0.16. The increase in absorbance value may be due to the inactivation of the iridium complex on the surface of Ir@CNT@ADH by Cys. In the absence of Cys, ADH acts as a catalyst for the dehydrogenation of ethanol, producing acetaldehyde and equimolar amounts of NADH. At the same time, ir@CNT@ADH surface modified iridium complex promotes hydrogen transfer from NADH to acetaldehyde and converts NAD again + And ethanol. This results in a decrease in NADH concentration in the solution. However, in the presence of Cys, due to the inactivation of Ir@CNT@ADH surface modified iridium complex by Cys, the generated NADH does not participate in the catalytic cycle initiated by the iridium complex, and a higher concentration of NADH can be maintained in the catalytic solution. The results showed that the alcohol dehydrogenase ADH was successfully modified on the surface of the carbon nanotubes.
Example three, example of benzyl alcohol preparation by catalytic benzaldehyde hydrogenation with the prepared iridium complex and enzyme-immobilized carbon tube nanocatalyst Ir@CNT@ADH.
Catalytic mechanism: the catalytic mechanism of preparing benzyl alcohol by catalyzing benzaldehyde hydrogenation by using the iridium complex and enzyme-immobilized carbon tube nano catalyst Ir@CNT@ADH provided by the invention is shown in figure 5, and the catalytic amount of NAD is shown in the catalytic amount + And sufficient formate to catalyze the oxidized coenzyme NAD with high efficiency + The reduced coenzyme NADH is converted, and a slow catalytic part of benzaldehyde is directly hydrogenated to generate corresponding benzyl alcohol, and formate ions in the reaction liquid are oxidized into carbon dioxide in the process; then, the generated reduced coenzyme NADH is combined with alcohol dehydrogenase ADH on the surface of a catalyst Ir@CNT@ADH to form a high-efficiency enzyme catalytic system, which can efficiently catalyze the hydrogenation of benzaldehyde in solution to benzyl alcohol, and at the same time, the reduced coenzyme NADH is oxidized to oxidized coenzyme NAD + The method comprises the steps of carrying out a first treatment on the surface of the Thus, in the catalytic system, benzaldehyde is continuously converted into benzyl alcohol as a target product.
And (3) optimizing the catalytic conditions: taking benzaldehyde hydrogenation to prepare benzyl alcohol as an example, the invention examines the use condition of the catalyst Ir@CNT@ADH. It is known that alcohol dehydrogenase ADH is capable of rapidly reducing benzaldehyde to benzyl alcohol in the presence of reduced coenzyme NADH, while at the same timeThe original coenzyme NADH will be oxidized to oxidized coenzyme NAD + The method comprises the steps of carrying out a first treatment on the surface of the In addition, in the presence of sufficient formate ion HCOO - In the presence of the pyridine nicotinamide iridium complex, the pyridine nicotinamide iridium complex can rapidly convert the oxidized coenzyme NAD + Reduced to reduced coenzyme NADH, the NADH produced will participate in the enzymatic reaction, and thus, benzaldehyde will be continuously converted into benzyl alcohol.
In order to determine the optimal reaction conditions, the invention respectively examines the reaction time and NAD + Influence of concentration, pH and Ir@CNT@ADH concentration on the yield of benzyl alcohol prepared by catalyzing benzaldehyde hydrogenation by a catalyst.
Influence of reaction time on the yield of benzyl alcohol prepared by catalyzing benzaldehyde hydrogenation by using Ir@CNT@ADH as catalyst: 1.0 mg catalyst Ir@CNT@ADH was weighed into a 2.0 mL centrifuge tube, followed by the sequential addition of 3.0 mg benzaldehyde, 10. Mu.L of NAD at a concentration of 100 mmoles per liter + An aqueous solution, sodium formate 6.8 mg, phosphate buffer solution 1.0 mL at a concentration of 0.2 moles per liter and a pH equal to 6.5; the centrifuge tube containing the reaction solution was then transferred to a shaker reactor and reacted at 37℃to test the benzyl alcohol yields by high performance liquid chromatography for 1 hour, 2 hours, 5 hours, 24 hours and 48 hours, respectively, as shown in Table 1.
TABLE 1 productivity of benzyl alcohol from benzaldehyde hydrogenation catalyzed by Ir@CNT@ADH with different reaction time catalysts
Influence of reaction time on the yield of benzyl alcohol prepared by hydrogenation of benzaldehyde catalyzed by Ir@CNT catalyst: 1.0 mg catalyst Ir@CNT was weighed into a 2.0 mL centrifuge tube, followed by the sequential addition of 3.0 mg benzaldehyde, 10. Mu.l of NAD at a concentration of 100 mmoles per liter + An aqueous solution, sodium formate 6.8 mg, phosphate buffer solution 1.0 mL at a concentration of 0.2 moles per liter and a pH equal to 6.5; then transferring the centrifuge tube filled with the reaction liquid into a shaking table reactor for reaction at 37 ℃, and respectively testing the reaction time of 1 hour by a high performance liquid chromatograph,After 2 hours, 5 hours, 24 hours and 48 hours, the yields of benzyl alcohol are shown in Table 2.
TABLE 2 productivity of benzyl alcohol from the hydrogenation of benzaldehyde catalyzed by Ir@CNT catalysts with different reaction times
NAD + Effect of concentration on the yield of benzyl alcohol prepared by catalytic hydrogenation of benzaldehyde under the catalyst Ir@CNT@ADH 1.0 mg catalyst Ir@CNT@ADH was weighed into a 2.0 mL centrifuge tube, followed by sequential addition of 3.0 mg benzaldehyde, 10. Mu.l of NAD of different concentrations + Aqueous solution (10 mmol per liter, 50 mmol per liter, 100 mmol per liter, 300 mmol per liter and 500 mmol per liter), sodium formate 6.8 mg, phosphate buffer solution with a concentration of 1.0 mL of 0.2 mol per liter and a pH of 6.5; the centrifuge tube containing the reaction solution was then transferred to a shaker reactor and reacted at 37℃for 24 hours, and the benzyl alcohol yield was measured by high performance liquid chromatography, and the specific yields are shown in Table 3.
TABLE 3 NAD concentrations + In the presence of a catalyst Ir@CNT@ADH, catalyzing benzaldehyde to prepare benzyl alcohol through hydrogenation, and obtaining the yield of benzyl alcohol
Effect of pH on catalyst ir@cnt@adh catalytic benzaldehyde hydrogenation to benzyl alcohol yield:
1.0 mg catalyst Ir@CNT@ADH was weighed into a 2.0 mL centrifuge tube, followed by the sequential addition of 3.0 mg benzaldehyde, 10. Mu.L of NAD at a concentration of 100 mmoles per liter + Aqueous solution, 6.8 mg sodium formate, 1.0 mL concentration 0.2 moles per liter phosphate buffer solution at pH 6.0, 6.5, 7.0, 7.5 and 8.0, respectively; the centrifuge tube containing the reaction solution was then transferred to a shaker reactor and reacted at 37℃for 24 hours, and the benzyl alcohol yield was measured by high performance liquid chromatography, and the specific yields are shown in Table 4.
TABLE 4 productivity of benzyl alcohol from the hydrogenation of benzaldehyde catalyzed by Ir@CNT@ADH catalyst under different pH conditions
Effect of ir@cnt@adh concentration on the yield of benzyl alcohol prepared by catalytic hydrogenation of benzaldehyde under the catalysis of catalyst ir@cnt@adh was weighed out to give catalysts ir@cnt@adh having mass of 0.1 mg, 0.5 mg, 0.8 mg, 1.0 mg, 2.0 mg and 5.0 mg respectively, and added to different 2.0 mL centrifuge tubes respectively, followed by sequential addition of 3.0 mg benzaldehyde, 10 μl of NAD having a concentration of 100 millimoles per liter + An aqueous solution, sodium formate 6.8 mg, phosphate buffer solution 1.0 mL at a concentration of 0.2 moles per liter and a pH equal to 6.5; the centrifuge tube containing the reaction solution was then transferred to a shaker reactor and reacted at 37℃for 24 hours, and the benzyl alcohol yield was measured by high performance liquid chromatography, and the specific yields are shown in Table 5.
TABLE 5 productivity of benzyl alcohol from the hydrogenation of benzaldehyde catalyzed by Ir@CNT@ADH with different concentrations of catalyst
Based on the above experimental data, the catalytic activity of the catalysts ir@cnt and ir@cnt@adh for the hydrogenation of benzaldehyde at different reaction times is shown in fig. 6 a). When the reaction time was increased from 1 h to 48 h, the benzyl alcohol yields of the catalysts Ir@CNT and Ir@CNT@ADH both increased with the increase of the reaction time, while the catalytic activity of the catalyst Ir@CNT@ADH was significantly higher than Ir@CNT. At a reaction time of 24.0 h, the benzyl alcohol yield of the catalyst Ir@CNT@ADH was about 50% higher than that of the catalyst Ir@CNT. The improvement of the catalytic performance of the catalyst Ir@CNT@ADH may be due to the increased number of times of recycling NADH in the enzyme catalytic reaction due to the presence of the ADH on the surface of the Ir@CNT@ADH. When the reaction time exceeded 24.0. 24.0 h, the benzyl alcohol yield began to stabilize, indicating that further extension of the reaction time did not significantly increase the yield. Thus, 24.0. 24.0 h is the optimal reaction time for the hydrogenation of benzaldehyde.
Further, the bookInvention investigation of NAD + Effect of concentration on catalytic efficiency of catalyst Ir@CNT@ADH, as shown in FIG. 6B), when NAD + At a concentration of 0.1. 0.1 mM, the benzyl alcohol yield was 46.7% and when NAD + When the concentration was increased to 0.5. 0.5 mM, the yield of benzyl alcohol was increased to 73.2%; when NAD + As the concentration was further increased to 1.0. 1.0 mM, the benzyl alcohol yield was slightly decreased to 72.9%, whereas when NAD was increased + When the concentration was increased to 5.0. 5.0 mM, the benzaldehyde yield was reduced to 44.2%, possibly due to NAD + Too high a concentration prevents the iridium complex from directly catalyzing the hydrogenation of benzaldehyde.
According to previous reports, amide form was used as complex for NAD under physiological conditions + Shows excellent catalytic hydrogenation activity, and the optimal environment for alcohol dehydrogenase ADH is reported to be pH 7.0-10.0. Therefore, the invention also further researches the influence of the pH value on the catalytic hydrogenation reaction of Ir@CNT@ADH. In phosphate buffer salt solution with pH value of 6.0-8.0, reacting at 37 ℃ in the presence of 30 mM benzaldehyde, 1.0 mg Ir@CNT@ADH and 100 mM HCOONa for 24 h. As shown in fig. 6C), at pH 6.5, the catalytic efficiency of ir@cnt@adh was highest and the benzyl alcohol yield was 80.4%, probably due to the co-catalytic effect of iridium complex and ADH. In addition, the effect of the amount of catalyst Ir@CNT@ADH on benzyl alcohol yield was studied by the present invention at 37℃with pH=6.5, 30 mM benzaldehyde, 24.0 h, 100 mM HCOONa, as shown in FIG. 6D). The yield of benzyl alcohol gradually increased as the Ir@CNT@ADH concentration increased from 0.1 mg/mL to 1.0 mg/mL, and at an Ir@CNT@ADH concentration of 1.0 mg/mL, the yield of benzyl alcohol reached 75.5% and was hardly changed with the increase in the Ir@CNT@ADH concentration.
According to the research results, the optimal catalytic condition for preparing benzyl alcohol by catalyzing benzaldehyde to hydrogenate through Ir@CNT@ADH of the carbon tube nano catalyst of immobilized iridium complex and enzyme provided by the invention is that the reaction time is 24 hours, the reaction pH is 6.5, and the NAD is + The concentration was 0.5 mM,Ir@CNT@ADH at 1.0 mg/mL.
Based on the results, the catalyst Ir@CNT@ADH provided by the invention has the following synergistic catalysis mechanism for preparing benzyl alcohol by hydrogenating benzaldehyde: first, the surface of Ir@CNT@ADH is modifiedIs capable of catalyzing NAD + Fast hydrogenation to generate a large amount of NADH; then, the NADH produced is used as coenzyme, and the alcohol dehydrogenase ADH can further catalyze the hydrogenation of the benzaldehyde derivative to produce corresponding benzyl alcohol. Successful establishment of this synergistic catalytic system requires assurance of iridium complex pair NAD + The hydrogenation activity of (2) is obviously higher than that of the p-benzaldehyde. This difference in catalytic activity ensures that NADH is preferentially formed, allowing continuous supply of coenzyme NADH in the enzymatic reaction. Furthermore, mutual deactivation between the organoiridium catalyst and the corresponding enzyme is a common problem in homogeneous co-catalytic systems, leading to deactivation of the catalyst. The double-solid-state carrier strategy of the metal complex catalyst and the biological enzyme provided by the invention effectively reduces the probability of mutual contact of the enzyme and the iridium complex, thereby greatly weakening the problem of mutual inactivation of the enzyme and the iridium complex and improving the overall catalytic performance of the synergistic catalytic system.
The ethanol dehydrogenase adopted by the invention has CAS number of 9031-72-5 and is from Saccharomyces cerevisiae.
The amino-functional carbon nanotube carrier material (NH) 2 CNT), also known as aminated carbon nanotube carrier material, which is a commercially available material, the amino-functionalized carbon nanotube carrier material (NH 2 -CNT), CAS number: (1333-86-4). The manufacturing factory: jiangsu Xianfeng nanometer materials science and technology Co., ltd., specification and model: the outer diameter is 8-15 nanometers, and the length is 50 micrometers.
Claims (5)
1. The carbon tube nano catalyst for immobilizing iridium complex and enzyme is characterized in that: it comprises glutaraldehyde activated carbon nanotube material CHO-CNT; the iridium complex is characterized by further comprising alcohol dehydrogenase ADH and pyrene functionalized iridium complexes which are respectively fixed on the surface of the glutaraldehyde activated carbon nanotube material CHO-CNT;
the structural formula of the carbon nanotube material CHO-CNT is as follows:
；
the pyrene functionalized iridium complex has the following structural formula:
。
2. the iridium complex and enzyme immobilized carbon tube nanocatalyst according to claim 1, wherein: the alcohol dehydrogenase ADH is alcohol dehydrogenase from Saccharomyces cerevisiae.
3. A method for preparing the iridium complex and enzyme immobilized carbon tube nanocatalyst according to claim 1 or 2, characterized by comprising the steps of:
step (1): adding an amino-functionalized carbon nanotube carrier material into glutaraldehyde aqueous solution, oscillating and incubating, centrifuging to remove excessive glutaraldehyde, cleaning, and then redispersing into the aqueous solution to obtain glutaraldehyde-activated carbon nanotube material aqueous solution;
step (2): dissolving a pyrene functionalized iridium complex in an N, N dimethylformamide solvent, adding the solution into the glutaraldehyde activated carbon nanotube material aqueous solution prepared in the step (1), performing ultrasonic treatment, centrifuging, washing with ethanol, and drying to obtain an iridium complex loaded carbon nanotube material Ir@CNT;
step (3): adding the iridium complex loaded carbon nanotube material Ir@CNT prepared in the step (2) into a phosphate buffer solution, then adding alcohol dehydrogenase ADH, centrifuging, washing with water and drying after the oscillating reaction is finished, thus obtaining the iridium complex and enzyme immobilized carbon nanotube nano catalyst Ir@CNT@ADH.
4. The method for applying the iridium complex and enzyme immobilized carbon tube nano-catalyst as claimed in claim 1 or 2, which is characterized in that: the catalyst is used for catalyzing the conversion of benzaldehyde compounds into corresponding benzyl alcohol compounds in the presence of formate and benzaldehyde.
5. Carbon tube nanocatalysis of the iridium complex and enzyme-immobilized catalyst of claim 4The application method of the agent is characterized in that the reaction conditions are as follows: the reaction time is 24 hours, the reaction pH is 6.5, and the reaction system NAD + The concentration was 0.5 mM,Ir@CNT@ADH at 1.0 mg/mL.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN202311321687.4A CN117070506B (en) | 2023-10-13 | 2023-10-13 | Carbon tube nano catalyst for immobilizing iridium complex and enzyme, preparation method and application thereof |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN202311321687.4A CN117070506B (en) | 2023-10-13 | 2023-10-13 | Carbon tube nano catalyst for immobilizing iridium complex and enzyme, preparation method and application thereof |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| CN117070506A CN117070506A (en) | 2023-11-17 |
| CN117070506B true CN117070506B (en) | 2023-12-12 |
Family
ID=88711971
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CN202311321687.4A Active CN117070506B (en) | 2023-10-13 | 2023-10-13 | Carbon tube nano catalyst for immobilizing iridium complex and enzyme, preparation method and application thereof |
Country Status (1)
| Country | Link |
|---|---|
| CN (1) | CN117070506B (en) |
Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN113058621A (en) * | 2019-12-12 | 2021-07-02 | 中国科学院大连化学物理研究所 | Reduced coenzyme and analogue regeneration catalyst thereof, preparation method and application |
| CN116183901A (en) * | 2023-01-04 | 2023-05-30 | 烟台大学 | Protein marker fluorescence detection method based on cyclodextrin-adamantane iridium complex main object assembly labeling |
-
2023
- 2023-10-13 CN CN202311321687.4A patent/CN117070506B/en active Active
Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN113058621A (en) * | 2019-12-12 | 2021-07-02 | 中国科学院大连化学物理研究所 | Reduced coenzyme and analogue regeneration catalyst thereof, preparation method and application |
| CN116183901A (en) * | 2023-01-04 | 2023-05-30 | 烟台大学 | Protein marker fluorescence detection method based on cyclodextrin-adamantane iridium complex main object assembly labeling |
Non-Patent Citations (2)
| Title |
|---|
| Tartaric acid stabilized iridium nanoparticles with excellent laccase-like activity;Hao, SH 等;Journal of meterials chemistry B;第11卷(第12期);2770-2777 * |
| 富CO2 气氛中镨基复合氧化物载金催化CO 氧化反应;张清逸等;分子催化;第37卷(第2期);109-117 * |
Also Published As
| Publication number | Publication date |
|---|---|
| CN117070506A (en) | 2023-11-17 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| Yuan et al. | Efficient NADH regeneration by a redox polymer-immobilized enzymatic system | |
| Wang et al. | Heterogeneous catalysis mediated cofactor NADH regeneration for enzymatic reduction | |
| Wu et al. | Methods for the regeneration of nicotinamide coenzymes | |
| Min et al. | Electroenzymatic synthesis of l-DOPA | |
| Lee et al. | Advances in electrochemical cofactor regeneration: enzymatic and non-enzymatic approaches | |
| Sharma et al. | Redox biocatalysis: quantitative comparisons of nicotinamide cofactor regeneration methods | |
| WO2022193381A1 (en) | Enzyme immobilization carrier and preparation method therefor, immobilized enzyme and preparation method therefor | |
| Nishigaki et al. | Oxidation of β-nicotinamide adenine dinucleotide (NADH) by Au cluster and nanoparticle catalysts aiming for coenzyme regeneration in enzymatic glucose oxidation | |
| CN114515581B (en) | Doped CdS photocatalyst and catalytic conversion of CO by same 2 Application in (a) | |
| Luan et al. | Bioelectrocatalysis for CO2 reduction: recent advances and challenges to develop a sustainable system for CO2 utilization | |
| CN113546661A (en) | Carbon-based single-atom photocatalyst and preparation method and application thereof | |
| JP4756601B2 (en) | Electrocatalyst and enzyme electrode | |
| Zhang et al. | Rhodium-based MOF-on-MOF difunctional core–shell nanoreactor for NAD (P) H regeneration and enzyme directed immobilization | |
| Zhao et al. | Hierarchical ZnIn2S4 microspheres as photocatalyst for boosting the selective biohydrogenation of furfural into furfuryl alcohol under visible light irradiation | |
| CN115236016A (en) | Chiral Co 3 O 4 -H 2 Application of TPPS-Au nano assembly | |
| CN117070506B (en) | Carbon tube nano catalyst for immobilizing iridium complex and enzyme, preparation method and application thereof | |
| Zhan et al. | Electroenzymatic reduction of furfural to furfuryl alcohol by an electron mediator and enzyme orderly assembled biocathode | |
| Sheng et al. | Light-Driven CO2 Reduction with a Surface-Displayed Enzyme Cascade–C3N4 Hybrid | |
| Zhou et al. | Highly selective regeneration of 1, 4-NADH enabled by a metal-free core-shell photocatalyst of resorcinol-formaldehyde resins@ polyaniline under visible light | |
| Wu et al. | Multienzyme co-immobilization-based bioelectrode: Design of principles and bioelectrochemical applications | |
| Jia et al. | Immobilization of enzymes on cyclodextrin-anchored dehiscent mesoporous TiO2 for efficient photoenzymatic hydroxylation | |
| US20070042479A1 (en) | Conversion of carbon dioxide to methanol in silica sol-gel matrix | |
| Liu et al. | Aspartic acid based metal–organic frameworks with dual function of NADH peroxidase and glycerol dehydrogenase-mimicking activities | |
| Burnett et al. | Supported Pt Enabled Proton-Driven NAD (P)+ Regeneration for Biocatalytic Oxidation | |
| CN108654679B (en) | Application of supported catalyst for improving selective hydrogenation of citronellal |
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 | ||
| GR01 | Patent grant | ||
| GR01 | Patent grant |