Immobilization of Thermoplasma acidophilum Glucose Dehydrogenase and Isocitrate Dehydrogenase Through Enzyme-Inorganic Hybrid Nanocrystal Formation.

Journal

Current microbiology
ISSN: 1432-0991
Titre abrégé: Curr Microbiol
Pays: United States
ID NLM: 7808448

Informations de publication

Date de publication:
18 Jan 2024
Historique:
received: 16 08 2023
accepted: 29 11 2023
medline: 18 1 2024
pubmed: 18 1 2024
entrez: 18 1 2024
Statut: epublish

Résumé

The development of green catalysts, specifically biocatalysts, is crucial for building a sustainable society. To enhance the versatility of biocatalysts, the immobilization of enzymes plays a vital role as it improves their recyclability and robustness. As target enzymes to immobilize, glucose dehydrogenases and carboxylases are particularly important among various kinds of enzymes due to their involvement in two significant reactions: regeneration of the reduced form of coenzyme required for various reactions, and carboxylation reactions utilizing CO

Identifiants

DOI: 10.1007/s00284-023-03577-6 PMID: 38236425
pubmed: 38236425
doi: 10.1007/s00284-023-03577-6
pii: 10.1007/s00284-023-03577-6
doi:

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

67

Subventions

Organisme : Iwatani Naoji Foundation
ID : 48th

Informations de copyright

© 2024. The Author(s).

Références

Sheldon RA, Woodley JM (2018) Role of biocatalysis in sustainable chemistry. Chem Rev 118:801–838. https://doi.org/10.1021/acs.chemrev.7b00203
doi: 10.1021/acs.chemrev.7b00203 pubmed: 28876904
Koesoema AA, Standley DM, Senda T, Matsuda T (2020) Impact and relevance of alcohol dehydrogenase enantioselectivities on biotechnological applications. Appl Microbiol Biotechnol 104:2897–2909
doi: 10.1007/s00253-020-10440-2 pubmed: 32060695
Li G, Wang JB, Reetz MT (2018) Biocatalysts for the pharmaceutical industry created by structure-guided directed evolution of stereoselective enzymes. Bioorganic Med Chem 26:1241–1251. https://doi.org/10.1016/j.bmc.2017.05.021
doi: 10.1016/j.bmc.2017.05.021
T.sriwong K, Matsuda T (2022) Recent advances in enzyme immobilization utilizing nanotechnology for biocatalysis. Org Process Res Dev 26:1857–1877. https://doi.org/10.1021/acs.oprd.1c00404
doi: 10.1021/acs.oprd.1c00404
Basso A, Serban S (2019) Industrial applications of immobilized enzymes—a review. Mol Catal 479:110607. https://doi.org/10.1016/j.mcat.2019.110607
doi: 10.1016/j.mcat.2019.110607
Liese A, Hilterhaus L (2013) Evaluation of immobilized enzymes for industrial applications. Chem Soc Rev 42:6236–6249. https://doi.org/10.1039/C3CS35511J
doi: 10.1039/C3CS35511J pubmed: 23446771
Tran TD, Il KM (2018) Organic–inorganic hybrid nanoflowers as potent materials for biosensing and biocatalytic applications. Biochip J 12:268–279. https://doi.org/10.1007/s13206-018-2409-7
doi: 10.1007/s13206-018-2409-7
Cui J, Jia S (2017) Organic–inorganic hybrid nanoflowers: A novel host platform for immobilizing biomolecules. Coord Chem Rev 352:249–263. https://doi.org/10.1016/j.ccr.2017.09.008
doi: 10.1016/j.ccr.2017.09.008
Ge J, Lei J, Zare RN (2012) Protein-inorganic hybrid nanoflowers. Nat Nanotechnol 7:428–432. https://doi.org/10.1038/nnano.2012.80
doi: 10.1038/nnano.2012.80 pubmed: 22659609
T.sriwong K, Matsuda T (2022) Facile mussel-inspired polydopamine-coated 3D-printed bioreactors for continuous flow biocatalysis. React Chem Eng. https://doi.org/10.1039/d2re00040g
doi: 10.1039/d2re00040g
Zhang Y, Sun W, Elfeky NM et al (2020) Self-assembly of lipase hybrid nanoflowers with bifunctional Ca2+ for improved activity and stability. Enzyme Microb Technol 132:109408. https://doi.org/10.1016/j.enzmictec.2019.109408
doi: 10.1016/j.enzmictec.2019.109408 pubmed: 31731973
Altinkaynak C, Yilmaz I, Koksal Z et al (2016) Preparation of lactoperoxidase incorporated hybrid nanoflower and its excellent activity and stability. Int J Biol Macromol 84:402–409. https://doi.org/10.1016/j.ijbiomac.2015.12.018
doi: 10.1016/j.ijbiomac.2015.12.018 pubmed: 26712698
Yu Y, Fei X, Tian J et al (2015) Self-assembled enzyme–inorganic hybrid nanoflowers and their application to enzyme purification. Colloids Surfaces B Biointerfaces 130:299–304. https://doi.org/10.1016/j.colsurfb.2015.04.033
doi: 10.1016/j.colsurfb.2015.04.033 pubmed: 25935264
López-Gallego F, Yate L (2015) Selective biomineralization of Co3(PO4)2-sponges triggered by His-tagged proteins: Efficient heterogeneous biocatalysts for redox processes. Chem Commun 51:8753–8756. https://doi.org/10.1039/c5cc00318k
doi: 10.1039/c5cc00318k
T.sriwong K, Koesoema AA, Matsuda T (2020) Organic–inorganic nanocrystal reductase to promote green asymmetric synthesis. RSC Adv 10:30953–30960. https://doi.org/10.1039/d0ra03160g
doi: 10.1039/d0ra03160g pubmed: 35516042 pmcid: 9056328
T.sriwong K, Ogura K, Hawari MA, Matsuda T (2021) Geotrichum candidum aldehyde dehydrogenase-inorganic nanocrystal with enhanced activity. Enzyme Microb Technol. https://doi.org/10.1016/j.enzmictec.2021.109866
doi: 10.1016/j.enzmictec.2021.109866 pubmed: 34489025
Takagi M, T.sriwong K, Masuda T et al (2022) Immobilization of Baeyer–Villiger monooxygenase from acetone grown Fusarium sp. Biotechnol Lett 44:461–471. https://doi.org/10.1007/s10529-022-03224-3
doi: 10.1007/s10529-022-03224-3 pubmed: 35083583
Truppo MD (2012) 7.4 Cofactor recycling for enzyme catalyzed processes. Elsevier, Amsterdam
doi: 10.1016/B978-0-08-095167-6.00704-7
Qian WZ, Ou L, Li CX et al (2020) Evolution of Glucose Dehydrogenase for Cofactor Regeneration in Bioredox Processes with Denaturing Agents. ChemBioChem 21:2680–2688. https://doi.org/10.1002/cbic.202000196
doi: 10.1002/cbic.202000196 pubmed: 32324965
Koesoema AA, Sugiyama Y, T.sriwong K et al (2019) Reversible control of enantioselectivity by the length of ketone substituent in biocatalytic reduction. Appl Microbiol Biotechnol 103:9529–9541. https://doi.org/10.1007/s00253-019-10206-5
doi: 10.1007/s00253-019-10206-5 pubmed: 31720775
Xia S, Zhao X, Frigo-Vaz B et al (2015) Cascade enzymatic reactions for efficient carbon sequestration. Bioresour Technol 182:368–372. https://doi.org/10.1016/j.biortech.2015.01.093
doi: 10.1016/j.biortech.2015.01.093 pubmed: 25708541
Are KRA, Ohshima S, Koike Y et al (2021) Enzymatic direct carboxylation under supercritical CO2. Biochem Eng J 171:108004. https://doi.org/10.1016/j.bej.2021.108004
doi: 10.1016/j.bej.2021.108004
Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248–254. https://doi.org/10.1016/0003-2697(76)90527-3
doi: 10.1016/0003-2697(76)90527-3 pubmed: 942051
Block H, Maertens B, Spriestersbach A et al (2009) Chapter 27 immobilized-metal affinity chromatography (IMAC). A review. Methods Enzymol 463:439–473. https://doi.org/10.1016/S0076-6879(09)63027-5
doi: 10.1016/S0076-6879(09)63027-5 pubmed: 19892187
Yu J, Chen X, Jiang M et al (2018) Efficient promiscuous Knoevenagel condensation catalyzed by papain confined in Cu3(PO4)2 nanoflowers. RSC Adv 8:2357–2364. https://doi.org/10.1039/c7ra12940h
doi: 10.1039/c7ra12940h pubmed: 35541490 pmcid: 9077389
T.sriwong K, Kamogawa R, Castro Issasi CS et al (2022) Geotrichum candidum acetophenone reductase immobilization on reduced graphene oxide: a promising biocatalyst for green asymmetric reduction of ketones. Biochem Eng J. https://doi.org/10.1016/j.bej.2021.108263
doi: 10.1016/j.bej.2021.108263
Vassiliadi E, Aridas A, Schmitt V et al (2022) (Hydroxypropyl)methyl cellulose-chitosan film as a matrix for lipase immobilization: Operational and morphological study. Mol Catal 522:112252. https://doi.org/10.1016/j.mcat.2022.112252
doi: 10.1016/j.mcat.2022.112252
Aleku GA, Roberts GW, Titchiner GR, Leys D (2021) Synthetic enzyme-catalyzed CO2 fixation reactions. Chemsuschem 14:1781–1804. https://doi.org/10.1002/cssc.202100159
doi: 10.1002/cssc.202100159 pubmed: 33631048 pmcid: 8252502
Ienaga S, Kosaka S, Honda Y et al (2013) P-aminosalicylic acid production by enzymatic kolbeschmitt reaction using salicylic acid decarboxylases improved through site-directed mutagenesis. Bull Chem Soc Jpn 86:628–634. https://doi.org/10.1246/bcsj.20130006
doi: 10.1246/bcsj.20130006
Wieser M, Fujii N, Yoshida T, Nagasawa T (1998) Carbon dioxide fixation by reversible pyrrole-2-carboxylate decarboxylase and its application. Eur J Biochem 257:495–499. https://doi.org/10.1046/j.1432-1327.1998.2570495.x
doi: 10.1046/j.1432-1327.1998.2570495.x pubmed: 9826198
Wieser M, Yoshida T, Nagasawa T (1998) Microbial synthesis of pyrrole-2-carboxylate by Bacillus megaterium PYR2910. Tetrahedron Lett 39:4309–4310. https://doi.org/10.1016/S0040-4039(98)00718-7
doi: 10.1016/S0040-4039(98)00718-7
Matsuda T, Ohashi Y, Harada T et al (2001) Conversion of pyrrole to pyrrole-2-carboxylate by cells of Bacillus megaterium in supercritical CO2. Chem Commun 21:2194–2195. https://doi.org/10.1039/b105137g
doi: 10.1039/b105137g

Auteurs

Shusuke Oshima (S)

Department of Life Science and Technology, School of Life Science and Technology, Tokyo Institute of Technology, 4259 Nagatsuta-Cho, Midori-Ku, Yokohama, 226-8501, Japan.

Yuri Oku (Y)

Department of Life Science and Technology, School of Life Science and Technology, Tokyo Institute of Technology, 4259 Nagatsuta-Cho, Midori-Ku, Yokohama, 226-8501, Japan.

Kotchakorn T Sriwong (K)

Department of Life Science and Technology, School of Life Science and Technology, Tokyo Institute of Technology, 4259 Nagatsuta-Cho, Midori-Ku, Yokohama, 226-8501, Japan.
Department of Chemistry and California Institute for Quantitative Bioscience, University of California, Berkeley, Berkeley, California, 94720, USA.

Yutaro Kimura (Y)

Department of Life Science and Technology, School of Life Science and Technology, Tokyo Institute of Technology, 4259 Nagatsuta-Cho, Midori-Ku, Yokohama, 226-8501, Japan.

Tomoko Matsuda (T)

Department of Life Science and Technology, School of Life Science and Technology, Tokyo Institute of Technology, 4259 Nagatsuta-Cho, Midori-Ku, Yokohama, 226-8501, Japan. tmatsuda@bio.titech.ac.jp.
ORCID: 0000-0002-8934-8198

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