Bioscience Evidence 2024, Vol.14, No.3, 131-142 http://bioscipublisher.com/index.php/be 140 Conflict of Interest Disclosure The author affirms that this research was conducted without any commercial or financial relationships that could be construed as a potential conflict of interest. References Acevedo-Rocha C., Gamble C., Lonsdale R., Li A., Nett N., Hoebenreich S., Lingnau J., Wirtz C., Farés C., Hinrichs H., Deege A., Mulholland A., Nov Y., Leys D., McLean K., Munro A., and Reetz M., 2018, P450-catalyzed regio- and diastereoselective steroid hydroxylation: efficient directed evolution enabled by mutability landscaping, ACS Catalysis, 8: 3395-3410. https://doi.org/10.1021/ACSCATAL.8B00389 Agresti J., Antipov E., Abate A., Ahn K., Rowat A., Baret J., Márquez M., Klibanov A., Griffiths A., and Weitz D., 2010, Ultrahigh-throughput screening in drop-based microfluidics for directed evolution, Proceedings of the National Academy of Sciences, 107: 4004-4009. https://doi.org/10.1073/pnas.0910781107 Ariaeenejad S., Jokar F., Hadian P., Ma’mani L., Gharaghani S., Fereidoonnezhad M., and Salekdeh G., 2020, An efficient nano-biocatalyst for lignocellulosic biomass hydrolysis: Xylanase immobilization on organically modified biogenic mesoporous silica nanoparticles, International Journal of Biological Macromolecules, 164: 3462-3473. https://doi.org/10.1016/j.ijbiomac.2020.08.211 Boukid F., Ganeshan S., Wang Y., Tülbek M., and Nickerson M., 2023, Bioengineered enzymes and precision fermentation in the food industry, International Journal of Molecular Sciences, 24(12): 10156. https://doi.org/10.3390/ijms241210156 Broom A., Rakotoharisoa R., Thompson M., Zarifi N., Nguyen E., Mukhametzhanov N., Liu L., Fraser J., and Chica R., 2020, Ensemble-based enzyme design can recapitulate the effects of laboratory directed evolution in silico, Nature Communications, 11(1): 4808. https://doi.org/10.1038/s41467-020-18619-x Cao Y., Li X., and Ge J., 2021, Enzyme catalyst engineering toward the integration of biocatalysis and chemocatalysis, Trends in Biotechnology, 39(11): 1173-1183. https://doi.org/10.1016/j.tibtech.2021.01.002 Chen K., and Arnold F., 2020, Engineering new catalytic activities in enzymes, Nature Catalysis, 3: 203-213. https://doi.org/10.1038/s41929-019-0385-5 Cobb R., Sun N., and Zhao H., 2013, Directed evolution as a powerful synthetic biology tool, Methods, 60(1): 81-90. https://doi.org/10.1016/j.ymeth.2012.03.009 Currin A., Parker S., Robinson C., Takano E., Scrutton N., and Breitling R., 2021, The evolving art of creating genetic diversity: From directed evolution to synthetic biology, Biotechnology Advances, 50: 107762. https://doi.org/10.1016/j.biotechadv.2021.107762 Denard C., Ren H., and Zhao H., 2015, Improving and repurposing biocatalysts via directed evolution, Current Opinion in Chemical Biology, 25: 55-64. https://doi.org/10.1016/j.cbpa.2014.12.036 Hoebenreich S., Zilly F., Acevedo-Rocha C., Zilly M., and Reetz M., 2015, Speeding up directed evolution: combining the advantages of solid-phase combinatorial gene synthesis with statistically guided reduction of screening effort, ACS Synthetic Biology, 4(3): 317-331. https://doi.org/10.1021/sb5002399 Jakočiūnas T., Pedersen L., Lis A., Jensen M., and Keasling J., 2018, CasPER, a method for directed evolution in genomic contexts using mutagenesis and CRISPR/Cas9, Metabolic Engineering, 48: 288-296. https://doi.org/10.1016/j.ymben.2018.07.001 Jensen E., Ambri F., Bendtsen M., Javanpour A., Liu C., Jensen M., and Keasling J., 2020, Integrating continuous hypermutation with high‐throughput screening for optimization of cis,cis-muconic acid production in yeast, Microbial Biotechnology, 14: 2617-2626. https://doi.org/10.1111/1751-7915.13774 Kaur J., and Sharma R., 2006, Directed evolution: an approach to engineer enzymes, Critical Reviews in Biotechnology, 26: 165-199. https://doi.org/10.1080/07388550600851423 Kim J., Huang R., Chen H., You C., and Zhang Y., 2016, Facile construction of random gene mutagenesis library for directed evolution without the use of restriction enzyme in Escherichia coli, Biotechnology Journal, 11(9): 1142-1150. https://doi.org/10.1002/biot.201600121 Kumar A., and Singh S., 2013, Directed evolution: tailoring biocatalysts for industrial applications, Critical Reviews in Biotechnology, 33: 365-378. https://doi.org/10.3109/07388551.2012.716810 Labrou N., 2009, Random mutagenesis methods for in vitro directed enzyme evolution, Current Protein & Peptide Science, 11(1): 91-100. https://doi.org/10.2174/138920310790274617 Leveson-Gower R., Mayer C., and Roelfes G., 2019, The importance of catalytic promiscuity for enzyme design and evolution, Nature Reviews Chemistry, 3: 687-705. https://doi.org/10.1038/s41570-019-0143-x
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