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• W2892900500 abstract "Methanol is a low-cost and abundantly available feedstock derived from natural gas and syngas. Although bioconversion holds promise for producing desired chemicals from methanol under economically viable operating conditions, the efficiency is limited by unfavorable kinetics of methanol oxidation and assimilation. Herein, artificial fusion proteins were engineered to enhance methanol bioconversion. Nicotinamide adenine dinucleotide (NAD)-dependent methanol dehydrogenase (Mdh), 3-hexulose-6-phosphate synthase (Hps) and 6-phospho-3-hexuloisomerase (Phi) from different sources were first screened for catalytic activity. Next, we designed six fusion proteins using the best enzyme candidates and flexible linkers. Fusing Mdh with Hps or Hps-Phi increased the Vmax of methanol oxidation up to 5.8-fold, and enhanced methanol conversion to fructose-6-phosphate up to 1.3-fold. Interestingly, fusion engineering changed the polymerization states of proteins and produced larger multimers, which may be responsible for the changed catalytic characteristics. This fusion engineering approach can be coupled with other metabolic engineering strategies for enhanced methanol bioconversion to valuable chemicals." @default.
• W2892900500 created "2018-10-05" @default.
• W2892900500 creator A5013434529 @default.
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• W2892900500 date "2018-10-23" @default.
• W2892900500 modified "2023-09-30" @default.
• W2892900500 title "Engineering Artificial Fusion Proteins for Enhanced Methanol Bioconversion" @default.
• W2892900500 cites W124695960 @default.
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• W2892900500 doi "https://doi.org/10.1002/cbic.201800424" @default.
• W2892900500 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/30246938" @default.
• W2892900500 hasPublicationYear "2018" @default.
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