ArticleBeilstein journal of organic chemistry2015
Engineering Pichia pastoris for improved NADH regeneration: A novel chassis strain for whole-cell catalysis.
Article in Beilstein journal of organic chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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11 citing papers in PubMed, 35 citations in OpenAlex.
- Efficient expression of full-length triple-helix recombinant type III collagen inSynthetic and systems biotechnology · 2027Article
- Enhanced recombinant xylanase B expression in Komagataella phaffii through metabolic engineering of methanol utilization.Archives of microbiology · 2025Article
- Freeze-cast SiOC ceramics supporting the growth of industrially relevant microorganisms.PloS one · 2025Article
- Hansenula polymorpha methanol metabolism genes enhance recombinant protein production in Komagataella phaffi.AMB Express · 2024Article
- Effect and mechanism of signal peptide and maltose on recombinant type III collagen production in Pichia pastoris.Applied microbiology and biotechnology · 2023Article
- Comparative transcriptome and metabolome analyses reveal the methanol dissimilation pathway of Pichia pastoris.BMC genomics · 2022Article
- Advances in Cell Engineering of theMetabolites · 2022Review
- Strains and Molecular Tools for Recombinant Protein Production in Pichia pastoris.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Carbon metabolism influenced for promoters and temperature used in the heterologous protein production using Pichia pastoris yeast.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2018Review
- Expanding the CRISPR/Cas9 toolkit for Pichia pastoris with efficient donor integration and alternative resistance markers.Journal of cellular biochemistry · 2018Article
- Refined Pichia pastoris reference genome sequence.Journal of biotechnology · 2016Review
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Authors and funding
6 authors at 4 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Many synthetically useful reactions are catalyzed by cofactor-dependent enzymes. As cofactors represent a major cost factor, methods for efficient cofactor regeneration are required especially for large-scale synthetic applications. In order to generate a novel and efficient host chassis for bioreductions, we engineered the methanol utilization pathway of Pichia pastoris for improved NADH regeneration. By deleting the genes coding for dihydroxyacetone synthase isoform 1 and 2 (DAS1 and DAS2), NADH regeneration via methanol oxidation (dissimilation) was increased significantly. The resulting Δdas1 Δdas2 strain performed better in butanediol dehydrogenase (BDH1) based whole-cell conversions. While the BDH1 catalyzed acetoin reduction stopped after 2 h reaching ~50% substrate conversion when performed in the wild type strain, full conversion after 6 h was obtained by employing the knock-out strain. These results suggest that the P. pastoris Δdas1 Δdas2 strain is capable of supplying the actual biocatalyst with the cofactor over a longer reaction period without the over-expression of an additional cofactor regeneration system. Thus, focusing the intrinsic carbon flux of this methylotrophic yeast on methanol oxidation to CO2 represents an efficient and easy-to-use strategy for NADH-dependent whole-cell conversions. At the same time methanol serves as co-solvent, inductor for catalyst and cofactor regeneration pathway expression and source of energy.
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