Data for Glucose Assimilation Rate Determines the Partition of Flux at Pyruvate Between Lactic Acid and Ethanol in Saccharomyces cerevisiae

Lane, Stephan; Turner, Timothy L.; Jin, Yong-Su

doi:10.13012/B2IDB-2019701_V1

Title: Data for Glucose Assimilation Rate Determines the Partition of Flux at Pyruvate Between Lactic Acid and Ethanol in Saccharomyces cerevisiae

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Abstract

Engineered Saccharomyces cerevisiae expressing a lactic acid dehydrogenase can metabolize pyruvate into lactic acid. However, three pyruvate decarboxylase (PDC) isozymes drive most carbon flux toward ethanol rather than lactic acid. Deletion of endogenous PDCs will eliminate ethanol production, but the resulting strain suffers from C2 auxotrophy and struggles to complete a fermentation. Engineered yeast assimilating xylose or cellobiose produce lactic acid rather than ethanol as a major product without the deletion of any PDC genes. We report here that sugar flux, but not sensing, contributes to the partition of flux at the pyruvate branch point in S. cerevisiae expressing the Rhizopus oryzae lactic acid dehydrogenase (LdhA). While the membrane glucose sensors Snf3 and Rgt2 did not play any direct role in the option of predominant product, the sugar assimilation rate was strongly correlated to the partition of flux at pyruvate: fast sugar assimilation favors ethanol production while slow sugar assimilation favors lactic acid. Applying this knowledge, we created an engineered yeast capable of simultaneously converting glucose and xylose into lactic acid, increasing lactic acid production to approximately 17 g L−1 from the 12 g L−1 observed during sequential consumption of sugars. This work elucidates the carbon source-dependent effects on productmore » selection in engineered yeast.« less

Authors:

; Turner, Timothy L.; Jin, Yong-Su

Carl R. Woese Institute for Genomic Biology, University of Illinois at Urbana-Champaign, Urbana, Illinois, USA; Center for Advanced Bioenergy and Bioproducts Innovation (CABBI), Urbana, IL (United States)
Department of Food Science and Human Nutrition, University of Illinois at Urbana-Champaign, Urbana, Illinois, USA

Publication Date:: Wed Feb 01 00:00:00 UTC 2023

DOE Contract Number:: SC0018420

Research Org.:: Center for Advanced Bioenergy and Bioproducts Innovation (CABBI), Urbana, IL (United States); University of Illinois Urbana-Champaign

Sponsoring Org.:: U.S. Department of Energy (DOE)

Subject:: Conversion; Metabolomics; Transcriptomics

OSTI Identifier:: 3014450

DOI:: https://doi.org/10.13012/B2IDB-2019701_V1

Citation Formats


                    Lane, Stephan, Turner, Timothy L., and Jin, Yong-Su. Data for Glucose Assimilation Rate Determines the Partition of Flux at Pyruvate Between Lactic Acid and Ethanol in Saccharomyces cerevisiae.  United States: N. p., 2023. 
        Web.  doi:10.13012/B2IDB-2019701_V1.

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                    Lane, Stephan, Turner, Timothy L., & Jin, Yong-Su. Data for Glucose Assimilation Rate Determines the Partition of Flux at Pyruvate Between Lactic Acid and Ethanol in Saccharomyces cerevisiae.  United States.  doi:https://doi.org/10.13012/B2IDB-2019701_V1

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                    Lane, Stephan, Turner, Timothy L., and Jin, Yong-Su. 2023.  
"Data for Glucose Assimilation Rate Determines the Partition of Flux at Pyruvate Between Lactic Acid and Ethanol in Saccharomyces cerevisiae".  United States.  doi:https://doi.org/10.13012/B2IDB-2019701_V1.  https://www.osti.gov/servlets/purl/3014450. Pub date:Wed Feb 01 00:00:00 UTC 2023

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@article{osti_3014450,

  title        = {Data for Glucose Assimilation Rate Determines the Partition of Flux at Pyruvate Between Lactic Acid and Ethanol in Saccharomyces cerevisiae},

  author       = {Lane, Stephan and Turner, Timothy L. and Jin, Yong-Su},

  abstractNote = {Engineered Saccharomyces cerevisiae expressing a lactic acid dehydrogenase can metabolize pyruvate into lactic acid. However, three pyruvate decarboxylase (PDC) isozymes drive most carbon flux toward ethanol rather than lactic acid. Deletion of endogenous PDCs will eliminate ethanol production, but the resulting strain suffers from C2 auxotrophy and struggles to complete a fermentation. Engineered yeast assimilating xylose or cellobiose produce lactic acid rather than ethanol as a major product without the deletion of any PDC genes. We report here that sugar flux, but not sensing, contributes to the partition of flux at the pyruvate branch point in S. cerevisiae expressing the Rhizopus oryzae lactic acid dehydrogenase (LdhA). While the membrane glucose sensors Snf3 and Rgt2 did not play any direct role in the option of predominant product, the sugar assimilation rate was strongly correlated to the partition of flux at pyruvate: fast sugar assimilation favors ethanol production while slow sugar assimilation favors lactic acid. Applying this knowledge, we created an engineered yeast capable of simultaneously converting glucose and xylose into lactic acid, increasing lactic acid production to approximately 17 g L−1 from the 12 g L−1 observed during sequential consumption of sugars. This work elucidates the carbon source-dependent effects on product selection in engineered yeast.},

  doi          = {10.13012/B2IDB-2019701_V1},

  journal      = {},

  number       = ,

  volume       = ,

  place        = {United States},

  year         = {Wed Feb 01 00:00:00 UTC 2023},

  month        = {Wed Feb 01 00:00:00 UTC 2023}

}

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DOI: https://doi.org/10.13012/B2IDB-2019701_V1

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Glucose assimilation rate determines the partition of flux at pyruvate between lactic acid and ethanol in Saccharomyces cerevisiae

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Engineered Saccharomyces cerevisiae expressing a lactic acid dehydrogenase can metab- olize pyruvate into lactic acid. However, three pyruvate decarboxylase (PDC) isozymes drive most carbon flux toward ethanol rather than lactic acid. Deletion of endoge- nous PDCs will eliminate ethanol production, but the resulting strain suffers from C₂ auxotrophy and struggles to complete a fermentation. Engineered yeast assimilating xylose or cellobiose produce lactic acid rather than ethanol as a major product with- out the deletion of any PDC genes. We report here that sugar flux, but not sensing, contributes to the partition of flux at the pyruvate branch point in S.more »« less
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