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Title: Enhanced production of 2,3-butanediol in pyruvate decarboxylase-deficient Saccharomyces cerevisiae through optimizing ratio of glucose/galactose

Authors:
 [1];  [1];  [1];  [2];  [2];  [3];  [2];  [1]
  1. Department of Agricultural Biotechnology and Center for Food and Bioconvergence, Seoul National University, Seoul Republic of Korea
  2. Department of Food Science and Human Nutrition, and Institute for Genomic Biology, University of Illinois at Urbana-Champaign, Urbana Illinois USA
  3. Department of Advanced Fermentation Fusion Science and Technology, Kookmin University, Seoul Republic of Korea
Publication Date:
Sponsoring Org.:
USDOE Office of Energy Efficiency and Renewable Energy (EERE), Bioenergy Technologies Office (EE-3B)
OSTI Identifier:
1401461
Grant/Contract Number:
2011-0031359
Resource Type:
Journal Article: Publisher's Accepted Manuscript
Journal Name:
Biotechnology Journal
Additional Journal Information:
Journal Volume: 11; Journal Issue: 11; Related Information: CHORUS Timestamp: 2017-10-20 17:24:35; Journal ID: ISSN 1860-6768
Publisher:
Wiley Blackwell (John Wiley & Sons)
Country of Publication:
Country unknown/Code not available
Language:
English

Citation Formats

Choi, Eun-Ji, Kim, Jin-Woo, Kim, Soo-Jung, Seo, Seung-Oh, Lane, Stephan, Park, Yong-Cheol, Jin, Yong-Su, and Seo, Jin-Ho. Enhanced production of 2,3-butanediol in pyruvate decarboxylase-deficient Saccharomyces cerevisiae through optimizing ratio of glucose/galactose. Country unknown/Code not available: N. p., 2016. Web. doi:10.1002/biot.201600042.
Choi, Eun-Ji, Kim, Jin-Woo, Kim, Soo-Jung, Seo, Seung-Oh, Lane, Stephan, Park, Yong-Cheol, Jin, Yong-Su, & Seo, Jin-Ho. Enhanced production of 2,3-butanediol in pyruvate decarboxylase-deficient Saccharomyces cerevisiae through optimizing ratio of glucose/galactose. Country unknown/Code not available. doi:10.1002/biot.201600042.
Choi, Eun-Ji, Kim, Jin-Woo, Kim, Soo-Jung, Seo, Seung-Oh, Lane, Stephan, Park, Yong-Cheol, Jin, Yong-Su, and Seo, Jin-Ho. 2016. "Enhanced production of 2,3-butanediol in pyruvate decarboxylase-deficient Saccharomyces cerevisiae through optimizing ratio of glucose/galactose". Country unknown/Code not available. doi:10.1002/biot.201600042.
@article{osti_1401461,
title = {Enhanced production of 2,3-butanediol in pyruvate decarboxylase-deficient Saccharomyces cerevisiae through optimizing ratio of glucose/galactose},
author = {Choi, Eun-Ji and Kim, Jin-Woo and Kim, Soo-Jung and Seo, Seung-Oh and Lane, Stephan and Park, Yong-Cheol and Jin, Yong-Su and Seo, Jin-Ho},
abstractNote = {},
doi = {10.1002/biot.201600042},
journal = {Biotechnology Journal},
number = 11,
volume = 11,
place = {Country unknown/Code not available},
year = 2016,
month = 9
}

Journal Article:
Free Publicly Available Full Text
Publisher's Version of Record at 10.1002/biot.201600042

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  • Pyruvate decarboxylase is a key enzyme in the production of low-molecular-weight byproducts (ethanol, acetate) in biomass-directed applications of Saccharomyces cerevisiae. To investigate whether decreased expression levels of pyruvate decarboxylase can reduce byproduct formation, the PDC2 gene, which encodes a positive regulator of pyruvate-decarboxylase synthesis, was inactivated in the prototrophic strain S. cerevisiae CEN.PK113-7D. This caused a 3--4-fold reduction of pyruvate-decarboxylase activity in glucose-limited, aerobic chemostat cultures grown at a dilution rate of 0.10 h{sup {minus}1}. Upon exposure of such cultures to a 50 mM glucose pulse, ethanol and acetate were the major byproducts formed by the wild type. In themore » pdc2{Delta} strain, formation of ethanol and acetate was reduced by 60--70%. In contrast to the wild type, the pdc2{Delta} strain produced substantial amounts of pyruvate after a glucose pulse. Nevertheless, its overall byproduct formation was ca. 50% lower. The specific rate of glucose consumption after a glucose pulse to pdc2{Delta} cultures was about 40% lower than in wild-type cultures.« less
  • A Gtr1p GTPase, the GDP mutant of which suppresses both temperature-sensitive mutants of Saccharomyces cerevisiae RanGEF/Prp20p and RanGAP/Rna1p, was presently found to interact with Yrb2p, the S. cerevisiae homologue of mammalian Ran-binding protein 3. Gtr1p bound the Ran-binding domain of Yrb2p. In contrast, Gtr2p, a partner of Gtr1p, did not bind Yrb2p, although it bound Gtr1p. A triple mutant: yrb2{delta} gtr1{delta} gtr2{delta} was lethal, while a double mutant: gtr1{delta} gtr2{delta} survived well, indicating that Yrb2p protected cells from the killing effect of gtr1{delta} gtr2{delta}. Recombinant Gtr1p and Gtr2p were purified as a complex from Escherichia coli. The resulting Gtr1p-Gtr2p complexmore » was comprised of an equal amount of Gtr1p and Gtr2p, which inhibited the Rna1p/Yrb2 dependent RanGAP activity. Thus, the Gtr1p-Gtr2p cycle was suggested to regulate the Ran cycle through Yrb2p.« less
  • Zymomonas mobilis genes for pyruvate decarboxylase (pdc) and alcohol dehydrogenase II (adhB) were integrated into the Escherichia coli chromosome within or near the pyruvate formate-lyase gene (pfl). Integration improved the stability of the Z. mobilis genes in E. coli, but further selection was required to increase expression. Spontaneous mutants were selected for resistance to high levels of chloramphenicol that also expressed high levels of the Z. mobilis genes. Analogous mutants were selected for increased expression of alcohol dehydrogenase on aldehyde indicator plates. These mutants were functionally equivalent to the previous plasmid-based strains for the fermentation of xylose and glucose tomore » ethanol. Ethanol concentrations of 54.4 and 41.6 g/liter were obtained from 10% glucose and 8% xylose, respectively. The efficiency of conversion exceeded theoretical limits (0.51 g of ethanol/g of sugar) on the basis of added sugars because of the additional production of ethanol from the catabolism of complex nutrients. Further mutations were introduced to inactivate succinate production (frd) and to block homologous recombination (recA).« less