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Co-expression of two heterologous lactate dehydrogenases genes in Kluyveromyces marxianus for L-lactic acid production

Title
Co-expression of two heterologous lactate dehydrogenases genes in Kluyveromyces marxianus for L-lactic acid production
Authors
Lee, Jae WonIn, Jung HoonPark, Joon-BumShin, JonghyeokPark, Jin HwanSung, Bong HyunSohn, Jung-HoonSeo, Jin-HoPark, Jin-ByoungKim, Soo RinKweon, Dae-Hyuk
Ewha Authors
박진병
SCOPUS Author ID
박진병scopus
Issue Date
2017
Journal Title
JOURNAL OF BIOTECHNOLOGY
ISSN
0168-1656JCR Link1873-4863JCR Link
Citation
vol. 241, pp. 81 - 86
Keywords
Lactic acidKluyveromyces marxianusLactate dehydrogenaseCo-expressionOptimal pH
Publisher
ELSEVIER SCIENCE BV
Indexed
SCI; SCIE; SCOPUS WOS scopus
Abstract
Lactic acid (LA) is a versatile compound used in the food, pharmaceutical, textile, leather, and chemical industries. Biological production of LA is possible by yeast strains expressing a bacterial gene encoding L-lactate dehydrogenase (LDH). Kluyveromyces marxianus is an emerging non-conventional yeast with various phenotypes of industrial interest. However, it has not been extensively studied for LA production. In this study, K. marxianus was engineered to express and co-express various heterologous LDH enzymes that were reported to have different pH optimums. Specifically, three LDH enzymes originating from Staphylococcus epidermidis (SeLDH; optimal at pH 5.6), Lactobacillus acidophilus (LaLDH; optimal at pH 5.3), and Bos taurus (BtLDH; optimal at pH 9.8) were functionally expressed individually and in combination in K. marxianus, and the resulting strains were compared in terms of LA production. A strain co-expressing SeLDH and LaLDH (KM5 La + SeLDH) produced 16.0 g/L LA, whereas the strains expressing those enzymes individually produced only 8.4 and 6.8 g/L, respectively. This co-expressing strain produced 24.0 g/LA with a yield of 0.48 gig glucose in the presence of CaCO3. Our results suggest that co-expression of LDH enzymes with different pH optimums provides sufficient LDH activity under dynamic intracellular pH conditions, leading to enhanced production of LA compared to individual expression of the LDH enzymes. (C) 2016 Elsevier B.V. All rights reserved.
DOI
10.1016/j.jblotec.2016.11.015
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엘텍공과대학 > 식품공학전공 > Journal papers
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