Transcriptional Changes in the Xylose Operon in and Their Use in Fermentation Optimization
Overview
Chemistry
Molecular Biology
Affiliations
The xylose operon is an efficient biological element used for the regulation of gene expression in . Although the mechanism underlying the xylose-mediated regulation of this operon has been elucidated, the transcriptional changes that occur under various fermentation conditions remain unclear. In this study, the effects of different conditions on xylose operon expression were investigated. Significant upregulation was observed during the transition from the logarithmic phase to the stationary phase (2.5-fold, = 3, < 0.01). Glucose suppressed transcription over 168-fold ( = 3, < 0.01). Meanwhile, the inhibitory effect of glucose hardly strengthened at concentrations from 20 to 180 g/L. Furthermore, the transcription of the xylose operon increased at elevated temperatures (25-42 °C) and was optimal at a neutral pH (pH 6.5-7.0). Based on these findings, relevant fermentation strategies (delaying the induction time, using dextrin as a carbon source, increasing the fermentation temperature, and maintaining a neutral pH) were proposed. Subsequently, these strategies were validated through the use of maltogenic amylase as a reporter protein, as an 8-fold ( = 3, < 0.01) increase in recombinant enzyme activity compared to that under unoptimized conditions was observed. This work contributes to the development of fermentation optimization and furthers the use of the xylose operon as an efficient expression element.
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Xiao F, Zhang Y, Zhang L, Li S, Chen W, Shi G Microorganisms. 2024; 12(8).
PMID: 39203534 PMC: 11356801. DOI: 10.3390/microorganisms12081693.
Zhang Y, Hu J, Zhang Q, Cai D, Chen S, Wang Y Bioresour Bioprocess. 2024; 10(1):27.
PMID: 38647919 PMC: 10991860. DOI: 10.1186/s40643-023-00641-8.
Li Y, Ma X, Zhang L, Ding Z, Xu S, Gu Z Int J Mol Sci. 2022; 23(21).
PMID: 36362266 PMC: 9655642. DOI: 10.3390/ijms232113480.
A new CcpA binding site plays a bidirectional role in carbon catabolism in .
Xiao F, Li Y, Zhang Y, Wang H, Zhang L, Ding Z iScience. 2021; 24(5):102400.
PMID: 33997685 PMC: 8091064. DOI: 10.1016/j.isci.2021.102400.
Nnolim N, Mpaka L, Okoh A, Nwodo U Microorganisms. 2020; 8(9).
PMID: 32867042 PMC: 7565512. DOI: 10.3390/microorganisms8091304.