Genes involved in the citrate and glyoxylate cycles, which are repressible by glucose (Gancedo 1998), were upregulated in the xylose alone medium, indicating that xylose lacked the carbon catabolite repression capability.
However, the negative effect of YAP1 overexpression on xylose utilization was also observed in mineral medium, indicating that such effect was not related to the presence of inhibitors.
This trend was similar to that observed for monacolin K production in glutamic acid-containing medium, indicating that glutamic acid stimulated monacolin K production via the upregulation of the expression levels of these eight genes.
However, in the current study, biomass production decreased in the presence of ethanol (3% (v/v)) in the PDB medium, indicating that ethanol exhibited cellular toxicity, as evidenced by the complete growth inhibition of Phomopsis sp. XP-8.
The alloy EOC was −0.29 V vs. Hg/HgO/OH−, similar to that of pure copper in this medium, indicating that the processes which occur on the alloy surface are mainly governed by copper.
In this study, we found that the rate of furfural degradation and half maximal inhibitory concentration for furfural of C. tropicalis in xylose medium increased 1.68-fold and 1.19-fold, respectively, compared with those in glucose medium, indicating that C. tropicalis obtained better furfural tolerance in xylose medium.
Although the total conversion obtained with hydrogenation in scCO2 is similar to that in ethanol, the selectivity to amino products is higher in the former reaction medium, indicating that scCO2 is an ideal medium for the production of amino compounds with hydrogenation of nitro substrates using conventional supported metal catalysts.
The co-transformant of RelB/RelE grew well on the screening medium, indicating that the RelB interacted with RelE.
However, the resulting protein did not suppress the growth defect of Δtpi1 yeast on glucose medium indicating that this variant lacks catalytic activity.
However, yeast cells expressing TPI2ndATG were unable to grow on glucose medium indicating that this protein variant has no catalytic activity (Fig. 4D).
Inhibition of protein synthesis by chloramphenicol dramatically reduced AGEs accumulation in the medium indicating that AGEs formation is dependent on protein synthesis.
