Degradation and assimilation of aromatic compounds by Corynebacterium glutamicum: another potential for applications for this bacterium?

Abstract

With the implementation of the well-established molecular tools and systems biology techniques, new knowledge on aromatic degradation and assimilation by Corynebacterium glutamicum has been emerging. This review summarizes recent findings on degradation of aromatic compounds by C. glutamicum. Among these findings, the mycothiol-dependent gentisate pathway was firstly discovered in C. glutamicum. Other important knowledge derived from C. glutamicum would be the discovery of linkages among aromatic degradation and primary metabolisms such as gluconeogenesis and central carbon metabolism. Various transporters in C. glutamicum have also been identified, and they play an essential role in microbial assimilation of aromatic compounds. Regulation on aromatic degradation occurs mainly at transcription level via pathway-specific regulators, but global regulator(s) is presumably involved in the regulation. It is concluded that C. glutamicum is a very useful model organism to disclose new knowledge of biochemistry, physiology, and genetics of the catabolism of aromatic compounds in high GC content Gram-positive bacteria, and that the new physiological properties of aromatic degradation and assimilation are potentially important for industrial applications of C. glutamicum.

Base-Catalyzed Depolymerization of Solid Lignin-Rich Streams Enables Microbial Conversion

“…These aromatics are intermediates in pcoumaric and ferulic acid catabolic pathways, respectively. 42,51 Thus, the accumulation of these compounds suggests that there may be bottlenecks within the β-ketoadipate pathway under the conditions studied in this work. Both p-hydroxybenzoic and vanillic acids were detected in all organisms, but this effect was more evident in P. putida, likely because of the faster consumption of p-coumaric acid.…”

“…33 This bacterium is capable of assimilating diverse aromatic compounds through the formation of catechol, protocatechuate, gentisate, 1,2,4-trihydroxybenzene, and other central aromatic intermediates that can be further converted into tricarboxylic acid cycle intermediates. 51 In contrast to C. glutamicum, the red yeast R. mucilaginosa has limited available information, and was able to produce 4.6 g/L of biomass with a 5-fold higher μ and a 43% higher Y b/s , making evident differences in substrate assimilation pathways and yields of biomass precursors (Figure 4b). R. mucilaginosa naturally produces a high concentration of pigments and lipids, offering attractive opportunities for valorization of lignin-derived compounds.…”

BacHBerry: BACterial Hosts for production of Bioactive phenolics from bERRY fruits

“…C. glutamicum is a very robust microorganism, which shows high resistance to the presence of small aromatic compounds (Liu et al 2013), which renders C. glutamicum a very promising host for the production of pharmacologically interesting plant-derived polyphenols (Marienhagen and Bott 2013). Until recently, the activity of a complex catabolic network for aromatic compounds meant that C. glutamicum was not used for the production of aromatic compounds (except for aromatic amino acids; Shen et al 2012) due to rapid degradation of the products of interest. However, C. glutamicum can be easily modified genetically and a toolbox for the high-level expression of heterologous genes originating from other organisms, has become available, and is based on a set of strong and inducible promoters (Eggeling and Bott 2005; Pátek and Nešvera 2013; Kortmann et al 2015).…”

Molecular characterization of a eukaryotic-like phenol hydroxylase from <i>Corynebacterium glutamicum</i>

“…This newly defined amino acid production processes provide an alternative pathway in bioremediation/bioconversion of phenolic pollutants in C. glutamicum. Although most of the pathways and enzymes involved in the assimilation of aromatic compounds have been characterized in C. glutamicum (Shen et al, 2005a(Shen et al, , 2012, no functional or biochemical information about phenol hydroxylase in the genus Corynebacterium has been reported so far. In this paper, we have biochemically identified the gene phe encoding a single-component, eukaryote-like phenol hydroxylase in C. glutamicum.…”