Facultative anaerobic conversion of lignocellulose biomass to new bioemulsifier by thermophilic Geobacillus thermodenitrificans NG80-2

Li, Mingchang; Yu, Jiaqi; Cao, Lei; Yin, Yujun; Su, Zhaoying; Chen, Shuai; Li, Guoqiang; Ma, Ting

doi:10.1016/j.jhazmat.2022.130210

Cited by 8 publications

(4 citation statements)

References 56 publications

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“…AlnA, a 349 amino acid protein produced by the environmental strain Acinetobacter radioresistens strain KA53, has obvious sequence similarity with OmpA from Escherichia coli and OprF, the major porin from Pseudomonas aeruginosa , and is responsible for the emulsifying activity of the Alasan complex ( 10 ). Due to their practical significance, research on developing harmless and ecologically friendly bioactive compounds, particularly bioemulsifiers, has increased dramatically in recent years ( 11 – 14 ). Bioemulsifiers are a class of substances whose actions are intimately tied to their chemical composition ( 15 ).…”

Section: Introductionmentioning

confidence: 99%

Unveiling the structure-emulsifying function relationship of truncated recombinant forms of the SA01-OmpA protein opens up a new vista in bioemulsifiers

Mohseni Sani,

Talaee,

Akbari

et al. 2024

Microbiol Spectr

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The emulsifying ability of SA01-OmpA (outer membrane protein A from Acinetobacter sp. SA01) was found to be constrained by challenges like low production efficiency and high costs associated with protein recovery from E. coli inclusion bodies, as described in our previous study. The present study sought to benefit from the advantages of the targeted truncating of SA01-OmpA protein, taking into account the reduced propensity of protein expression as inclusion bodies and cytotoxicity. Here, the structure and activity relationship of two truncated recombinant forms of SA01-OmpA protein was unraveled through a hybrid approach based on experimental data and computational methodologies, representing an innovative bioemulsifier with advantageous emulsifying activity. The recombinant truncated SA01-OmpA variants were cloned and heterologously expressed in E. coli host cells and subsequently purified. The results showed increased emulsifying activity of N-terminally truncated SA01-OmpA (NT-OmpA) compared to full-length SA01-OmpA. Molecular dynamics (MD) simulations analysis demonstrated a direct correlation between the C-terminally truncated SA01-OmpA (CT-OmpA) and its expression as inclusion bodies. Analysis of the structure-activity relationship of truncated variants of SA01-OmpA revealed that, compared to the full-length protein, deletion of the β-barrel portion from the N-terminal of SA01-OmpA increased the emulsifying activity of NT-OmpA while lowering its expression as inclusion bodies. Contrary to the full-length protein, the N-terminally truncated SA01-OmpA was not as cytotoxic, according to the MTT assay, FCM analysis, and AO/EB staining. The findings of this extensive study advance our knowledge of SA01-OmpA at the molecular level as well as the design and development of efficient bioemulsifiers. IMPORTANCE Previous research (Shahryari et al. 2021, mSystems 6: e01175-20) introduced and characterized the SA01-OmpA protein as a multifaceted protein with a variety of functions, including maintaining cellular homeostasis under oxidative stress conditions, biofilm formation, outer membrane vesicles (OMV) biogenesis, and beneficial emulsifying capacity. By truncating the SA01-OmpA protein, the current study presents a unique method for developing protein-type bioemulsifiers. The findings indicate that the N-terminally truncated SA01-OmpA (NT-OmpA) has the potential to fully replace full-length SA01-OmpA as a novel bioemulsifier with significant emulsifying activity. This study opens up a new frontier in bioemulsifiers, shedding light on a possible relationship between the structure and activity of SA01-OmpA truncated forms.

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Section: Introductionmentioning

confidence: 99%

Unveiling the structure-emulsifying function relationship of truncated recombinant forms of the SA01-OmpA protein opens up a new vista in bioemulsifiers

Mohseni Sani,

Talaee,

Akbari

et al. 2024

Microbiol Spectr

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“…Bioemulsifiers produced by the facultative anaerobic bacterium G. thermodenitrificans NG80-2 proved to be polysaccharide–protein complexes . Detailed mechanisms of oxidation and degradation of hydrocarbons by Geobacillus sp have been reported.…”

Section: Introductionmentioning

confidence: 99%

“… 21 Bioemulsifiers produced by the facultative anaerobic bacterium G. thermodenitrificans NG80-2 proved to be polysaccharide–protein complexes. 22 Detailed mechanisms of oxidation and degradation of hydrocarbons by Geobacillus sp have been reported. However, there are only four reports that Geobacillus sp can produce biosurfactants, and the structural information of biosurfactants is scarce.…”

Section: Introductionmentioning

confidence: 99%

Structural Diversity of the Lipopeptide Biosurfactant Produced by a Newly Isolated Strain, Geobacillus thermodenitrifcans ME63

Li,

Liu,

Zhou

et al. 2023

ACS Omega

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The genus Geobacillus is active in degradation of hydrocarbons in thermophilic and facultative environments since it was first reported in 1920. Here, we report a new strain, Geobacillus thermodenitrificans ME63, isolated from an oilfield with the ability of producing the biosurfactant. The composition, chemical structure, and surface activity of the biosurfactant produced by G. thermodenitrificans ME63 were investigated by using a combination of the high-performance liquid chromatography, time-of-flight ion mass spectrometry, and surface tensiometer. The biosurfactant produced by strain ME63 was identified as surfactin with six variants, which is one of the representative family of lipopeptide biosurfactants. The amino acid residue sequence in the peptide of this surfactin is N-Glu → Leu → Leu → Val → Leu → Asp → Leu-C. The critical micelle concentration (CMC) of the surfactin is 55 mg L −1 , and the surface tension at CMC is 35.9 mN m −1 , which is promising in bioremediation and oil recovery industries. The surface activity and emulsification properties of biosurfactants produced by G. thermodenitrificans ME63 showed excellent resistance to temperature changes, salinity changes, and pH changes.

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“…EPS of cyanobacteria have been reported to be closely associated with colony formation and development, which can further protect the bacteria from unfavorable environments [5]. In fact, for strains that can produce EPS, the main factors affecting the production of EPS include the culture substrate (e.g., carbon and nitrogen sources) [6], the growth conditions (e.g., temperature, pH, and oxygen supply) [7], and trace heavy metal ions (e.g., Cu 2+ , Fe 3+ ) [8]. As far as the same strain is concerned, the temperature change has a significant effect on the polysaccharide content in EPS, CO 2 can affect the protein content in EPS, the sugar yield in EPS of the bacterium is the highest at the optimum pH, the protein content in EPS is positively correlated with the pH value within the general environmental pH range, and the amino acid yield in EPS is positively correlated with the growth of the bacteria.…”

Section: Introductionmentioning

confidence: 99%

Analysis of the Effects of Surfactants on Extracellular Polymeric Substances

Zhang,

Zheng,

Lai

2023

Processes

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Reservoirs after chemical flooding usually have residual chemicals, which can affect the driving effect of subsequent microbial drives. Among them, the effect of surfactants on the metabolites of oil-recovering bacteria is the most obvious. Therefore, this paper investigates the influence mechanism of sodium dodecyl sulfate (SDS) on the nature and structure of Extracellular Polymeric Substances (EPS) produced by metabolism of Enterobacter cloacae, through a variety of characterization to analysis the components and structure of EPS under SDS stress. The results showed that Enterobacter cloacae was identified as a glycolipid-producing strain, the main components of EPS were polysaccharides and proteins. The polysaccharide composition (%: w/w) was glucosamine, 37.2; glucose, 31.5; rhamnose, 26.3; xylose, 1.7; and unidentified sugar, 3.3; and the main component of proteins was polyglutamic acid. EPS under the stress of SDS showed an increase in the content of functional groups such as -C=O and -COOH and an increase in the cellular particle size, and production of EPS increased by 10.69 × 103 mg/L when the SDS concentration was 2.5 × 102 mg/L; 3D-EEM results showed that the components of all three types of EPS The 3D-EEM results showed that all three types of EPS fractions contained tryptophan and protein-like substances, humic acid-like substances were only distributed in the solubilized extracellular polymers (SL-EPS), and aromatic proteins were only present in the loosely bound type (LB-EPS) and tightly bound type (TB-EPS). In addition, the peaks representing humic-like substances showed a blue shift, indicating that SDS had the greatest effect on SL-EPS. This study provides a guidance for refining the mechanism of strain EPS response to reservoir residual surfactant SDS, and provides a more comprehensive and in-depth understanding of surfactant-protein interactions.

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Facultative anaerobic conversion of lignocellulose biomass to new bioemulsifier by thermophilic Geobacillus thermodenitrificans NG80-2

Cited by 8 publications

References 56 publications

Unveiling the structure-emulsifying function relationship of truncated recombinant forms of the SA01-OmpA protein opens up a new vista in bioemulsifiers

Unveiling the structure-emulsifying function relationship of truncated recombinant forms of the SA01-OmpA protein opens up a new vista in bioemulsifiers

Structural Diversity of the Lipopeptide Biosurfactant Produced by a Newly Isolated Strain, Geobacillus thermodenitrifcans ME63

Analysis of the Effects of Surfactants on Extracellular Polymeric Substances

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