Are microbial biosurfactants actually only surfactants?

Baccile, Niki

doi:10.1016/j.cocis.2023.101747

Cited by 5 publications

(2 citation statements)

References 69 publications

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“…Bioemulsifiers are a class of substances whose actions are intimately tied to their chemical composition ( 15 ). Furthermore, bioemulsifiers present a versatile and environmentally friendly substitute to synthetic emulsifiers, with applications in a variety of industrial sectors, including food, medicine, and cosmetics ( 16 ). The high molecular weight and hydrophobicity of proteins influence how well they interact with cell membranes and how cytotoxic they are ( 17 , 18 ).…”

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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“…Recent biotechnological advancements have made some of these natural products economically affordable. However, it is becoming increasingly clear that biosurfactants present a peculiar behavior in solution which determines different performance profiles with respect to conventional amphiphiles [20,21], thus pointing out that the design of innovative sustainable formulations requires the physico-chemical features of the specific components and their mixtures to be carefully characterized.…”

Section: Introductionmentioning

confidence: 99%

Surface and Aggregation Properties of Rhamnolipids in Water–Bioethanol Mixtures: A Step toward Green Formulation Design

Esposito,

Taddeo,

Russo

et al. 2024

Surfaces

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Water–ethanol mixtures are largely exploited for many different applications, from industrial processes to pharmaceutical formulations. Surfactants are often added to tune their interfacial properties. Sustainability concerns require redesigning such blends to minimize their environmental impact. A successful approach is to replace synthetic oil-based components with affordable unpurified bio-derived alternatives. In this respect, we have characterized aqueous mixtures of bioethanol, obtained by the fermentation of algae, and rhamnolipids, biosurfactants of microbial origin. The physico-chemical characterization of water–bioethanol binary mixtures in terms of refractive index, density, viscosity, and surface tension indicates that bioethanol behaves like pure ethanol with negligible effects of impurities. Analysis of tensiometric titrations shows that, at bioethanol contents higher than 20–30% bioethanol mass percent, rhamnolipid aggregation is impaired, whereas surface adsorption at the water–air interface remains poorly affected. Overall, bio-derived components can be proposed as a promising alternative to oil-derived chemicals in eco-sustainable formulations.

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Myelin figures from microbial glycolipid biosurfactant amphiphiles

Roy,

Chaleix,

Parikh

et al. 2024

J Surfact & Detergents

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Myelin figures (MFs)—cylindrical lyotropic liquid crystalline structures consisting of concentric arrays of bilayers and aqueous media—arise from the hydration of the bulk lamellar phase of many common amphiphiles. Prior efforts have concentrated on the formation, structure, and dynamics of myelin produced by phosphatidylcholine (PC)‐based amphiphiles. Here, we study the myelinization of glycolipid microbial amphiphiles, commonly addressed as biosurfactants, produced through the process of fermentation. The hydration characteristics (and phase diagrams) of these biological amphiphiles are atypical (and thus their capacity to form myelin) because unlike typical amphiphiles, their molecular structure is characterized by two hydrophilic groups (sugar, carboxylic acid) on both ends with a hydrophobic moiety in the middle. We tested three different glycolipid molecules: C18:1 sophorolipids and single‐glucose C18:1 and C18:0 glucolipids, all in their nonacetylated acidic form. Neither sophorolipids (too soluble) nor C18:0 glucolipids (too insoluble) displayed myelin growth at room temperature (RT, 25°C). The glucolipid C18:1 (G‐C18:1), on the other hand, showed dense myelin growth at RT below pH 7.0. Examining their growth rates, we find that they display a linear (L, myelin length; t, time) growth rate, suggesting ballistic growth, distinctly different from the dependence, characterizing diffusive growth such as what occurs in more conventional phospholipids. These results offer some insight into lipidic mesophases arising from a previously unexplored class of amphiphiles with potential applications in the field of drug delivery.

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Are microbial biosurfactants actually only surfactants?

Cited by 5 publications

References 69 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

Surface and Aggregation Properties of Rhamnolipids in Water–Bioethanol Mixtures: A Step toward Green Formulation Design

Myelin figures from microbial glycolipid biosurfactant amphiphiles

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