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The present paper is a systematic, comparative study on the reconstitution of an apocytochrome b.sub.6 purified from a heterologous system using a detergent-free method and reconstitution into liposomes performed using three different detergents: SDS, Triton X-100 and DM, and two methods of detergent removal by dialysis and using Bio-Beads. The product size, its distribution and zeta potential, and other parameters were monitored throughout the process. We found that zeta potential of proteoliposomes is correlated with reconstitution efficiency and, as such, can serve as a quick and convenient quality control for reconstitution experiments. We also advocate using detergent-free protein purification methods as they allow for an unfettered choice of detergent for reconstitution, which is the most crucial factor influencing the final product parameters.

Detergents are indispensable for membrane protein (MP) research, yet innovative designs are needed to meet the diverse requirements of MPs. Herein, anthracene‐bridged detergents (ABDs) are presented, featuring a curved anthracene‐based scaffold with a hydrophobic core and hydrophilic exterior. The modular synthesis of ABDs facilitates a systematic exploration of their structure‐property relationships. Evaluation across representative G protein‐coupled receptors demonstrates superior or comparable stabilization to conventional detergents. Notably, PP‐ABD maintains complete homogeneity of A2AAR after heat shock and exhibits strong potential for electron microscopy applications. This study establishes ABDs as versatile and effective tools for MP research, offering valuable insights into the rational design of next‐generation detergents. Anthracene‐bridged detergents (ABDs) are introduced as facial amphiphiles with a rigid, tunable architecture. Evaluations across representative G protein‐coupled receptors demonstrate that ABDs offer stabilization performance comparable or superior to conventional detergents. Notably, PP‐ABD maintains A2AAR homogeneity after heat stress and supports electron microscopy analysis, highlighting the potential of ABDs in membrane protein research and detergent design.

This work describes a novel extracellular lipolytic carboxylester hydrolase named FAL, with lipase and phospholipase A 1 (PLA 1 ) activity, from a newly isolated filamentous fungus Ascomycota CBS strain, identified as Fusarium annulatum Bunigcourt. FAL was purified to about 62-fold using ammonium sulphate precipitation, Superdex ® 200 Increase gel filtration and Q-Sepharose Fast Flow columns, with a total yield of 21%. The specific activity of FAL was found to be 3500 U/mg at pH 9 and 40°C and 5000 U/mg at pH 11 and 45°C, on emulsions of triocanoin and egg yolk phosphatidylcholine, respectively. SDS-PAGE and zymography analysis estimated the molecular weight of FAL to be 33 kDa. FAL was shown to be a PLA 1 with a regioselectivity to the sn -1 position of surface-coated phospholipids esterified with α-eleostearic acid. FAL is a serine enzyme since its activity on triglycerides and phospholipids was completely inhibited by the lipase inhibitor Orlistat (40 μM). Interestingly, compared to Fusarium graminearum lipase (GZEL) and the Thermomyces lanuginosus lipase (Lipolase ® ), this novel fungal (phospho)lipase showed extreme tolerance to the presence of non-polar organic solvents, non-ionic and anionic surfactants, and oxidants, in addition to significant compatibility and stability with some available laundry detergents. The analysis of washing performance showed that it has the capability to efficiently eliminate oil-stains. Overall, FAL could be an ideal choice for application in detergents.

In the era of COVID-19, concerns about and consumption of soaps and detergents have increased. The environmental effects, along with their direct impacts on the human body, are being simultaneously considered to ensure safety and support healthy living. Natural soap compounds are considered readily biodegradable and unlikely to produce hazardous waste, while artificial detergents are composed of synthetic surfactants, plasticizers, binders, and additives. This study aimed to investigate representative natural soap compounds consisting of fatty acid salts and compare them with synthetic detergents, such as sodium dodecylbenzene sulfonate (SDB) and sodium lauryl sulfate (SLS). Environmental assays recommended by the OECD, as well as human keratinocyte assays for toxicity and biodegradability, were utilized. The major components of natural soap were found to be less toxic and more biodegradable in aquatic environments—assessed using algae, crustaceans, and fish—compared to synthetic detergents. Additionally, in the human keratinocyte assay, natural soap compounds were significantly less toxic and demonstrated higher viability than SLS after a 48 h culture and a 5 min exposure. The half-maximal inhibitory concentration (IC 50 ) obtained from the viability assay revealed values of 7.82 mM for potassium laurate (C12K), 7.56 mM for potassium oleate (C18:1K), and 0.604 mM for SLS. Therefore, natural soap appears to be valuable due to its lower toxicity, greater biodegradability in aquatic environments, enhanced safety for human cells, and potential efficiency in clinical applications.

[This corrects the article DOI: 10.1371/journal.pone.0153436.].

Protein stability in detergent or membrane-like environments is the bottleneck for structural studies on integral membrane proteins (IMP). Irrespective of the method to study the structure of an IMP, detergent solubilization from the membrane is usually the first step in the workflow. Here, we establish a simple, high-throughput screening method to identify optimal detergent conditions for membrane protein stabilization. We apply differential scanning fluorimetry in combination with scattering upon thermal denaturation to study the unfolding of integral membrane proteins. Nine different prokaryotic and eukaryotic membrane proteins were used as test cases to benchmark our detergent screening method. Our results show that it is possible to measure the stability and solubility of IMPs by diluting them from their initial solubilization condition into different detergents. We were able to identify groups of detergents with characteristic stabilization and destabilization effects for selected targets. We further show that fos-choline and PEG family detergents may lead to membrane protein destabilization and unfolding. Finally, we determined thenmodynamic parameters that are important indicators of IMP stability. The described protocol allows the identification of conditions that are suitable for downstream handling of membrane proteins during purification.

Advanced developments in the field of enzyme technology have increased the use of enzymes in industrial applications, especially in detergents. Enzymes as detergent additives have been extensively studied and the demand is considerably increasing due to its distinct properties and potential applications. Enzymes from microorganisms colonized at various geographical locations ranging from extreme hot to cold are explored for compatibility studies as detergent additives. Especially psychrophiles growing at cold conditions have cold-active enzymes with high catalytic activity and their stability under extreme conditions makes it as an appropriate eco-friendly and cost-effective additive in detergents. Adequate number of reports are available on cold-active enzymes such as proteases, lipases, amylases, and cellulases with high efficiency and exceptional features. These enzymes with increased thermostability and alkaline stability have become the premier choice as detergent additives. Modern approaches in genomics and proteomics paved the way to understand the compatibility of cold-active enzymes as detergent additives in broader dimensions. The molecular techniques such as gene coding, amino acid sequencing, and protein engineering studies helped to solve the mysteries related to alkaline stability of these enzymes and their chemical compatibility with oxidizing agents. The present review provides an overview of cold-active enzymes used as detergent additives and molecular approaches that resulted in development of these enzymes as commercial hit in detergent industries. The scope and challenges in using cold-active enzymes as eco-friendly and sustainable detergent additive are also discussed.

Among the different contaminants, detergent as an important pollutant has serious risks to natural ecosystems. Furthermore, detergents can pass into the wastewater treatment plants and have bad effect on their performance. They are part of human life and consumed for different aims especially hygienic purposes. Therefore, detergent components can enter to soil and water bodies from different sources. Detergents affect fauna and flora, and they have direct and indirect effects on ecosystems. Eutrophication, foaming, and altering parameters such as temperature, salinity, turbidity, and pH are more important, and their effects need to be managed and controlled. Researchers confirmed that aerobic processes are able to degrade the most of detergents but anaerobic degradation is not possible because of restricted metabolic pathways and toxicity of them. Therefore, production of environment-friendly detergent is an important issue around the world. Graphical abstract

The influence of poly(ethylene glycol) (PEG) polymers H–(O–CH2–CH2)p–OH with different average molecular sizes p on the micelle formation of n-alkyl-β-D-maltoside detergents with the number of carbon atoms in the alkyl chain ranging from 10 to 12 is investigated with the aim to learn more about the detergent behavior under conditions suitable for the crystallization of the photosynthetic pigment–protein complex photosystem II. PEG is shown to increase the critical micelle concentration (CMC) of all three detergents in the crystallization buffer in a way that the free energy of micelle formation increases linearly with the concentration of oxyethylene units (O–CH2–CH2) irrespective of the actual molecular weight of the polymer. The CMC shift is modeled by assuming for simplicity that it is dominated by the interaction between PEG and detergent monomers and is interpreted in terms of an increase of the transfer free energy of a methylene group of the alkyl chain by 0.2 kJ mol−1 per 1 mol L−1 increase of the concentration of oxyethylene units at 298 K. Implications of this effect for the solubilization and crystallization of protein–detergent complexes as well as detergent extraction from crystals are discussed.

Low-temperature laundry washing prompted the formulation of a new biobased detergent that meets sustainability criteria. A soapnut extract conferred good cleaning performance on the standard soiling agents EMPA 101 and EMPA 114 but showed rather weak performance on EMPA 116 and EMPA 160. The results indicated the good disinfection properties of the soapnut extract–Carvacrol emulsion (>6 log CFU/carriers), whereas the commercial detergent and sole soapnut extract were less effective. Comparable results were observed for cross-contamination assessment and wash water, whereas total elimination was achieved only for the soapnut extract–Carvacrol emulsion. We demonstrated significantly decreased water surface tension for all three compounds. The microorganism cell membrane integrity assessment showed the highest number of dead cells on cotton carriers washed with the soapnut extract–Carvacrol emulsion. All this indicated that the newly formulated biobased laundry detergent made of soapnut extract and Carvacrol could effectively remove standard soiling agents and ensure good disinfection.