ArticleApplied and environmental microbiology2001
Emulsifying activities of purified Alasan proteins from Acinetobacter radioresistens KA53.
Article in Applied and environmental microbiology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed.
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- Natural surfactant mediated bioremediation approaches for contaminated soil.RSC advances · 2023Review
- Elaboration and Characterization of a New Heavy Metal Sensor Functionalized by Extracellular Polymeric Substances Isolated from a Tunisian Thermophilic Microalga StrainSensors (Basel, Switzerland) · 2023Article
- Biosurfactant: an emerging tool for the petroleum industries.Frontiers in microbiology · 2023Review
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- Surface-Active Compounds Produced by Microorganisms: Promising Molecules for the Development of Antimicrobial, Anti-Inflammatory, and Healing Agents.Antibiotics (Basel, Switzerland) · 2022Review
- Production and Characterization of a Bioemulsifier Derived from Microorganisms with Potential Application in the Food Industry.Life (Basel, Switzerland) · 2022Review
- Structural and mechanical characterization of biofilm-associated bacterial polymer in the emulsification of petroleum hydrocarbon.3 Biotech · 2021Article
- New Provisional Function of OmpA frommSystems · 2021Article
- Biosurfactants and Their Applications in the Oil and Gas Industry: Current State of Knowledge and Future Perspectives.Frontiers in bioengineering and biotechnology · 2021Review
- Production and potential biotechnological applications of microbial surfactants: An overview.Saudi journal of biological sciences · 2021Review
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- Heterologous Expression of Sfp-Type Phosphopantetheinyl Transferase is Indispensable in the Biosynthesis of Lipopeptide Biosurfactant.Molecular biotechnology · 2019Article
- Designer bioemulsifiers based on combinations of different polysaccharides with the novel emulsifying esterase AXE from Bacillus subtilis CICC 20034.Microbial cell factories · 2019Article
- Complete Genome Sequence of Hydrocarbon-Degrading Halotolerant Acinetobacter radioresistens DD78, Isolated from the Aconcagua River Mouth in Central Chile.Microbiology resource announcements · 2019Article
- Characterization of a novel bioemulsifier from Pseudomonas stutzeri.World journal of microbiology & biotechnology · 2017Article
- Characterization of novel Acidobacteria exopolysaccharides with potential industrial and ecological applications.Scientific reports · 2017Article
- Rhamnolipids Produced by IndigenousFrontiers in microbiology · 2016Article
- Biodegradation of diesel oil by a novel microbial consortium: comparison between co-inoculation with biosurfactant-producing strain and exogenously added biosurfactants.Environmental science and pollution research international · 2015Article
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The bioemulsifier of Acinetobacter radioresistens KA53, referred to as alasan, is a high-molecular-weight complex of polysaccharide and protein. The emulsifying activity of the purified polysaccharide (apo-alasan) is very low. Three of the alasan proteins were purified by preparative sodium dodecyl sulfate-polyacrylamide gel electrophoresis and had apparent molecular masses of 16, 31, and 45 kDa. Emulsification assays using the isolated alasan proteins demonstrated that the active components of the alasan complex are the proteins. The 45-kDa protein had the highest specific emulsifying activity, 11% higher than the intact alasan complex. The 16- and 31-kDa proteins gave relatively low emulsifying activities, but they were significantly higher than that of apo-alasan. The addition of the purified 16- and 31-kDa proteins to the 45-kDa protein resulted in a 1.8-fold increase in the specific emulsifying activity and increased stability of the oil-in-water emulsion. Fast-performance liquid chromatography analysis indicated that the 45-kDa protein forms a dimer in nondenaturing conditions and interacts with the 16- and 31-kDa proteins to form a high-molecular-mass complex. The 45-kDa protein and the three-protein complex had substrate specificities for emulsification and a range of pH activities similar to that of alasan. The fact that the purified proteins are active emulsifiers should simplify structure-function studies and advance our understanding of their biological roles.
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