DOCSLIB.ORG

Characterization of Surfactin-Like Cyclic Depsipeptides Synthesized By

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
Characterization of Surfactin-Like Cyclic Depsipeptides Synthesized By Characterization of Surfactin-like Cyclic Depsipeptides Synthesized by Bacillus pumilus from Ascidian Halocynthia aurantium Natalie I. Kalinovskaya,1* Tatyana A. Kuznetsova,1 Elena P. Ivanova,1** Ludmila A. Romanenko,1 Valery G. Voinov,1 Felix Huth,2 and Hartmut Laatsch2 1Pacific Institute of Bio-organic Chemistry of the Far-Eastern Branch of the Russian Academy of Sciences, 159 pr. 100-Let Vladivostoku, 690022 Vladivostok, Russian Federation 2Department of Organic Chemistry, University of Goettingen, Tammanstr. 2. D-37077 Goettingen. Germany * Corresponding author; telephone: +7(423 2)311168; fax: +7(423 2)314050; e-mail: [email protected] ** Present address: Swinburne University of Technology, 533-545 Burwood Rd, Hawthorn, 33122, Melbourne, Australia Running title: Surfactin-like cyclic depsipeptides from Bacillus pumilus Key words: Surfactin analog, cyclic depsipeptides, Bacillus pumilus, ascidian Halocynthia aurantium Summary: A marine bacterium (KMM 1364), identified as Bacillus pumilus, was isolated from the surface of ascidian Halocynthia aurantium. Structural analysis revealed that the strain KMM 1364 produced a mixture of lipopeptide surfactin analogs with major components ranging in size from molecular masses of 1035, 1049, 1063 and 1077. The variation in molecular weight represents changes in the number of methylene groups in the lipid and/or peptide portion of the compounds. Structurally, these lipopeptides differ from surfactin in the subsitution of the valine residue in position 4 by leucine, and have been isolated as two C-terminal variants, with valine or isoleucine in position 7. As constituents of the lipophilic part of the peptides, only β-hydroxy-C15-, β-hydroxy-C16- and a high amount of β-hydroxy-C17 fatty acid were determined. INTRODUCTION Biosurfactants comprise a structurally diverse group of surface-active compounds produced by microorganisms. Increasing interest to these substances is explained by the wide range of their biotechnological applications including enhanced oil recovery due to reduction of surface and interfacial tensions in aqueous solution and hydrocarbon mixtures (Singer, 1985), deemulsification (Cairns et al., 1982; Mulligan, and Gibbs, 1993), health care (Muller- Hurting et al., 1993), and food-processing industries (Velikonja and Kosaric, 1993). Microbial surfactants are of particular interest because they, in contrast to synthetic analogs, are biodegradable and can be produced through fermentation on renewable substrates. The biosurfactant-producing microorganisms belong to different taxa (Desai and Banat, 1997). However, among Gram-positive spore-forming bacteria only a few species of the genus Bacillus (i.e. B. subtilis and B. licheniformis), Brevibacillus brevis (former Bacillus brevis) and Paenibacillus polymyxa (former Bacillus polymyxa) are known producers of cyclic lipopeptides including decapeptide antibiotics (gramicidins) and lipopeptides antibiotics (polymyxins) with surface-active and chelating properties. The cyclic lipopeptide surfactin from B. subtilis was intensively structurally studied in respect to its biotechnological and pharmacological applications (Cooper et al., 1981; Vollenbroich et al., 1997). A surfactin like lipopeptide surfactant, lichenisin, is produced by B. licheniformis JF-2 and was patented as an enhanced oil recowery agent (McInerney et al., 1985). The structure, molecular genetics, properties, and production of biosufactants have been reviewed recently (Desai and Banat, 1997; Sullivan, 1998). Over the last decade we studied the biologically active secondary metabolites produced by marine bacteria isolated from both seawater and an array of marine invertebrates (Elyakov et al., 1996). Previously we reported about cyclic depsipeptides found in B. pumilus isolated from the sponge Ircinia sp. (Kalinovskaya et al., 1995). This paper describes the isolation and structure elucidation of one of the isoforms of surfactin produced by B. pumilus, isolated from surface of cuticula of the ascidian Halocynthia aurantium, common inhabitant of the Sea of Japan. MATERIALS AND METHODS Instruments UV spectra were recorded on a Specord UV-VIS M 40 spectrophotometer (Carl Zess Jena) in methanol. IR spectra were obtained on a Specord M-82 (Carl Zeiss Jena) spectrometer in CHCl3. The amino acid composition was determined on an amino acid analyzer (Biotronic LC 2000, Sweden, using DS-6A resin column) after total hydrolysis of the lipopeptides in 5.6 N HCl at 105oC for 48 h. NMR spectra were recorded on a Bruker AM 500 spectrometer (500 and 125.7 MHz for 1H and 13C, respectively, using TMS as the internal reference). The native peptides were analyzed by fast atom bombardment mass spectrometry (FABMS) on a Finnigan 95 A mass spectrometer, using a 3-nitro-benzaldehyde matrix (3-NBA). Positive and negative ions were detected. Bacterial strain The strain Bacillus pumilus KMM 1364 was isolated from the ascidian Halocynthia aurantium in August 1989, the Troitza Bay, Gulf of Peter the Great (Romanenko et al., 2001). This strain was grown on a rotary shaker (120 rpm) in 1 L Erlenmeyer flasks containing 200 ml of the medium (g/L): K2HPO4 (0.07), NH4Cl (1.0 ), yeast extract (5.0 ), FeSO4 (0.025 ), 1 M Tris buffer (20 ml), artificial sea water (200 ml), distilled water (800 ml), pH adjusted to 7.5, during 20 h at 24-26oC. Isolation of Depsipeptides 1, 2, 6-8 The cells (from 6 L of culture medium) were collected by centrifugation at 5000 g for 40 min and suspended in water (50 ml), frozen and destructed by ultrasonic treatment. The suspension was extracted with a mixture of chloroform-methanol (3:1) and the organic phase evaporated to dryness. Column chromatography of the сrude extract (402 mg) on a silica gel column (40/100 µ, Chemapol, Czechoslovakia, 1.5x20 cm) with solvents of increasing polarity gave the following fractions: hexane-ethyl acetate 3:1 (F1-F4); 2:1 (F5-F7); 1:1 (F8-F9); 1:3 (F10-F11); ethyl acetate (F12-F14); ethyl acetate-MeOH, 95:5 (F15-F17); 9:1 (F18-F19); 1:1 (F20-F21). Thin-layer Chromatography (TLC) The mixture of peptides was analyzed by TLC on silica gel 5/40 µ (Czechoslovakia) in a chloroform-methanol-water mixture (65:25:4, v/v/v), the zones were visualized using the chlorine-tolidine reaction. High Pressure Liquid Chromatography (HPLC) The combined fractions F10-F17 were separated by reversed phase HPLC with a Waters instrument (USA) on a Separon SGX column (C18, 5 µ, 4.0 i. d. x 250 mm, acetonitrile-0.01% TFA/H2O 86:14, flow rate 1.5 ml/min, detection by UV absorption at 214 nm). The individual depsipeptides 1, 2, and 6-8 were obtained at retention times of t1=16.2, t2=20.7, t6/7=29.7, and t8=37.6 min. NMR Data of Peptide 1 ([D6]-Acetone) 13С NMR: 173.90 (Cδ), 173.90 (CO), 172.15 (2-CO), 171.74 (CO), 171.60 (CO), 171.14 (CO), 170.66 (Cγ), 170.25 (CO), 57.45 (α-CH), 52.40 (α-CH), 51.75 (α-CH), 51.34 (α-CH), 50.83 (α- CH), 49.81 (α-CH), 48.54 (α-CH), 40.68 (β-CH2), 39.0 (β-CH2), 38.43 (2 β-CH2), 35.95 (β- CH2), 31.23 (β-CH2), 29.36 (β-CH), 28.57 (γ-CH2), 27.32 (γ-CH), 24.22 (γ-CH), 24.20 (γ-CH), 24.09 (γ-CH), 22.92 (δ1-CH3), 22.88 (δ2-CH3), 22.81 (δ1-CH3), 22.64 (δ2-CH3), 21.78 (δ1-CH3), 21.63 (δ2-CH3), 21.44 (δ1-CH3), 21.39 (δ2-CH3), 19.01 (γ1-CH3), 18.1 (γ2-CH3); alkyl chain: 169.63 (C-1), 41.06 (C-2, CH2), 71.72 (C-3, CH), 33.42 (C-4, CH2), 26.70 (C-5, CH2), 29.24- 28.82 (C-6-C-10, CH2), 30.04 (iso, C-11, CH2), 29.24 (anteiso, C-11, CH2), 38.81 (iso, C-12, CH2), 33.69 (anteiso, C-12, CH), 27.32 (iso, C-13, CH), 29.24 (anteiso, C-13, CH2), 22.42 (iso, 1 C-14, CH3), 11.09 (anteiso, C-14, CH3), 22.42 (iso, 13-Met), 19.16 (anteiso, 12-Met). H NMR: 4.71, 4.52, 4.37, 4.25, 4.12, 4.06 (2H, αCH), 2.49 t, 2.28, 1.60-1.46 (8H), 2.88 d, 2.49, 2.64 d (βCH); 1.88-1.60 (4H), 1.60-1.46 (2H, γCH); 1.02-0.8 (10 CH3); alkyl chain: 2.69, 2.15 (C-2, H), 5.33 (C-3, H), 1.60-1.46 (C-4, H), 1.30-1.15 (CH2)5-12, 1.15 (C-13), 1.02-0.8 (C-14-15). NH: 8.14 (d, J=6.0), 7.86 (d, J=7.2), 7.79 (t, 2H, J=7.2), 7.72 (d, J=8.5), 7.60 (d, J=6.0), 7.34 (d, J=8.0). NMR Data of Peptide 2 ([D6]-DMSO) 13С NMR: 173.89 ( CO), 173.89 (Cδ),-172.06 (2 CO), 171.63 (Cγ), 171.55 (CO), 171.09 (CO), 170.61 (CO), 170.13 (CO), 56.43 (α-CH), 52.29 (α-CH), 51.78 (α-CH), 51.71 (α-CH), 51.30 (α-CH), 50.74 (α-CH), 49.77 (α-CH), 40.55 (β-CH2), 39.44 (β-CH2), 38.39 (2 β-CH2), 35.91 (β- CH2), 35.74 (β-CH), 30.00 (β-CH2), 27.28 (γ-CH), 27.12 (γ-CH2), 24.50 (γ1-CH2), 24.19 (γ-CH), 24.16 (γ-CH), 24.07 (γ-CH), 22.89 (δ1-CH3), 22.86 (δ2-CH3), 22.81 (CH3), 22.61 (CH3), 21.81 ((δ1-CH3), 21.62 (δ2-CH3), 21.44 (δ1-CH3), 21.31 (δ2-CH3), 15.41 (γ2-CH3), 10.95 (δ-CH3); alkyl chain: 169.54 (C-1), 41.05 (C-2, CH2), 71.74 (C-3, CH), 33.26 (C-4, CH2), 26.66 (С-5, CH2), 29.20-28.78 [(C-6-C-10), CH2], 29.20 (iso, C-11, CH2), 28.52 (anteiso, C-11, CH2), 39.00 (iso, C-12, CH2), 33.66 (anteiso, C-12, CH), 27.28 (iso, C-13, CH), 29.26 (anteiso, C-13, CH2), 22.39 1 (iso, C-14, CH3), 11.07 (anteiso, C-14, CH3), 22.39 (iso, 13-Met), 18.98 (anteiso, 12-Met).
Load more

Recommended publications
  • Identification of Novel Surfactin Derivatives from NRPS Modification
    Jiang et al. BMC Microbiology (2016) 16:31 DOI 10.1186/s12866-016-0645-3 RESEARCH ARTICLE Open Access Identification of novel surfactin derivatives from NRPS modification of Bacillus subtilis and its antifungal activity against Fusarium moniliforme Jian Jiang, Ling Gao, Xiaomei Bie*, Zhaoxin Lu, Hongxia Liu, Chong Zhang, Fengxia Lu and Haizhen Zhao Abstract Background: Bacillus subtilis strain PB2-L1 produces the lipopeptide surfactin, a highly potent biosurfactant synthesized by a large multimodular nonribosomal peptide synthetase (NRPS). In the present study, the modules SrfA-A-Leu, SrfA-B-Asp, and SrfA-B-Leu from surfactin NRPS in B. subtilis BP2-L1 were successfully knocked-out using a temperature-sensitive plasmid, pKS2-mediated-based, homologous, recombination method. Results: Three novel surfactin products were produced, individually lacking amino acid Leu-3, Asp-5, or Leu-6. These surfactins were detected, isolated, and characterized by HPLC and LC-FTICR-MS/MS. In comparison with native surfactin, [ΔLeu3]surfactin and [ΔLeu6]surfactin showed evidence of reduced toxicity, while [ΔAsp5]surfactin showed stronger inhibition than native surfactin against B. pumilus and Micrococcus luteus. These results showed that the minimum inhibitory concentration of [ΔLeu6]surfactin for Fusarium moniliforme was 50 μg/mL, such that [ΔLeu6]surfactin could lead to mycelium projection, cell damage, and leakage of nucleic acids and protein. These factors all contributed to stimulating apoptosis in F. moniliforme. Conclusions: The present results revealed that [ΔLeu6]surfactin showed a significant antifungal activity against F. moniliforme and might successfully be employed to control fungal food contamination and improve food safety. Keywords: Surfactin, NRPS, Module deletion, Fusarium moniliforme Background structure peptide chain and possesses a β-hydroxy fatty Fusarium moniliforme mainly contaminates maize, sor- acid chain (typically C13–C16) containing seven amino acids ghum, wheat, cotton, beans, tomatoes, peanuts, bananas, formed by crosslinking [7].
    [Show full text]
  • Surfactin – Novel Solutions for Global Issues
    13 Surfactin – Novel Solutions for Global Issues Gabriela Seydlová, Radomír Čabala and Jaroslava Svobodová Charles University in Prague Czech Republic 1. Introduction The constant demand for new, effective therapeutic agents has triggered intensive research in the field of diverse antimicrobials of natural origin. These compounds are synthesized by all forms of life and have important biomedical and biotechnological properties, and are thus widely considered a potential solution to the growing problem of resistance to conventional antibiotics, fungal infection and life-threatening diseases. Among these molecules, lipopeptides represent a unique class of bioactive secondary metabolites with increasing scientific, therapeutic and biotechnological interest. The principal representative of the anionic lipopeptide family is surfactin, which is produced by bacterium Bacillus subtilis. This most potent known biosurfactant (i.e. surface-active compound of microbial origin), was named surfactin due to its exceptional surface activity. Since its discovery (Arima et al., 1968) and the identification of its molecular structure as a macrolide lipopeptide (Kakinuma et al., 1969) it has been best recognized for its high amhiphilicity and strong tendency for self-aggregation (Ishigami et al., 1995). Due to these characteristics it shows remarkable surface-, interface- and membrane-active properties, resulting in a number of promising biological activities, which are of great relevance in health care and biotechnology. These properties make surfactin a candidate drug for the resolution of a number of global issues in medicine (Banat et al., 2010; Cao et al., 2010), industry (Nitschke & Costa, 2007; Abdel-Mawgoud et al., 2008) and environmental protection (Mulligan, 2009). 2. Structure and physicochemical properties Surfactin (M.W.
    [Show full text]
  • Role of Surfactin from Bacillus Subtilis in Protection Against Antimicrobial Peptides Produced by Bacillus Species
    Role of surfactin from Bacillus subtilis in protection against antimicrobial peptides produced by Bacillus species by Hans André Eyéghé-Bickong BSc. Honours (Biochemistry) February 2011 Dissertation approved for the degree Doctor of Philosophy (Biochemistry) in the Faculty of Science at the University of Stellenbosch Promoter: Prof. Marina Rautenbach Department of Biochemistry University of Stellenbosch ii Declaration By submitting this dissertation electronically, I declare that the entirety of the work contained therein is my own, original work, that I am the sole author thereof (save to the extent explicitly otherwise stated), that reproduction and publication thereof by Stellenbosch University will not infringe any third party rights and that I have not previously in its entirety or in part submitted it for obtaining any qualification. ……………………………………………. ………28/02/2011..…………… Hans André Eyéghé-Bickong Date Copyright©2011 Stellenbosch University All rights reserved iii Summary Antagonism of antimicrobial action represents an alternative survival strategy for cohabiting soil organisms. Under competitive conditions, our group previously showed that surfactin (Srf) produced by Bacillus subtilis acts antagonistically toward gramicidin S (GS) from a cohabiting bacillus, Aneurinibacillus migulanus, causing the loss the antimicrobial activity of GS. This antagonism appeared to be caused by inactive complex formation. This study aimed to elucidate whether the previously observed antagonism of GS activity by Srf is a general resistance mechanism that also extends to related peptides such as the tyrocidines (Trcs) and linear gramicidins (Grcs) from Bacillus aneurinolyticus. Molecular interaction between the antagonistic peptide pairs was investigated using biophysical analytical methods such as electrospray mass spectrometry (ESMS), circular dichroism (CD), fluorescence spectroscopy (FS) and nuclear magnetic resonance (NMR).
    [Show full text]
  • Selection of Sponge-Associated Bacteria with High Potential for The
    www.nature.com/scientificreports OPEN Selection of sponge‑associated bacteria with high potential for the production of antibacterial compounds Riyanti1,2, Walter Balansa3, Yang Liu1, Abha Sharma1, Sanja Mihajlovic4, Christoph Hartwig4, Benedikt Leis4, Frets Jonas Rieuwpassa3, Frans Gruber Ijong3, Heike Wägele5, Gabriele M. König6 & Till F. Schäberle1,4,7* The potential of sponge‑associated bacteria for the biosynthesis of natural products with antibacterial activity was evaluated. In a preliminary screening 108 of 835 axenic isolates showed antibacterial activity. Active isolates were identifed by 16S rRNA gene sequencing and selection of the most promising strains was done in a championship like approach, which can be done in every lab and feld station without expensive equipment. In a competition assay, strains that inhibited most of the other strains were selected. In a second round, the strongest competitors from each host sponge competed against each other. To rule out that the best competitors selected in that way represent similar strains with the same metabolic profle, BOX PCR experiments were performed, and extracts of these strains were analysed using metabolic fngerprinting. This proved that the strains are diferent and have various metabolic profles, even though belonging to the same genus, i.e. Bacillus. Furthermore, it was shown that co‑culture experiments triggered the production of compounds with antibiotic activity, i.e. surfactins and macrolactin A. Since many members of the genus Bacillus possess the genetic equipment for the biosynthesis of these compounds, a potential synergism was analysed, showing synergistic efects between C14‑surfactin and macrolactin A against methicillin‑resistant Staphylococcus aureus (MRSA). Te oceans house highly dynamic and diverse microbiological habitats with an inherent high potential to discover species that are completely new, unique and highly adapted 1.
    [Show full text]
  • Surfactin – a Review on Biosynthesis, Fermentation, Purification and Applications
    N.S. SHALIGRAM and R.S. SINGHAL: Surfactin – A Review, Food Technol. Biotechnol. 48 (2) 119–134 (2010) 119 ISSN 1330-9862 review (FTB-2226) Surfactin – A Review on Biosynthesis, Fermentation, Purification and Applications Nikhil S. Shaligram and Rekha S. Singhal* Food Engineering and Technology Department, Institute of Chemical Technology, Matunga, Mumbai, IN-400 019 India Received: January 28, 2009 Accepted: January 11, 2010 Summary Surfactin, a bacterial cyclic lipopeptide, is produced by various strains of Bacillus subti- lis and is primarily recognized as one of the most effective biosurfactants. It has the ability to reduce surface tension of water from 72 to 27 mN/m at a concentration as low as 0.005 %. The structure of surfactin consists of seven amino acids bonded to the carboxyl and hydrox- yl groups of a 14-carbon fatty acid. Surfactin possesses a number of biological activities such as the ability to lyse erythrocytes, inhibit clot formation, lyse bacterial spheroplasts and protoplasts, and inhibit cyclic 3',5-monophosphate diesterase. The high cost of produc- tion and low yields have limited its use in various commercial applications. Both sub- merged and solid-state fermentation have been investigated with the mutational approach to improve the productivity. In this review, current state of knowledge on biosynthesis of surfactin, its fermentative production, purification, analytical methods and biomedical appli- cations is presented. Key words: biosurfactant, surfactin, Bacillus subtilis, biosynthesis, fermentation, purification Introduction Surfactin was discovered by Arima et al. (3)from the culture broth of Bacillus subtilis (Fig. 1). It was Surfactants are ampiphilic molecules that partition named thus due to its exceptional surfactant activity (4).
    [Show full text]
  • Safety Data Sheet - Version 5.0 Preparation Date 12/21/2018 Latest Revision Date (If Revised) SDS Expiry Date 12/19/2021
    Safety Data Sheet - Version 5.0 Preparation Date 12/21/2018 Latest Revision Date (If Revised) SDS Expiry Date 12/19/2021 1. IDENTIFICATION OF THE SUBSTANCE/MIXTURE AND OF THE COMPANY/UNDERTAKING 1.1 Product Identifier Chemical Name Surfactin Catalogue # S860003 1.2 Relevant Identified Uses of the Substance or Mixture and Uses Advised Against Product Uses To be used only for scientific research and development. Not for use in humans or animals. 1.3 Details of the Supplier of the Safety Data Sheet Company Toronto Research Chemicals 2 Brisbane Road Toronto, ON M3J 2J8 CANADA Telephone +14166659696 FAX +14166654439 Email [email protected] 1.4 Emergency Telephone Number Emergency# +1(416) 665-9696 between 0800-1700 (GMT-5) 2. HAZARDS IDENTIFICATION WHMIS Classification (Canada) WHMIS Symbols (Canada) None Not WHMIS controlled. 2.1/2.2 Classification of the Substance or Mixture and Label Elements GHS Hazards Classification (According to EU Regulation 1272/2008 and US OSHA 1910.1200) Not a hazardous substance by GHS. GHS Hazards Identification (According to EU Regulation 1272/2008 and US OSHA 1910.1200) Signal Word None GHS Hazard Statements None Not a hazardous substance according to GHS. GHS Precautionary Statements 2.3 Unclassified Hazards/Hazards Not Otherwise Classified No data available. 3. COMPOSITION/INFORMATION ON INGREDIENTS Toronto Research Chemicals - S860003 Page 1 This Safety Data Sheet contains 16 sections. All 16 sections must be present for this document to be valid. This Safety Data Sheet contains 16 sections. All 16 sections
    [Show full text]
  • Bacillus Subtilis Spreads by Surfing on Waves of Surfactant
    Bacillus subtilis spreads by surfing on waves of surfactant Thomas E. Angelinia,1, Marcus Roperb,1, Roberto Kolterc, David A. Weitza, and Michael P. Brennera,1 aSchool of Engineering and Applied Sciences, Harvard University, Cambridge, MA 02138; bDepartment of Mathematics and Lawrence Berkeley National Laboratory, University of California, Berkeley, CA 94720; and cDepartment of Microbiology and Molecular Genetics, Harvard Medical School, Boston, MA 02115 Edited by E. Peter Greenberg, University of Washington School of Medicine, Seattle, WA, and approved August 18, 2009 (received for review May 28, 2009) The bacterium Bacillus subtilis produces the molecule surfactin, B. subtilis pellicles, including both the rate of spreading and a which is known to enhance the spreading of multicellular colonies direct measurement of the decrease in surface tension below the on nutrient substrates by lowering the surface tension of the sur- center of the pellicle. We then present a mathematical model that rounding fluid, and to aid in the formation of aerial structures. quantitatively explains the observed spreading–both the shape of Here we present experiments and a mathematical model that the spreading front and its velocity. The model predicts how quan- demonstrate how the differential accumulation rates induced by tities under the control of individual cells (surfactin-production the geometry of the bacterial film give rise to surfactant waves. rate, and biofilm rheology) control the collective motion of the The spreading flux increases with increasing biofilm viscosity. Com- biofilm. Finally, we rule out individual cell motility as the cause munity associations are known to protect bacterial populations of the spreading by demonstrating that whereas the B.
    [Show full text]
  • Nanoemulsion Stabilized by Safe Surfactin from Bacillus Subtilis As a Multifunctional, Custom-Designed Smart Delivery System
    pharmaceutics Article Nanoemulsion Stabilized by Safe Surfactin from Bacillus subtilis as a Multifunctional, Custom-Designed Smart Delivery System Agnieszka Lewi ´nska 1,* , Marta Dom˙zał-K˛edzia 2, Anna Jaromin 3 and Marcin Łukaszewicz 2,* 1 Faculty of Chemistry, University of Wroclaw, Joliot-Curie 14, 50-383 Wroclaw, Poland 2 Department of Biotransformation, Faculty of Biotechnology, University of Wroclaw, Joliot-Curie 14a, 50-383 Wroclaw, Poland; [email protected] 3 Department of Lipids and Liposomes, Faculty of Biotechnology, University of Wroclaw, Joliot-Curie 14a, 50-383 Wroclaw, Poland; [email protected] * Correspondence: [email protected] (A.L.); [email protected] (M.Ł.); Tel.: +48-71-3757324 (A.L.); +48-71375-6250 (M.Ł.) Received: 16 September 2020; Accepted: 7 October 2020; Published: 10 October 2020 Abstract: The developing field of bio-nanotechnology aims to advance colloidal research via the introduction of multifunctional nanoparticles to augment the dermal effectiveness of active substances. Self-emulsifying drug delivery systems (SEDDS)—isotropic mixtures of oils, surfactants, solvents and co-solvents or surfactants—are attracting interest in the cosmeceutical field. As part of this study, SEDDS systems containing vitamin C or vitamin E and curcumin were developed, whereby the bioavailability of the active compounds increased by enhancing their permeability to deeper layers of the skin. A composition consisting of 50% surfactin from Bacillus subtilis, 30% Transcutol and 20% oil phase was designed to encapsulate the active substances, i.e., vitamin C or vitamin E and curcumin, contained in the oil phase. The developed carriers were characterized by average particle sizes of 69–183 nm.
    [Show full text]
  • Small Cationic Antimicrobial Peptides Delocalize Peripheral Membrane Proteins
    Small cationic antimicrobial peptides delocalize PNAS PLUS peripheral membrane proteins Michaela Wenzela, Alina Iulia Chiriacb, Andreas Ottoc, Dagmar Zweytickd, Caroline Maye, Catherine Schumacherf, Ronald Gustg, H. Bauke Albadah, Maya Penkovah, Ute Krämeri, Ralf Erdmannj, Nils Metzler-Nolteh, Suzana K. Strausk, Erhard Bremerl, Dörte Becherc, Heike Brötz-Oesterheltf, Hans-Georg Sahlb, and Julia Elisabeth Bandowa,1 aBiology of Microorganisms, hBioinorganic Chemistry, and iPlant Physiology, eImmune Proteomics, Medical Proteome Center, and jInstitute of Physiological Chemistry, Ruhr University Bochum, 44801 Bochum, Germany; bInstitute for Medical Microbiology, Immunology, and Parasitology, Pharmaceutical Microbiology Section, University of Bonn, 53113 Bonn, Germany; cDepartment of Microbial Physiology and Molecular Biology, Ernst Moritz Arndt University, 17489 Greifswald, Germany; dBiophysics Division, Institute of Molecular Biosciences, University of Graz, 8010 Graz, Austria; fInstitute for Pharmaceutical Biology and Biotechnology, Heinrich Heine University, 40225 Düsseldorf, Germany; gDepartment of Pharmaceutical Chemistry, University of Innsbruck, 6020 Innsbruck, Austria; kDepartment of Chemistry, University of British Columbia, Vancouver, BC, Canada V6T 1Z1; and lDepartment of Biology, University of Marburg, 35037 Marburg, Germany Edited by Michael Zasloff, Georgetown University Medical Center, Washington, DC, and accepted by the Editorial Board February 27, 2014 (received for review October 22, 2013) Short antimicrobial peptides rich
    [Show full text]
  • Sustainable Surfactin Production by Bacillus Subtilis Using Crude Glycerol from Different Wastes
    molecules Article Sustainable Surfactin Production by Bacillus subtilis Using Crude Glycerol from Different Wastes Tomasz Janek 1,* , Eduardo J. Gudiña 2 , Xymena Połomska 1, Piotr Biniarz 1,3 , Dominika Jama 1, Lígia R. Rodrigues 2 , Waldemar Rymowicz 1 and Zbigniew Lazar 1 1 Department of Biotechnology and Food Microbiology, Wrocław University of Environmental and Life Sciences, 51-630 Wrocław, Poland; [email protected] (X.P.); [email protected] (P.B.); [email protected] (D.J.); [email protected] (W.R.); [email protected] (Z.L.) 2 Centre of Biological Engineering, University of Minho, 4710-057 Braga, Portugal; [email protected] (E.J.G.); [email protected] (L.R.R.) 3 Łukasiewicz Research Network—PORT Polish Center for Technology Development, 54-066 Wrocław, Poland * Correspondence: [email protected]; Tel.: +48-71-320-7734 Abstract: Most biosurfactants are obtained using costly culture media and purification processes, which limits their wider industrial use. Sustainability of their production processes can be achieved, in part, by using cheap substrates found among agricultural and food wastes or byproducts. In the present study, crude glycerol, a raw material obtained from several industrial processes, was evaluated as a potential low-cost carbon source to reduce the costs of surfactin production by Bacil- lus subtilis #309. The culture medium containing soap-derived waste glycerol led to the best surfactin production, reaching about 2.8 g/L. To the best of our knowledge, this is the first report describing surfactin production by B. subtilis using stearin and soap wastes as carbon sources.
    [Show full text]
  • Detergent-Like Action of the Antibiotic Peptide Surfactin on Lipid Membranes
    View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by Elsevier - Publisher Connector Biophysical Journal Volume 81 September 2001 1547–1554 1547 Detergent-Like Action of the Antibiotic Peptide Surfactin on Lipid Membranes Heiko Heerklotz and Joachim Seelig Department of Biophysical Chemistry, Biocenter of the University of Basel, CH-4056 Basel, Switzerland ABSTRACT Surfactin is a bacterial lipopeptide with powerful surfactant-like properties. High-sensitivity isothermal titration calorimetry was used to study the self association and membrane partitioning of surfactin. The critical micellar concentration ␮ ⌬ w3m ϭϩ (CMC), was 7.5 M, the heat of micellization was endothermic with HSu 4.0 kcal/mol, and the free energy of ⌬ 0,w3m ϭϪ micellization GSu 9.3 kcal/mol (25°C; 100 mM NaCl; 10 mM TRIS, 1 mM EDTA; pH 8.5). The specific heat capacity ⌬ w3m ⌬ w3m ϭϪ Ϯ ⅐ of micellization was deduced from temperature dependence of HSu as CP 250 10 cal/(mol K). The data can be explained by combining the hydrophobicity of the fatty acyl chain with that of the hydrophobic amino acids. The membrane partition equilibrium was studied using small (30 nm) and large (100 nm) unilamellar POPC vesicles. At 25°C, the partition Ϯ ϫ 4 Ϫ1 ⌬ 0,w3b ϭϪ coefficient, K, was (2.2 0.2) 10 M for large vesicles leading to a free energy of GSu 8.3 kcal/mol. The partition ⌬ w3b ϭ Ϯ enthalpy was again endothermic, with HSu 9 1 kcal/mol. The strong preference of surfactin for micelle formation over membrane insertion explains the high membrane-destabilizing activity of the peptide.
    [Show full text]
  • Supplementary Discussion
    1 Supplementary discussion 2 The intracellular pools of precursors and the flexibility of the NRP machinery drive surfactin 3 variant diversity 4 Surfactin producing strains are always producing the cLP as a mixture of different 5 structural variants. Specific amino acids substitution in the peptide as well as differences in 6 the fatty acid (FA) chain length and branching type represent the main structural variations 7 found in this mixture of surfactins. Two main factors are found to be involved in this diversity. 8 On one hand, the availability of precursors as well as the balance between these latter 9 is an important factor that drive the surfactin structural diversity. Indeed, feeding the bacteria 10 with specific amino acids will result in changes in the ratio between the different variants 11 (peptidic and lipidic) as well as production of new variants that are not produced in normal 12 lab conditions [1,2]. Among the important amino acids for surfactin production, isoleucine, 13 valine and leucine (branched chain amino acids or BCAAs) constitute the major precursors (5 14 out of 7). The key role of BCAAs is even more important since the branched chain fatty acids 15 (BCFAs) tail of surfactin biosynthetic pathway also require these BCAAs as precursors for their 16 biosynthesis. Indeed, Ile, Leu and Val are precursors of odd anteiso-FAs, odd iso-FAs and even 17 iso FAs, respectively [3]. This makes thus from the BCAAs balance the key factor for most part 18 of the building blocks of surfactin. Therefore, deciphering the BCAAs biosynthetic pathways 19 as well as its regulation can bring some clues on what can be involved in the balance changes 20 of surfactin precursors.
    [Show full text]