Abstract
Strain BAS50, isolated from a petroleum reservoir at a depth of 1,500 m and identified as Bacillus licheniformis, grew and produced a lipopeptide surfactant when cultured on a variety of substrates at salinities of up to 13% NaCl. Surfactant production occurred both aerobically and anaerobically and was optimal at 5% NaCl and temperatures between 35 and 45 degrees C. The biosurfactant, termed lichenysin A, was purified and chemically characterized. A tentative structure and composition for the surfactant are described. Lichenysin A is a mixture of lipopeptides, with the major components ranging in size from 1,006 to 1,034 Da. The lipid moiety contains a mixture of 14 linear and branched beta-hydroxy fatty acids ranging in size from C12 to C17. There are seven amino acids per molecule. The peptide moiety is composed of the following amino acids: glutamic acid as the N-terminal amino acid, asparagine, valine, leucine, and isoleucine as the C-terminal amino acid, at a ratio of 1.1:1.1:1.0:2.8:1.0, respectively. Purified lichenysin A decreases the surface tension of water from 72 mN/m to 28 mN/m and achieves the critical micelle concentration with as little as 12 mg/liter, characterizing the product as a powerful surface-active agent that compares favorably to others surfactants. The antibacterial activity of lichenysin A has been demonstrated.
Full Text
The Full Text of this article is available as a PDF (331.2 KB).
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Arima K., Kakinuma A., Tamura G. Surfactin, a crystalline peptidelipid surfactant produced by Bacillus subtilis: isolation, characterization and its inhibition of fibrin clot formation. Biochem Biophys Res Commun. 1968 May 10;31(3):488–494. doi: 10.1016/0006-291x(68)90503-2. [DOI] [PubMed] [Google Scholar]
- Aveldaño M. I., Horrocks L. A. Quantitative release of fatty acids from lipids by a simple hydrolysis procedure. J Lipid Res. 1983 Aug;24(8):1101–1105. [PubMed] [Google Scholar]
- Bryant M. P. Commentary on the Hungate technique for culture of anaerobic bacteria. Am J Clin Nutr. 1972 Dec;25(12):1324–1328. doi: 10.1093/ajcn/25.12.1324. [DOI] [PubMed] [Google Scholar]
- Cooper D. G., Macdonald C. R., Duff S. J., Kosaric N. Enhanced Production of Surfactin from Bacillus subtilis by Continuous Product Removal and Metal Cation Additions. Appl Environ Microbiol. 1981 Sep;42(3):408–412. doi: 10.1128/aem.42.3.408-412.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Horowitz S., Griffin W. M. Structural analysis of Bacillus licheniformis 86 surfactant. J Ind Microbiol. 1991 Jan;7(1):45–52. doi: 10.1007/BF01575602. [DOI] [PubMed] [Google Scholar]
- Hosono K., Suzuki H. Acylpeptides, the inhibitors of cyclic adenosine 3',5'-monophosphate phosphodiesterase. II. Amino acid sequence and location of lactone linkage. J Antibiot (Tokyo) 1983 Jun;36(6):674–678. doi: 10.7164/antibiotics.36.674. [DOI] [PubMed] [Google Scholar]
- Hosono K., Suzuki H. Acylpeptides, the inhibitors of cyclic adenosine 3',5'-monophosphate phosphodiesterase. J Antibiot (Tokyo) 1983 Feb;36(2):194–196. doi: 10.7164/antibiotics.36.194. [DOI] [PubMed] [Google Scholar]
- Javaheri M., Jenneman G. E., McInerney M. J., Knapp R. M. Anaerobic Production of a Biosurfactant by Bacillus licheniformis JF-2. Appl Environ Microbiol. 1985 Sep;50(3):698–700. doi: 10.1128/aem.50.3.698-700.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Jenny K., Käppeli O., Fiechter A. Biosurfactants from Bacillus licheniformis: structural analysis and characterization. Appl Microbiol Biotechnol. 1991 Oct;36(1):5–13. doi: 10.1007/BF00164690. [DOI] [PubMed] [Google Scholar]
- Kluge B., Vater J., Salnikow J., Eckart K. Studies on the biosynthesis of surfactin, a lipopeptide antibiotic from Bacillus subtilis ATCC 21332. FEBS Lett. 1988 Apr 11;231(1):107–110. doi: 10.1016/0014-5793(88)80712-9. [DOI] [PubMed] [Google Scholar]
- Lin S. C., Minton M. A., Sharma M. M., Georgiou G. Structural and immunological characterization of a biosurfactant produced by Bacillus licheniformis JF-2. Appl Environ Microbiol. 1994 Jan;60(1):31–38. doi: 10.1128/aem.60.1.31-38.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Matsuyama T., Kaneda K., Ishizuka I., Toida T., Yano I. Surface-active novel glycolipid and linked 3-hydroxy fatty acids produced by Serratia rubidaea. J Bacteriol. 1990 Jun;172(6):3015–3022. doi: 10.1128/jb.172.6.3015-3022.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Matsuyama T., Kaneda K., Nakagawa Y., Isa K., Hara-Hotta H., Yano I. A novel extracellular cyclic lipopeptide which promotes flagellum-dependent and -independent spreading growth of Serratia marcescens. J Bacteriol. 1992 Mar;174(6):1769–1776. doi: 10.1128/jb.174.6.1769-1776.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
- McInerney M. J., Javaheri M., Nagle D. P., Jr Properties of the biosurfactant produced by Bacillus licheniformis strain JF-2. J Ind Microbiol. 1990 Apr-May;5(2-3):95–101. doi: 10.1007/BF01573858. [DOI] [PubMed] [Google Scholar]
- Morikawa M., Daido H., Takao T., Murata S., Shimonishi Y., Imanaka T. A new lipopeptide biosurfactant produced by Arthrobacter sp. strain MIS38. J Bacteriol. 1993 Oct;175(20):6459–6466. doi: 10.1128/jb.175.20.6459-6466.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Parkinson M. Bio-surfactants. Biotechnol Adv. 1985;3(1):65–83. doi: 10.1016/0734-9750(85)90006-0. [DOI] [PubMed] [Google Scholar]
- Peypoux F., Bonmatin J. M., Labbé H., Das B. C., Ptak M., Michel G. Isolation and characterization of a new variant of surfactin, the [Val7]surfactin. Eur J Biochem. 1991 Nov 15;202(1):101–106. doi: 10.1111/j.1432-1033.1991.tb16349.x. [DOI] [PubMed] [Google Scholar]
- Ullrich C., Kluge B., Palacz Z., Vater J. Cell-free biosynthesis of surfactin, a cyclic lipopeptide produced by Bacillus subtilis. Biochemistry. 1991 Jul 2;30(26):6503–6508. doi: 10.1021/bi00240a022. [DOI] [PubMed] [Google Scholar]
- Wilkinson S. G. Composition and structure of the ornithine-containing lipid from Pseudomonas rubescens. Biochim Biophys Acta. 1972 May 23;270(1):1–17. doi: 10.1016/0005-2760(72)90171-3. [DOI] [PubMed] [Google Scholar]
- Wray V., Kakoschke C., Nokihara K., Naruse S. Solution structure of pituitary adenylate cyclase activating polypeptide by nuclear magnetic resonance spectroscopy. Biochemistry. 1993 Jun 8;32(22):5832–5841. doi: 10.1021/bi00073a016. [DOI] [PubMed] [Google Scholar]