The name surfactin refers to a bacterial cyclic lipopeptide, primarily renowned for its exceptional surfactant power since it lowers the surface tension of water from 72 mN m-1 to 27 mN m-1 at a concentration as low as 20 microM. Although surfactin was discovered about 30 years ago, there has been a revival of interest in this compound over the past decade, triggered by an increasing demand for effective biosurfactants for difficult contemporary ecological problems. This simple molecule also looks very promising as an antitumoral, antiviral and anti-Mycoplasma agent. Structural characteristics show the presence of a heptapeptide with an LLDLLDL chiral sequence linked, via a lactone bond, to a beta-hydroxy fatty acid with 13-15 C atoms. In solution, the molecule exhibits a characteristic "horse saddle" conformation that accounts for its large spectrum of biological activity, making it very attractive for both industrial applications and academic studies. Surfactin biosynthesis is catalysed non-ribosomally by the action of a large multienzyme complex consisting of four modular building blocks, called the surfactin synthetase. The biosynthetic activity involves the multicarrier thiotemplate mechanism and the enzyme is organized in structural domains that place it in the family of peptide synthetases, a class of enzymes involved in peptidic secondary-metabolite synthesis. The srfA operon, the sfp gene encoding a 4'-phosphopantetheinyltransferase and the comA regulatory gene work together for surfactin biosynthesis, while the gene encoding the acyltransferase remains to be isolated. Concerning surfactin production, there is no indication whether the genetic regulation, involving a quorum-sensing mechanism, overrides other regulation factors promoted by the fermentation conditions. Knowledge of the modular arrangement of the peptide synthetases is of the utmost relevance to combinatorial biosynthetic approaches and has been successfully used at the gene level to modify the surfactin template. Biosynthetic and genetic rationales have been described for building variants. A fine study of the structure/function relationships associated with the three-dimensional structure has led to the recognition of the specific residues required for activity. These studies will assist researchers in the selection of molecules with improved and/or refined properties useful in oil and biomedical industries.

Recent trends in the biochemistry of surfactin.

The review discusses current knowledge of the biosynthesis, composition and arrangement of the mycobacterial envelope, describes the biological activities of the constituents and considers how these activities may be relevant to the pathology of mycobacterial disease. The envelope possesses three structural components: plasma membrane, wall and capsule. Although the major biomolecules occurring in each of these parts are known, the distribution of numerous minor substances is poorly understood; an attempt has been made to assign them to particular positions on rational grounds. The plasma membrane appears to be a typical bacterial membrane but, though vital to the mycobacterium, probably plays little part in pathological processes. The wall partly resembles a Gram-positive wall, but is unusual in having a layer of lipid (mycolate esters) which is probably arranged to form a permeability barrier to polar molecules. The capsule, whose chemical composition has only recently been recognized, consists of polysaccharide and protein with traces of lipid; the arrangement of these components is imperfectly understood. Constituents of all parts of the envelope have biological activities which may be relevant. The likely importance of these activities in the overall effect of the envelope is considered.

The envelope layers of mycobacteria with reference to their pathogenicity.

A study on the structure-function relationship of lipopeptide biosurfactants.

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.

Characterization of a new lipopeptide surfactant produced by thermotolerant and halotolerant subsurface Bacillus licheniformis BAS50.

Biosynthesis of vitamin K (menaquinone) in bacteria.

The structure of mycosubtilin, a peptidolipid antibiotic from Bacillus subtilis, was revised by FAB mass spectrometry, 2D NMR spectrometry and also by Edman degradation of the peptide resulting from the N-bromosuccinimide reaction. Four homologous β-amino acid components were identified by capillary gas chromatography. The cyclopeptide mycosubtilin consists of seven α-amino acids in an LDDLLDL sequence closed by a β-amino acid linkage similar to that found in other antibiotics of the iturin group.

Revised structure of mycosubtilin, a peptidolipid antibiotic from bacillus subtilis

Isolement de l'acide 3-amino 12-methyl tetradecanoique et de l'acide 3-amino 12-methyl tridecanoique a partir de l'iturine, antibiotique de Bacillus subtilis

B.C. Das

Papers

Revised structure of mycosubtilin, a peptidolipid antibiotic from bacillus subtilis

Isolement de l'acide 3-amino 12-methyl tetradecanoique et de l'acide 3-amino 12-methyl tridecanoique a partir de l'iturine, antibiotique de Bacillus subtilis

Structure de l'iturine C de Bacillus subtilis

Triterpenoids—XXXVII : The structure and stereochemistry of lantanolic acid—a new triterpenoid from Lantana camara

Alkaloids from the leaves ofStrychnos icaja Baill.