Structural and molecular characteristics of lichenysin and its relationship with surface activity.
Lichenysins are most potent anionic cyclic lipoheptapeptide biosurfactants produced by Bacillus licheniformis on hydrocarbonless medium with mainly glucose as carbon source. They have the capacity to lower the surface tension of water from 72 to 27 mN/m. Based on species specific variations they are named lichenysin A, B, C, D, G and surfactant BL86. The lowest ever interfacial tension against decane of 0.006 mN/m is obtained with acid precipitated lichenysin B. Surfactant BL86 and lichenysin B have recorded lowest ever CMC of 10 mg/L by any surfactant under optimal conditions. Surface and interfacial tension lowering ability bears significance in the context of oil recovery from oil reservoir. Similarity exists between structure and biosynthesis of surfactin and lichenysin. Surfactin being the most studied of the two, understanding its structure and biosynthesis gives an insight into the structure and biosynthesis of lichenysin. Lichenysin is synthesized by a multienzyme complex, lichenysin synthetase (LchA/Lic) encoded by 32.4 (26.6 kb) lichenysin operon lchA (lic). The structure of lichenysin and its operon indicate the nonribosomal biosynthesis with the same multifunctional modular arrangement as seen in surfactin synthetase SrfA. The lchA operon consists of lchAA-AC (lic A-C) and lchA TE (licTE) genes encoding the proteins LchAA, LchAB, LchAC and thioesterase LchA-TE. The licA (lchAA) gene is 10,746 bp and codes for a 3,582 amino acids protein, licB (lchAB) gene is 10,764 bp and codes for a similar sized protein, while licC (lchAC) gene is 3,864 bp and codes for protein containing 1,288 amino acid. The biotechnological potential of lichenysin in MEOR has triggered research on structure-activity relationship. Both the nature of peptide and fatty acid dictate the activity of the biosurfactant. Tailormade biosurfactant with desired attributes can be obtained from engineered synthetases. Basic studies are lacking on mechanism of biosynthesis by lichenysin synthetase however, studies on various aspects of lichenysin including regulation are expected to swell in coming years.
Nerurkar
Anuradha S
AS
Department of Microbiology, Faculty of Science, The Maharaja Sayajirao University of Baroda, Vadodara-390 002, Gujarat, India. anuner@gmail.com
D001407:Bacillus / Q000235:genetics* / Q000378:metabolism*; D001426:Bacterial Proteins / Q000096:biosynthesis; D008025:Ligases / Q000378:metabolism; D055666:Lipopeptides / Q000096:biosynthesis / Q000737:chemistry; D008074:Lipoproteins / Q000737:chemistry; D009876:Operon; D010456:Peptides, Cyclic / Q000096:biosynthesis / Q000737:chemistry; D013329:Structure-Activity Relationship; D013501:Surface-Active Agents / Q000737:chemistry*
D001426:Bacterial Proteins; D055666:Lipopeptides; D008074:Lipoproteins; D010456:Peptides, Cyclic; D013501:Surface-Active Agents; C094325:lichenysin A; C009365:surfactin peptide; D008025:Ligases; C110472:lichenysin A synthetase