Utilization of coconut oil mill waste as a substrate for optimized lipase production, oil biodegradation and enzyme purification studies in Staphylococcus pasteuri

Electronic Journal of Biotechnology

Volumn 18, Issue 1, 2015, Pages 20-28

  Kanmani, P ^a   Kumaresan, K ^a   Aravind, J ^a  

^a KUMARAGURU COLLEGE OF TECHNOLOGY   (India)

Author keywords

Bioremediation; Fat and oil contaminants; Ion exchange chromatography; Lipase characterization; Response surface methodology

Indexed keywords

BACTERIOLOGY; BIODEGRADATION; BIODIESEL; BIOREMEDIATION; BIOTECHNOLOGY; CHROMATOGRAPHIC ANALYSIS; CULTIVATION; EFFLUENTS; ENZYMES; ION CHROMATOGRAPHY; ION EXCHANGE; PETROLEUM INDUSTRY; PURIFICATION; SUBSTRATES; SURFACE PROPERTIES; VEGETABLE OILS; WASTEWATER TREATMENT;

BIODIESEL PRODUCTION; DETERGENT FORMULATIONS; EXTRACELLULAR LIPASE; ION EXCHANGE CHROMATOGRAPHY; MODERATELY THERMOPHILIC; OIL CONTAMINANTS; RECEIVING WATER BODIES; RESPONSE SURFACE METHODOLOGY;

WATER POLLUTION;

OIL; TRIACYLGLYCEROL LIPASE;

ARTICLE; BACILLUS SUBTILIS; BACTERIUM ISOLATION; BIODEGRADATION; COCONUT OIL MILL WASTE; EFFLUENT; ENZYME PURIFICATION; ENZYME SUBSTRATE; ENZYME SYNTHESIS; HYDROLYSIS; LIPOLYSIS; MOLECULAR WEIGHT; NONHUMAN; NUCLEOTIDE SEQUENCE; PH; PROCESS OPTIMIZATION; STAPHYLOCOCCUS PASTEURI; WASTE;

BACILLUS SUBTILIS; BACTERIA (MICROORGANISMS); STAPHYLOCOCCUS PASTEURI;

EID: 84922419383     PISSN: None     EISSN: 07173458     Source Type: Journal    
DOI: 10.1016/j.ejbt.2014.11.003     Document Type: Article

References (38)

1. LiuGF, Liang ZW, Yang SY, Du P, YangY, Chen YX. Bio-treatment of greasewastewater: Research progress. Chin J Appl Ecol 2011; 22: 2219-26.
2. Cammarota MC, Freire DMG. A review on hydrolytic enzymes in the treatment of wastewater with high oil and grease content. Bioresour Technol 2006; 97: 2195-210.
3. Romero CM, Pera LM, Loto F, Vallejos C, Castro G, Baigori MD. Purification of an organic solvent-tolerant lipase from Aspergillus niger MYA 135 and its application in ester synthesis. Biocatal Agric Biotechnol 2012; 1: 25-31. http://dx. doi. org/10. 1016/j. bcab. 2011. 08. 013.
4. Santos RD, Comim SRR, De Oliveira D, Treichel H, Di Luccio M, Ferreira SRS, et al. Lipase-catalyzed synthesis of poly(e-caprolactone) in supercritical carbon dioxide. Biocatal Agric Biotechnol 2012; 1: 280-3. http://dx. doi. org/10. 1016/j. bcab. 2012. 04. 002.
5. Hasan F, Shah AA, Hameed A. Industrial applications of microbial lipases. Enzym Microb Technol 2006; 39: 235-51. http://dx. doi. org/10. 1016/j. enzmictec. 2005. 10. 016.
6. Winkler UK, Stuckmann M. Glycogen, hyaluronate and some other polysaccharides greatly enhance the formation of exolipase by Serratia marcescens. J Bacteriol 1979; 138: 663-70.
7. Lowry OH, Rosebrough NJ, Farr AL, Randall RJ. Protein measurement with the Folin phenol reagent. J Biol Chem 1951; 193: 265-75.
8. Giovanoni SJ. The polymerase chain reaction. In: Stackebrandt E, Goodfellow M, editors. Nucleic acid techniques in bacterial systematics. New York: Wiley; 1991. p. 177-203.
9. Altschul SF, Madden TL, Schaffer AA, Zhang J, Zhang Z, Miller W, et al. Gapped BLAST and PSI-BLAST: A new generation of protein database search programs. Nucleic Acids Res 1997; 25: 3389-402. http://dx. doi. org/10. 1093/nar/25. 17. 3389.
10. Greenberg AE. Standard methods for the examination of water and wastewater. 17th ed. Washington DC: APHA, AWWA, WPCF; 1989.
11. Folin O, Ciocalteau V. On tyrosine and tryptophan determinations in proteins. J Biol Chem 1927; 73: 627-50.
12. Bernfeld P. Amylase. In: Colowick SP, Kaplan NO, editors. Methods in enzymology. New York: Academic Press; 1955. p. 149-58.
13. Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227: 680-5. http://dx. doi. org/10. 1038/227680a0.
14. Sarkar P, Yamasaki S, Basak S, Bera A, Bag PK. Purification and characterization of a new alkali-thermostable lipase from Staphylococcus aureus isolated from Arachis hypogaea rhizosphere. Process Biochem 2012; 47: 858-66. http://dx. doi. org/10. 1016/j. procbio. 2012. 02. 023.
15. Bouaziz A, Horchani H, Salem NB, Gargouri Y, Sayari A. Expression, purification of a novel alkaline Staphylococcus xylosus lipase acting at high temperature. BiochemEng J 2011; 54: 93-102. http://dx. doi. org/10. 1016/j. bej. 2011. 02. 003.
16. Sayari A, Agrebi N, Jaoua S, Gargouri Y. Biochemical and molecular characterization of Staphylococcus simulans lipases. Biochimie 2001; 83: 863-71. http://dx. doi. org/10. 1016/S0300-9084(01)01327-X.
17. Van Kampen MD, Rosenstein R, Gotz F, Egmond MR. Cloning, purification and characterisation of Staphylococcus warneri lipase 2. Biochim Biophys Acta Protein Struct Mol Enzymol 2001; 1544: 229-41. http://dx. doi. org/10. 1016/S0167-4838(00)00224-7.
18. Prasad MP, Manjunath K. Comparative study on biodegradation of lipid-rich wastewater using lipase producing bacterial species. Indian J Biotechnol 2011; 10: 121-4.
19. Bhosale HJ, Kadam TA, Sukalkar SR. Hydrolytic enzyme profiling of moderately halophilic Staphylococcus xylosus isolated from saline soils. Asian J Microbiol Biotechnol Environ Sci 2013; 15: 337-43.
20. Acikel U, Ersan M, Acikel YS. Optimization of critical medium components using response surface methodology for lipase production by Rhizopus delemar. Food Bioprod Process 2010; 88: 31-9. http://dx. doi. org/10. 1016/j. fbp. 2009. 08. 003.
21. Basheer SM, Chellappan S, Beena PS, Sukumaran RK, Elyas KK, Chandrasekaran M. Lipase from marine Aspergillus awamori BTMFW032: Production, partial purification and application in oil effluent treatment. New Biotechnol 2011; 28: 627-38. http://dx. doi. org/10. 1016/j. nbt. 2011. 04. 007.
22. Kaushik R, Saran S, Isar J, Saxena RK. Statistical optimization of medium components and growth conditions by response surfacemethodology to enhance lipase production by Aspergillus carneus. J Mol Catal B Enzym 2006; 40: 121-6. http://dx. doi. org/10. 1016/j. molcatb. 2006. 02. 019.
23. Nawani N, Kaur J. Purification, characterization and thermostability of lipase from a thermophilic Bacillus sp. J33. Mol Cell Biochem 2000; 206: 91-6. http://dx. doi. org/10. 1023/A: 1007047328301.
24. Sánchez-Otero MG, Ruiz-López II, Ávila-Nieto DE, Oliart-Ros RM. Significant improvement of Geobacillus thermoleovorans CCR11 thermoalkalophilic lipase production using response surface methodology. New Biotechnol 2011; 28: 761-6. http://dx. doi. org/10. 1016/j. nbt. 2011. 01. 010.
25. Hasan-Beikdashti M, Forootanfar H, Safiarian MS, Ameri A, Ghahremani MH, Khoshayand MR, et al. Optimization of culture conditions for production of lipase by a newly isolated bacterium Stenotrophomonas maltophilia. J Taiwan Inst Chem Eng 2012; 43: 670-7. http://dx. doi. org/10. 1016/j. jtice. 2012. 03. 005.
26. Liu CH, Lu WB, Chang JS. Optimizing lipase production of Burkholderia sp. by response surface methodology. Process Biochem 2012; 41: 1910-4. http://dx. doi. org/10. 1016/j. procbio. 2006. 04. 013.
27. Gupta N, Sahai V, Gupta R. Alkaline lipase from a novel strain Burkholderia multivorans: Statistical medium optimization and production in a bioreactor. Process Biochem 2007; 42: 518-26. http://dx. doi. org/10. 1016/j. procbio. 2006. 10. 006.
28. Horchani H, Mosbah H, Salem NB, Gargouri Y, Sayari A. Biochemical and molecular characterization of a thermoactive, alkaline and detergent-stable lipase from a newly isolated Staphylococcus aureus strain. J Mol Catal B Enzym 2009; 56: 237-45. http://dx. doi. org/10. 1016/j. molcatb. 2008. 05. 011.
29. Mosbah H, Sayari A, Bezzine S, Gargouri Y. Expression, purification, and characterization of His-tagged Staphylococcus xylosus lipase wild-type and its mutant Asp 290 Ala. Protein Expr Purif 2006; 47: 516-23. http://dx. doi. org/10. 1016/j. pep. 2005. 11. 013.
30. Rosenstein R, Gotz F. Staphylococcal lipases: Biochemical and molecular characterization. Biochimie 2000; 82: 1005-14. http://dx. doi. org/10. 1016/S0300-9084(00)01180-9.
31. Illanes A. Stability of biocatalysts. Electron J Biotechnol 1999: 2. http://dx. doi. org/10. 2225/vol2-issue1-fulltext-2.
32. Simons JWFA, Van Kampen MD, Ubarretxena-Belandia I, Cox RC, dos Santos CM, Egmond MR, et al. Identification of a calcium binding site in Staphylococcus hyicus lipase: Generation of calcium-independent variants. Biochemistry 1999; 38: 2-10. http://dx. doi. org/10. 1021/bi981869l.
33. Delorme V, Dhouib R, Canaan S, Fotiadu F, Carrière F, Cavalier JF. Effects of surfactants on lipase structure, activity, and inhibition. Pharm Res 2011; 28: 1831-42. http://dx. doi. org/10. 1007/s11095-010-0362-9.
34. Gargouri Y, Julien R, Sugihara A, Verger R, Sarda L. Inhibition of pancreatic and microbial lipases by proteins. Biochim Biophys Acta Lipids Lipid Metab 1984; 795: 326-31. http://dx. doi. org/10. 1016/0005-2760(84)90082-1.
35. Gargouri Y, Pieroni G, Rivière C, Sugihara A, Sarda L, Verger R. Inhibition of lipases by proteins. A kinetic study with dicaprin monolayers. J Biol Chem 1985; 260: 2268-73.
36. Daoud L, Kamoun J, Ali MB, Jallouli R, Bradai R, Mechichi T, et al. Purification and biochemical characterization of a halotolerant Staphylococcus sp. extracellular lipase. Int J Biol Macromol 2013; 57: 232-7. http://dx. doi. org/10. 1016/j. ijbiomac. 2013. 03. 018.
37. Shimada Y, Koga C, Sugihara A, Nagao T, Takada N, Tsunasawa S, et al. Purification and characterization of a novel solvent-tolerant lipase from Fusarium heteroporum. J Ferment Bioeng 1993; 75: 349-52. http://dx. doi. org/10. 1016/0922-338X(93)90132-R.
38. Chakraborty K, Raj RP. An extracellular alkaline metallolipase from Bacillus licheniformis MTCC 6824: Purification and biochemical characterization. Food Chem 2008; 109: 727-36. http://dx. doi. org/10. 1016/j. foodchem. 2008. 01. 026.