Molecular cloning and characterization of a thermostable lipase from deep-sea thermophile Geobacillus sp. EPT9

World Journal of Microbiology and Biotechnology

Volumn 31, Issue 2, 2015, Pages 295-306

  Zhu, Yanbing ^a,b,c,d   Li, Hebin ^e   Ni, Hui ^a,b,c,d   Xiao, Anfeng ^a,b,c,d   Li, Lijun ^a,b,c,d   Cai, Huinong ^a,b,c,d  

^a JIMEI UNIVERSITY   (China)

^b FUJIAN PROVINCIAL KEY LABORATORY OF FOOD MICROBIOLOGY AND ENZYME ENGINEERING   (China)

^c Research Center of Food Microbiology and Enzyme Engineering Technology (Jimei University)   (China)

^d Xiamen Southern Ocean Technology Center of China   (China)

^e Xiamen Medical College   (China)

Author keywords

Characterization; Expression; Lipase; Thermostability

Indexed keywords

AMINO ACIDS; BACTERIOLOGY; CLONE CELLS; ENZYMES; ESCHERICHIA COLI; FLUORINE COMPOUNDS; GENES; LIPASES; PALMITIC ACID; PURIFICATION;

AMINO ACID RESIDUES; CATALYTIC MECHANISMS; ENZYMATIC ACTIVITIES; EXPRESSION; PHENYLMETHYLSULFONYL FLUORIDE; RECOMBINANT ENZYMES; RECOMBINANT LIPASE; THERMOSTABILITY;

CLONING;

BACTERIAL PROTEIN; THERMOSTABLE LIPASE; TRIACYLGLYCEROL LIPASE;

CHEMICAL STRUCTURE; CHEMISTRY; ENZYME ACTIVE SITE; ENZYME SPECIFICITY; ENZYME STABILITY; ENZYMOLOGY; GENETICS; GEOBACILLUS; METABOLISM; MOLECULAR CLONING; PHYLOGENY; PROCEDURES; PROTEIN SECONDARY STRUCTURE; STRUCTURAL HOMOLOGY;

BACTERIAL PROTEINS; CATALYTIC DOMAIN; CLONING, MOLECULAR; ENZYME STABILITY; GEOBACILLUS; LIPASE; MODELS, MOLECULAR; PHYLOGENY; PROTEIN STRUCTURE, SECONDARY; STRUCTURAL HOMOLOGY, PROTEIN; SUBSTRATE SPECIFICITY;

EID: 84922338398     PISSN: 09593993     EISSN: 15730972     Source Type: Journal    
DOI: 10.1007/s11274-014-1775-0     Document Type: Article

References (55)

1. Abd Rahman RN, Shariff FM, Basri M, Salleh AB (2012) 3D structure elucidation of thermostable L2 lipase from thermophilic Bacillus sp. L2. Int J Mol Sci 13:9207–9217
2. Abdel-Fattah YR, Gaballa AA (2008) Identification and over-expression of a thermostable lipase from Geobacillus thermoleovorans Toshki in Escherichia coli. Microbiol Res 163:13–20
3. Altschul SF, Madden TL, Schäffer AA, Zhang J, Zhang Z, Miller W, Lipman DJ (1997) Gapped BLAST and PSI-BLAST: a new generation of protein databases search programs. Nucleic Acids Res 25:3389–3402
4. Arnold K, Bordoli L, Kopp J, Schwede T (2006) The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling. Bioinformatics 22:195–201
5. Bancerz R, Ginalska G (2007) A novel thermostable lipase from Basidiomycete Bjerkandera adusta R59: characterisation and esterification studies. J Ind Microbiol Biotechnol 34:553–560
6. Bornscheuer UT (2002) Microbial carboxyl esterases: classification, properties and application in biocatalysis. FEMS Microbiol Rev 26:73–81
7. Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248–254
8. Castro-Ochoa LD, Rodríguez-Gómez C, Valerio-Alfaro G, Ros RO (2005) Screening, purification and characterization of the thermoalkalophilic lipase produced by Bacillus thermoleovorans CCR11. Enzyme Microb Technol 37:648–654
9. Cygler M, Schrag JD, Ergan F (1992) Advances in structural understanding of lipases. Biotechnol Genet Eng Rev 10:143–184
10. Delboni LF, Mande SC, Rentier-Delrue F, Mainfroid V, Turley S, Vellieux FM, Martial JA, Hol WG (1995) Crystal structure of recombinant triosephosphate isomerase from Bacillus stearothermophilus. An analysis of potential thermostability factors in six isomerases with known three-dimensional structures points to the importance of hydrophobic interactions. Protein Sci 4:2594–2604
11. Dheeman DS, Henehan GT, Frías JM (2011) Purification and properties of Amycolatopsis mediterranei DSM 43304 lipase and its potential in flavour ester synthesis. Bioresour Technol 102:3373–3379
12. Ebrahimpour A, Rahman RN, Basri M, Salleh AB (2011) High level expression and characterization of a novel thermostable, organic solvent tolerant, 1,3-regioselective lipase from Geobacillus sp. strain ARM. Bioresour Technol 102:6972–6981
13. Geourjon C, Deléage G (1995) SOPMA: significant improvements in protein secondary structure prediction by consensus prediction from multiple alignments. Comput Appl Biosci 11:681–684
14. Gupta R, Gupta N, Rathi P (2004) Bacterial lipases: an overview of production, purification and biochemical properties. Appl Microbiol Biotechnol 64:763–781
15. Hasan F, Shah AA, Hameed A (2006) Industrial applications of microbial lipases. Enzyme Microb Technol 39:235–251
16. H-Kittikun A, Prasertsan P, Zimmermann W, Seesuriyachan P, Chaiyaso T (2012) Sugar ester synthesis by thermostable lipase from Streptomyces thermocarboxydus ME168. Appl Biochem Biotechnol 166:1969–1982
17. Jaeger KE, Eggert T (2002) Lipases for biotechnology. Curr Opin Biotechnol 13:390–397
18. Jaeger KE, Dijkstra BW, Reetz MT (1999) Bacterial biocatalysts: molecular biology, three-dimensional structures, and biotechnological applications of lipases. Annu Rev Microbiol 53:315–351
19. Johri S, Bhat A, Sayed S, Nargotra A, Jain A, Qazi GN (2012) Novel thermostable lipase from Bacillus circulans IIIB153: comparison with the mesostable homologue at sequence and structure level. World J Microbiol Biotechnol 28:193–203
20. Kambourova M, Kirilova N, Mandeva R, Derekova A (2003) Purification and properties of thermostable lipase from a thermophilic Bacillus stearothermophilus MC 7. J Mol Catal B Enzym 22:307–313
21. Kim HK, Park SY, Lee JK, Oh TK (1998) Gene cloning and characterization of thermostable lipase from Bacillus stearothermophilus L1. Biosci Biotechnol Biochem 62:66–71
22. Kim MH, Kim HK, Lee JK, Park SY, Oh TK (2000) Thermostable lipase of Bacillus stearothermophilus: high-level production, purification, and calcium-dependent thermostability. Biosci Biotechnol Biochem 64:280–286
23. Kreil DP, Ouzounis CA (2001) Identification of thermophilic species by the amino acid compositions deduced from their genomes. Nucleic Acids Res 29:1608–1615
24. Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680–685
25. Lailaja VP, Chandrasekaran M (2013) Detergent compatible alkaline lipase produced by marine Bacillus smithii BTMS 11. World J Microbiol Biotechnol 29:1349–1360
26. Laskowski RA, MacArthur MW, Moss DS, Thornton JM (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J Appl Cryst 26:283–291
27. Lee D, Koh Y, Kim K, Kim B, Choi H, Kim D, Suhartono MT, Pyun Y (1999) Isolation and characterization of a thermophilic lipase from Bacillus thermoleovorans ID-1. FEMS Microbiol Lett 179:393–400
28. Lee DW, Kim HW, Lee KW, Kim BC, Choe EA, Lee HS, Kim DS, Pyun YR (2001) Purification and characterization of two distinct thermostable lipases from the gram-positive thermophilic bacterium Bacillus thermoleovorans ID-1. Enzyme Microb Technol 29:363–371
29. Leow TC, Rahman RN, Basri M, Salleh AB (2004) High level expression of thermostable lipase from Geobacillus sp. strain T1. Biosci Biotechnol Biochem 68:96–103
30. Letunic I, Doerks T, Bork P (2012) SMART 7: recent updates to the protein domain annotation resource. Nucleic Acids Res. 40(Database issue):D302–D305
31. Li HB, Zhang XB (2005) Characterization of thermostable lipase from thermophilic Geobacillus sp. TW1. Protein Expr Purif 42:153–159
32. Lopes Mde F, Leitão AL, Regalla M, Marques JJ, Carrondo MJ, Crespo MT (2002) Characterization of a highly thermostable extracellular lipase from Lactobacillus plantarum. Int J Food Microbiol 76:107–115
33. Masomian M, Rahman RN, Salleh AB, Basri M (2013) A new thermostable and organic solvent-tolerant lipase from Aneurinibacillus thermoaerophilus strain HZ. Process Biochem 48:169–175
34. Matsumura H, Yamamoto T, Leow TC, Mori T, Salleh AB, Basri M, Inoue T, Kai Y, Rahman RN (2008) Novel cation-π interaction revealed by crystal structure of thermoalkalophilic lipase. Proteins 70:592–598
35. Moreno C, Romero J, Espejo RT (2002) Polymorphism in repeated 16S rRNA genes is a common property of type strains and environmental isolates of the genus Vibrio. Microbiology 148:1233–1239
36. Olusesan AT, Azura LK, Forghani B, Bakar FA, Mohamed AK, Radu S, Manap MY, Saari N (2011) Purification, characterization and thermal inactivation kinetics of a non-regioselective thermostable lipase from a genotypically identified extremophilic Bacillus subtilis NS 8. N Biotechnol 28:738–745
37. Oppenheimer CH, ZoBell CE (1952) The growth and viability of sixty-three species of marine bacteria as influenced by hydrostatic pressure. J Mar Res 11:10–18
38. Overbeeke P, Govardhan C, Khalaf N, Jongejan J, Heijnen J (2000) Influence of lid conformation on lipase enantioselectivity. J Mol Catal B Enzym 10:385–393
39. Quintana-Castro R, Díaz P, Valerio-Alfaro G, García HS, Oliart-Ros R (2009) Gene cloning, expression, and characterization of the Geobacillus thermoleovorans CCR11 thermoalkaliphilic lipase. Mol Biotechnol 42:75–83
40. Royter M, Schmidt M, Elend C, Höbenreich H, Schäfer T, Bornscheuer UT, Antranikian G (2009) Thermostable lipases from the extreme thermophilic anaerobic bacteria Thermoanaerobacter thermohydrosulfuricus SOL1 and Caldanaerobacter subterraneus subsp. tengcongensis. Extremophiles 13:769–783
41. 2+-activated thermostable L2 lipase. Protein Expr Purif 68:161–166
42. Saitou N, Nei M (1987) The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol Biol Evol 4:406–425
43. Salameh MA, Wiegel J (2007) Purification and characterization of two highly thermophilic alkaline lipases from Thermosyntropha lipolytica. Appl Environ Microbiol 73:7725–7731
44. Sarkar P, Yamasaki S, Basak S, Bera A, Bag PK (2012) Purification and characterization of a new alkali-thermostable lipase from Staphylococcus aureus isolated from Arachis hypogaea rhizosphere. Process Biochem 47:858–866
45. Schmidt-Dannert C, Rúa ML, Schmid RD (1997) Two novel lipases from thermophile Bacillus thermocatenulatus: screening, purification, cloning, overexpression, and properties. Methods Enzymol 284:194–220
46. Sinchaikul S, Sookkheo B, Phutrakul S, Pan FM, Chen ST (2001) Optimization of a thermostable lipase from Bacillus stearothermophilus P1: overexpression, purification, and characterization. Protein Expr Purif 22:388–398
47. Soliman NA, Knoll M, Abdel-Fattah YR, Schmid RD, Lange S (2007) Molecular cloning and characterization of thermostable esterase and lipase from Geobacillus thermoleovorans YN isolated from desert soil in Egypt. Process Biochem 42:1090–1100
48. Sugihara A, Ueshima M, Shimada Y, Tsunasawa S, Tominaga Y (1992) Purification and characterization of a novel thermostable lipase from Pseudomonas cepacia. J Biochem 112:598–603
49. Tamura K, Stecher G, Peterson D, Filipski A, Kumar S (2013) MEGA6: molecular evolutionary genetics analysis version 6.0. Mol Biol Evol 30:2725–2729
50. Tayyab M, Rashid N, Akhtar M (2011) Isolation and identification of lipase producing thermophilic Geobacillus sp. SBS-4S: cloning and characterization of the lipase. J Biosci Bioeng 111:272–278
51. Tyndall JD, Sinchaikul S, Fothergill-Gilmore LA, Taylor P, Walkinshaw MD (2002) Crystal structure of a thermostable lipase from Bacillus stearothermophilus P1. J Mol Biol 323:859–869
52. Vieille C, Zeikus GJ (2001) Hyperthermophilic enzymes: source, uses, and molecular mechanisms for thermostability. Microbiol Mol Biol Rev 65:1–43
53. Vogt G, Woell S, Argos P (1997) Protein thermal stability, hydrogen bonds, and ion pairs. J Mol Biol 269:631–643
54. Winkler UK, Stuckmann M (1979) Glycogen, hyaluronate, and some other polysaccharides greatly enhance the formation of exolipase by Serratia marcescens. J Bacteriol 138:663–670
55. Yang JK, Guo DY, Yan YJ (2007) Cloning, expression and characterization of a novel thermal stable and short-chain alcohol tolerant lipase from Burkholderia cepacia strain G63. J Mol Catal B Enzym 45:91–96