Characterization and a point mutational approach of a psychrophilic lipase from an arctic bacterium, Bacillus pumilus

Biotechnology Letters

Volumn 36, Issue 6, 2014, Pages 1295-1302

  Wi, Ah Ram ^a   Jeon, Sung Jong ^b   Kim, Sunghui ^a   Park, Ha Ju ^a   Kim, Dockyu ^a   Han, Se Jong ^a   Yim, Joung Han ^a   Kim, Han Woo ^a  

^a Korea Polar Research Institute (KOPRI)   (South Korea)

^b Dong Eui University   (South Korea)

Author keywords

Arctic bacterium; Bacillus pumilus; Lipase; Psychrophilic lipase; Rational mutation

Indexed keywords

3D MODELING; ENZYMES; ESCHERICHIA COLI; LIPASES;

3D STRUCTURE; ARCTIC OCEAN; BACILLUS PUMILUS; IMPROVED ACTIVITIES; LIPOLYTIC ACTIVITY; PROTEIN DENATURATION; RATIONAL MUTATION; RECOMBINANT ENZYMES;

BACTERIOLOGY;

BACILLUS PUMILUS; BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

BACTERIAL DNA; MUTANT PROTEIN; RECOMBINANT PROTEIN; SEA WATER; TRIACYLGLYCEROL LIPASE;

AMINO ACID SUBSTITUTION; ARCTIC; BACILLUS; CHEMICAL STRUCTURE; CHEMISTRY; DNA SEQUENCE; ENZYME SPECIFICITY; ENZYME STABILITY; ENZYMOLOGY; ESCHERICHIA COLI; GENETICS; ISOLATION AND PURIFICATION; METABOLISM; MICROBIOLOGY; MOLECULAR GENETICS; PH; PROTEIN CONFORMATION; SEA; SITE DIRECTED MUTAGENESIS; TEMPERATURE;

AMINO ACID SUBSTITUTION; ARCTIC REGIONS; BACILLUS; DNA, BACTERIAL; ENZYME STABILITY; ESCHERICHIA COLI; HYDROGEN-ION CONCENTRATION; LIPASE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; MUTANT PROTEINS; OCEANS AND SEAS; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; SEAWATER; SEQUENCE ANALYSIS, DNA; SUBSTRATE SPECIFICITY; TEMPERATURE;

EID: 84899929050     PISSN: 01415492     EISSN: 15736776     Source Type: Journal    
DOI: 10.1007/s10529-014-1475-8     Document Type: Article

References (18)

1. Arifin AR, Kim SJ, Yim JH, Suwanto A, Kim HK (2013) Isolation and biochemical characterization of Bacillus pumilus lipases from the Antarctic. J Microbiol Biotechnol 23: 661-667.
2. Bell PJ, Sunna A, Gibbs MD, Curach NC, Nevalainen H, Bergquist PL (2002) Prospecting for novel lipase genes using PCR. Microbiology 148(8): 2283-2291.
3. D'Amico S, Marx JC, Gerday C, Feller G (2003) Activity-stability relationships in extremophilic enzymes. J Biol Chem 278: 7891-7896.
4. Detry J, Rosenbaum T, Lutz S, Hahn D, Jaeger KE, Muller M, Eggert T (2006) Biocatalytic production of enantiopure cyclohexane-trans-1, 2-diol using extracellular lipases from Bacillus subtilis. Appl Microbiol Biotechnol 72: 1107-1116.
5. Feller G, Gerday C (2003) Psychrophilic enzymes: hot topics in cold adaptation. Nat Rev Microbiol 1: 200-208.
6. Fields PA, Somero GN (1998) Hot spots in cold adaptation: localized increases in conformational flexibility in lactate dehydrogenase A4 orthologs of Antarctic notothenioid fishes. Proc Natl Acad Sci USA 95: 11476-11481.
7. Gupta R, Gupta N, Rathi P (2004) Bacterial lipases: an overview of production, purification and biochemical properties. Appl Microbiol Biotechnol 64: 763-781.
8. Jaeger KE, Eggert T (2002) Lipases for biotechnology. Curr Opin Biotechnol 13: 390-397.
9. Jeong JY, Yim HS, Ryu JY, Lee HS, Lee JH, Seen DS, Kang SG (2012) One-step sequence- and ligation-independent cloning as a rapid and versatile cloning method for functional genomics studies. Appl Environ Microbiol 78: 5440-5443.
10. Joseph B, Ramteke PW, Thomas G, Shrivastava N (2007) Standard review cold-active microbial lipases: a versatile tool for industrial applications. Biotechnol Mol Biol Rev 2: 10.
11. Joseph B, Ramteke PW, Thomas G (2008) Cold active microbial lipases: some hot issues and recent developments. Biotechnol Adv 26: 457-470.
12. Laskowski RA, Rullmannn JA, MacArthur MW, Kaptein R, Thornton JM (1996) AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J Biomol NMR 8: 477-486.
13. Rasool S, Johri S, Riyaz-ul-Hassan S, Maqbool QU, Verma V, Koul S, Taneja SC, Qazi GN (2005) Molecular cloning of enantioselective ester hydrolase from Bacillus pumilus DBRL-191. FEMS Microbiol Lett 249: 113-120.
14. Schmid RD, Verger R (1998) Lipases: interfacial enzymes with attractive applications. Angew Chem Int Ed Engl 37: 26.
15. Straathof AJJ (2001) Development of a computer program for analysis of enzyme kinetics by progress curve fitting. J Mol Catal B Enzy 11: 991-998.
16. van Pouderoyen G, Eggert T, Jaeger KE, Dijkstra BW (2001) The crystal structure of Bacillus subtilis lipase: a minimal alpha/beta hydrolase fold enzyme. J Mol Biol 309: 215-226.
17. Willeman WF, Hanefeld U, Straathof AJ, Heijnen JJ (2000) Estimation of kinetic parameters by progress curve analysis for the synthesis of (R)-mandelonitrile by Prunus amygdalus hydroxynitrile lyase. Enzy Microb Technol 27: 423-433.
18. Zhang Y (2008) I-TASSER server for protein 3D structure prediction. BMC Bioinform 9: 40.