A cold-adapted esterase from psychrotrophic Pseudoalteromas sp. strain 643A

Archives of Microbiology

Volumn 188, Issue 1, 2007, Pages 27-36

  Cieśliński, Hubert ^a   Białkowska, Aneta M ^b   Długołęcka, Anna ^a   Daroch, Maurycy ^b   Tkaczuk, Karolina L ^b,c   Kalinowska, Halina ^b   Kur, Józef ^a   Turkiewicz, Marianna ^b  

^a GDANSK UNIVERSITY OF TECHNOLOGY   (Poland)

^b LODZ UNIVERSITY OF TECHNOLOGY   (Poland)

^c INTERNATIONAL INSTITUTE OF MOLECULAR AND CELL BIOLOGY   (Poland)

Author keywords

Cloning; Cold adapted enzyme; Esterases lipases; GDSL esterase; Psychrotolerant bacterium

Indexed keywords

AGAR; AMINO ACID; BENZYLSULFONYL FLUORIDE; CALCIUM ION; COBALT; COPPER ION; DITHIOTHREITOL; ESTERASE; FATTY ACID; GENOMIC DNA; GLUTATHIONE; LONG CHAIN FATTY ACID; MAGNESIUM ION; MERCAPTOETHANOL; PALMITIC ACID; STEARIC ACID; TRIBUTYRIN;

AMINO ACID SEQUENCE; ARTICLE; BACTERIAL GROWTH; BACTERIAL STRAIN; BACTERIUM; BACTERIUM ISOLATION; DIGESTIVE SYSTEM; DNA LIBRARY; ENZYME ACTIVITY; ESCHERICHIA COLI; GENE ISOLATION; LOW TEMPERATURE; MOLECULAR WEIGHT; NONHUMAN; NUCLEOTIDE SEQUENCE; PH MEASUREMENT; PRIORITY JOURNAL; PSEUDOALTEROMAS; PURIFICATION; TEMPERATURE MEASUREMENT;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; EUPHAUSIA SUPERBA; EUPHAUSIACEA; PSEUDOALTEROMONAS SP.;

EID: 34250303378     PISSN: 03028933     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00203-007-0220-2     Document Type: Article

References (27)

1. Akoh CC, Lee GC, Liaw YC, Huang TH, Shaw JF (2004) GDSL family of serine esterases/lipases. Prog Lipid Res 43:534-552
2. Arpigny JL, Jaeger KE (1999) Bacterial lipolytic enzymes: classification and properties. Biochem J 343:177-183
3. Bendtsen JD, Nielsen H, Heijne G, Brunak S (2004) Improved prediction of signal peptides: signalP 3.0. J Mol Biol 340:783-795
4. 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
5. Cho H, Cronan Jr JE (1993) Escherichia coli thioesterase I, molecular cloning and sequencing of the structural gene and identification as a periplasmic enzyme. J Biol Chem 268:9238-9245
6. Cygler MJ, Schrag D, Sussman JL, Harel M, Silman I, Gentry MK, Doctor BP (1993) Relationship between sequence conservation and three-dimensional structure in a large family of esterases, lipases, and related proteins. Protein Sci 2:366-382
7. Davis BJ (1964) Disc electrophoresis. II. Methods and application to human serum protein. Ann N Y Acad Sci 121:404-427
8. Diaz P, Prim N, Javier Pastor FI (1999) Direct fluorescence-based lipase activity assay. BioTechniques 27:696-698
9. Flieger A, Neumeister B, Cianciotto NP (2002) Characterization of the gene encoding the major secreted lysophospholipase A of Legionella pneumophila and its role in detoxification of lysophosphatidylcholine. Infect Immun 70:6094-6106
10. Fojan P, Jonson PH, Petersen MTN, Petersen SB (2000) What distinguishes an esterase from a lipase: a novel structural approach. Biochimie 82:1033-1041
11. Gardy JL, Laird MR, Chen F, Rey S, Walsh CJ, Ester M, Brinkman FSL (2005) PSORTb v.2.0: expanded prediction of bacterial protein subcellular localization and insights gained from comparative proteome analysis. Bioinformatics 21:617-623
12. Jaeger KE, Reetz MT (1998) Microbial lipases form versatile tools for biotechnology. Trends Biotechnol 16:396-403
13. Jaeger KE, Eggert T (2002) Lipases for biotechnology. Curr Opin Biotechnol 13:390-397
14. 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
15. Kulakova L, Galkin A, Nakayama T, Nishino T, Esaki N (2004) Cold-active esterase from Psychrobacter sp. Ant300; gene cloning, characterization, and the effects of Gly→Pro substitution near the active site on its catalytic activity and stability. Biochim Biophys Acta 1696:59-65
16. Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685
17. Lo YC, Lin SC, Shaw JF, Liaw YC (2003) Crystal structure of Escherichia coli thioesterase I/protease I/lysophospholipases L1: consensus sequence blocks constitute the catalytic center of SGNH-hydrolases through a conserved hydrogen bond network. J Mol Biol 330:539-551
18. Margesin R, Schinner F (1994) Properties of cold-adapted microorganisms and their potential role in biotechnology. J Biotechnol 33:1-14
19. Ornstein L (1964) Disc electrophoresis. I. Background and theory. Ann N Y Acad Sci 121:321-349
20. Pandey A, Benjamin S, Soccol, Nigam P, Krieger N, Soccol VT (1999) The realm of microbial lipases in biotechnology. Biotechnol Appl Biochem 29:119-131
21. Rashid N, Shimada Y, Ezaki S, Atomi H, Imanaka T (2001) Low-temperature lipase from psychrotrophic Pseudomonas sp. strain KB700A. Appl Environ Microbiol 67:4064-4069
22. Ryu HS, Kim HK, Choi WC, Kim MH, Park SY, Han NS, Oh TK, Lee JK (2006) New cold-adapted lipase from Photobacterium lipolyticum sp. nov. that is closely related to filamentous fungal lipases. Appl Microbiol Biotechnol 70:321-326
23. Sharma R, Chisti Y, Banerjee UC (2001) Production, purification, characterization, and application of lipases. Biotechnol Adv 19:627-662
24. Singh R, Gupta N, Goswami VK, Gupta R (2006) A simple activity staining protocol for lipases and esterases. Appl Microbiol Biotechnol 70:679-682
25. Suzuki T, Nakayama T, Kurihara T, Nishino T, Esaki N (2002) A cold-active esterase with a substrate preference for vinyl esters from a psychrotroph, Acinetobacter sp. Strain no. 6 gene cloning, purification, and characterization. J Mol Catal B Enzym 16:255-263
26. Suzuki T, Nakayama T, Choo DW, Hirano Y, Kurihara T, Nishino T, Esaki N (2003) Cloning, heterologous expression, renaturation, and characterization of a cold-adapted esterase with unique primary structure from a psychrotroph Pseudomonas sp. strain B11-1. Protein Expr Purif 30:171-178
27. WeisburgWG, Barns SM, Pelletier DA, Lane DJ (1991) 16S ribosomal DNA amplification for phylogenetic study. J Bacteriol 173:697-703