Expression and characterization of an extremely thermostable β-glycosidase (mannosidase) from the hyperthermophilic archaeon Pyrococcus furiosus DSM3638

New Biotechnology

Volumn 28, Issue 6, 2011, Pages 639-648

  Park, Sung H ^a   Park, Kwan H ^b   Oh, Byung C ^c   Alli, Inteaz ^a   Lee, Byong H ^d  

^a MCGILL UNIVERSITY   (Canada)

^b SolarLight Ltd   (South Korea)

^c Gachon University   (South Korea)

^d MCGILL UNIVERSITY   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYTIC EFFICIENCIES; CELLOBIOSE; GALACTO-OLIGOSACCHARIDES; GALACTOSIDASES; GENOMIC ANALYSIS; GLYCOSIDASES; GLYCOSIDE HYDROLASE FAMILY 1; HYPERTHERMOPHILIC ARCHAEON; HYPERTHERMOSTABLE; ISOTHERMAL TITRATION; KINETIC STUDY; MALTOOLIGOSACCHARIDES; MANNOBIOSE; MANNOSIDASE; OPEN READING FRAME; PH OPTIMA; PHARMACEUTICAL APPLICATIONS; PYROCOCCUS FURIOSUS; SENSITIVE METHOD; SODIUM CITRATE; SUBSTRATE SPECIFICITY; THERMOSTABLE GLYCOSIDASE; TRANSGLYCOSYLATION;

AFFINITY CHROMATOGRAPHY; AMINO ACIDS; ENZYME ACTIVITY; ENZYME KINETICS; ESCHERICHIA COLI; GENE ENCODING; SODIUM; SUGARS;

MICROORGANISMS;

4 NITROPHENYL BETA DEXTRO GALACTOPYRANOSIDE; 4 NITROPHENYL BETA DEXTRO GLUCOPYRANOSIDE; 4 NITROPHENYL BETA DEXTRO MANNOPYRANOSIDE; 4 NITROPHENYL BETA DEXTRO XYLOPYRANOSIDE; BETA GALACTOSIDASE; BETA GLYCOSIDASE; BETA MANNOSIDASE; GALACTOSE OLIGOSACCHARIDE; GLYCOSIDASE; GLYCOSIDE HYDROLASE FAMILY 1; MALTOSE OLIGOSACCHARIDE; MANNOSE OLIGOSACCHARIDE; OLIGOSACCHARIDE; PYRANOSIDE; THERMOSTABLE GLYCOSIDASE; UNCLASSIFIED DRUG;

AFFINITY CHROMATOGRAPHY; AMINO ACID SEQUENCE; ARTICLE; CLONING; ENZYME KINETICS; ENZYME SPECIFICITY; ESCHERICHIA COLI; GENOME ANALYSIS; HYDROLYSIS; HYPERTHERMOPHILIC ARCHAEON; MOLECULAR WEIGHT; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN PURIFICATION; PYROCOCCUS FURIOSUS; THERMOSTABILITY;

ARCHAEAL PROTEINS; CATALYSIS; ESCHERICHIA COLI; GENE EXPRESSION; GENES, ARCHAEAL; HOT TEMPERATURE; HYDROGEN-ION CONCENTRATION; MANNANS; MANNOSIDASES; MANNOSIDES; PYROCOCCUS FURIOSUS; RECOMBINANT PROTEINS; SUBSTRATE SPECIFICITY;

ARCHAEA; ESCHERICHIA COLI; PYROCOCCUS FURIOSUS;

EID: 80052960642     PISSN: 18716784     EISSN: 18764347     Source Type: Journal    
DOI: 10.1016/j.nbt.2011.05.002     Document Type: Article

References (26)

1. Adaptation to Life at High Salt Concentrations in Archaea, Bacteria, and Eukarya 2005, Vol. 9. Springer-Verlag.
2. Demirjian D.C., et al. Enzymes from extremophiles. Curr. Opin. Chem. Biol. 2001, 5:144-151.
3. van den Burg B. Extremophiles as a source for novel enzymes. Curr. Opin. Microbiol. 2003, 6:213-218.
4. Stetter K.O. Hyperthermophiles in the history of life. Ciba Found. Symp. 1996, 202:1-10.
5. Adams M.W.W. Enzymes and proteins from organisms that grow near and above 100 degree. Annu. Rev. Microbiol. 1993, 47:627-658.
6. Lee B.H. Carbohydrate-active Enzymes: Structure, Function and Applications 2008, Woodhead Publishing Limited. K.H. Park (Ed.).
7. Duffaud G.D., et al. Purification and characterization of extremely thermostable beta-mannanase, beta-mannosidase, and alpha-galactosidase from the hyperthermophilic eubacterium Thermotoga neapolitana 5068. Appl. Environ. Microbiol. 1997, 63:169-177.
8. Sambrook J., Russell D.W. Molecular Cloning: A Laboratory Manual 2001, Cold Harbor Laboratory Press. 3rd ed.
9. Altschul, et al. Basic local alignment search tool. J. Mol. Biol. 1990, 215:403-410.
10. Thompson J.D., et al. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 1994, 22:4673-4680.
11. Laemmli U.K., et al. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
12. Craven G.R., et al. Purification, composition, and molecular weight of the beta-galactosidase of Escherichia coli K12. J. Biol. Chem. 1965, 240:2468-2477.
13. Chadwick R.W., et al. Possible errors in assay for beta-glycosidase activity. Appl. Environ. Microbiol. 1995, 61:820-822.
14. Bradford M.M., et al. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72:248-254.
15. Todd M.J., Gomez J. Enzyme kinetics determined using calorimetry: a general assay for enzyme activity. Anal. Biochem. 2001, 296:179-187.
16. Maeder D.L., et al. Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences. Genetics 1999, 152:1299-1305.
17. Verhees C.H., et al. Biochemical adaptations of two sugar kinases from the hyperthermophilic archaeon Pyrococcus furiosus. Biochem. J. 2002, 366:121-127.
18. Kengen S.W., et al. Purification and characterization of an extremely thermostable beta-glucosidase from the hyperthermophilic archaeon Pyrococcus furiosus. Eur. J. Biochem./FEBS 1993, 213:305-312.
19. Bauer M.W., et al. Comparison of a beta-glucosidase and a beta-mannosidase from the hyperthermophilic archaeon Pyrococcus furiosus. Purification, characterization, gene cloning, and sequence analysis. J. Biol. Chem. 1996, 271:23749-23755.
20. Grogan D.W. Evidence that β-galactosidase of Sulfolobus solfataricus is only one of several activities of a thermostable β-d-glycosidase. Appl. Environ. Microbiol. 1991, 57:1644-1649.
21. Henrissat B. A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 1991, 280:309-316.
22. Shockley K.R., et al. Heat shock response by the hyperthermophilic archaeon Pyrococcus furiosus. Appl. Environ. Microbiol. 2003, 69:2365-2371.
23. Chhabra S.R., et al. Regulation of endo-acting glycosyl hydrolases in the hyperthermophilic bacterium Thermotoga maritima grown on glucan- and mannan-based polysaccharides. Appl. Environ. Microbiol. 2002, 68:545-554.
24. Moracci M., et al. Expression of the thermostable beta-galactosidase gene from the archaebacterium Sulfolobus solfataricus in Saccharomyces cerevisiae and characterization of a new inducible promoter for heterologous expression. J. Bacteriol. 1992, 174:873-882.
25. Opassiri R., et al. Analysis of rice glycosyl hydrolase family 1 and expression of Os4bglu12 beta-glucosidase. BMC Plant Biol. 2006, 6:33-52.
26. Kaper T., et al. Substrate specificity engineering of β-mannosidase and β-glucosidase from Pyrococcus by exchange of unique active site residues. Biochemistry 2002, 41:4147-4155.