Heterologously expressed family 51 α-L-arabinofuranosidases from Oenococcus oeni and Lactobacillus brevis

Applied and Environmental Microbiology

Volumn 77, Issue 4, 2011, Pages 1528-1531

  Michlmayr, Herbert ^a   Schümann, Christina ^a,b   Kulbe, Klaus D ^a   del Hierro, Andrés M ^a  

^a UNIVERSITY OF NATURAL RESOURCES AND LIFE SCIENCES   (Austria)

^b RESEARCH CENTRE APPLIED BIOCATALYSIS   (Austria)

Author keywords

[No Author keywords available]

Indexed keywords

ASPERGILLUS NIGER; FUNCTIONAL PROPERTIES; LACTOBACILLUS BREVIS; OENOCOCCUS OENI; RECOMBINANT ENZYMES;

ALPHA N ARABINOFURANOSIDASE; ALPHA-N-ARABINOFURANOSIDASE; GLYCOSIDASE; RECOMBINANT PROTEIN;

BACTERIUM; ENZYME ACTIVITY; GENE EXPRESSION; RECOMBINATION;

ARTICLE; ASPERGILLUS NIGER; CHEMISTRY; ENZYMOLOGY; GENETICS; LACTOBACILLUS BREVIS; METABOLISM; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE; OENOCOCCUS; POLYACRYLAMIDE GEL ELECTROPHORESIS;

ASPERGILLUS NIGER; ELECTROPHORESIS, POLYACRYLAMIDE GEL; GLYCOSIDE HYDROLASES; LACTOBACILLUS BREVIS; MOLECULAR SEQUENCE DATA; OENOCOCCUS; RECOMBINANT PROTEINS;

ASPERGILLUS NIGER; LACTOBACILLUS BREVIS; OENOCOCCUS OENI;

EID: 79953199815     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.01385-10     Document Type: Article

References (26)

1. Bendtsen, J. D., H. Nielsen, G. Von Heijne, and S. Brunak. 2004. Improved prediction of signal peptides: SignalP 3.0. J. Mol. Biol. 340:783-795.
2. Benson, D. A., I. Karsch-Mizrachi, D. J. Lipman, J. Ostell, and E. W. Sayers. 2009. GenBank. Nucleic Acids Res. 38:D46-D51.
3. Boido, E., A. Lloret, K. Medina, F. Carrau, and E. Dellacassa. 2002. Effect of β-glycosidase activity of Oenococcus oeni on the glycosylated flavor precursors of Tannat wine during malolactic fermentation. J. Agric. Food Chem. 50:2344-2349.
4. Cantarel, B. I., et al. 2009. The Carbohydrate-Active EnZymes database (CAZy): an expert resource for glycogenomics. Nucleic Acids Res. 37:D233-D238.
5. Capaldo, A., M. E. Walker, C. M. Ford, and V. Jiranek. 2011. (-Glucoside metabolism in Oenococcus oeni: cloning and characterisation of the phospho-(-glucosidase bglD. Food Chem. 125:476-482.
6. Gagné, S., et al. 26 October 2010, posting date. Variety and variability of glycosidase activities in an Oenococcus oeni strain collection tested with synthetic and natural substrates. J. Appl. Microbiol. [Epub ahead of print.] doi:10.1111/j.1365-2672.2010.04878.x.
7. Grimaldi, A., E. Bartowsky, and V. Jiranek. 2005. A survey of glycosidase activities of commercial wine strains of Oenococcus oeni. Int. J. Food Microbiol. 105:233-244.
8. Grimaldi, A., E. Bartowsky, and V. Jiranek. 2005. Screening of Lactobacillus spp. and Pediococcus spp. for glycosidase activities that are important in oenology. J. Appl. Microbiol. 99:1061-1069.
9. Hawksworth, G., B. S. Drasar, and M. J. Hill. 1971. Intestinal bacteria and the hydrolysis of glycosidic bonds. J. Med. Microbiol. 4:451-459.
10. Henrissat, B., and G. Davies. 1997. Structural and sequence-based classification of glycoside hydrolases. Curr. Opin. Struct. Biol. 7:637-644.
11. Hofmann, K., and W. Stoffel. 1993. TMbase-a database of membrane spanning proteins segments. Biol. Chem. Hoppe-Seyler 374:166.
12. Hövel, K., et al. 2003. Crystal structure and snapshots along the reaction pathway of a family 51 α-L-arabinofuranosidase. EMBO J. 22:4922-4932.
13. Inácio, J. M., I. Lopes Correia, and I. de Sá-Nogueira. 2008. Two distinct arabinofuranosidases contribute to arabino-oligosaccharide degradation in Bacillus subtilis. Microbiology 154:2719-2729.
14. Knob, A., C. R. F. Terrasan, and E. C. Carmona. 2010. β-Xylosidases from filamentous fungi: an overview. World J. Microbiol. Biotechnol. 26:389-407.
15. Maicas, S., and J. J. Mateo. 2005. Hydrolysis of terpenyl glycosides in grape juice and other fruit juices: a review. Appl. Microbiol. Biotechnol. 67:322-335.
16. Makarova, K., et al. 2006. Comparative genomics of the lactic acid bacteria. Proc. Natl. Acad. Sci. U. S. A. 103:15611-15616.
17. McIlvaine, T. C. 1921. A buffer solution for colorimetric comparison. J. Biol. Chem. 49:183-186.
18. Michlmayr, H., et al. 2010. A β-glucosidase from Oenococcus oeni ATCC BAA-1163 with potential for aroma release in wine: cloning and expression in E. coli. World J. Microbiol. Biotechnol. 26:1281-1289.
19. Numan, M. T., and N. B. Bhosle. 2006. α-L-Arabinofuranosidases: the potential applications in biotechnology. J. Ind. Microbiol. Biotechnol. 33:247-260.
20. Renwick, A. G., and S. M. Tarka. 2008. Microbial hydrolysis of steviol glycosides. Food Chem. Toxicol. 46:S70-S74.
21. Rodríguez, H., J. A. Curiel, J. M. Landete, B. de las Rivas, F. L. de Felipe, C. Gómez-Cordovés, J. M. Mancheño, and R. Muñoz. 2009. Food phenolics and lactic acid bacteria. Int. J. Food Microbiol. 132:79-90.
22. Segel, I. H. 1993. Enzyme kinetics: behavior and analysis of rapid equilibrium and steady state enzyme systems. John Wiley & Sons, New York, NY.
23. Shin, H. Y., S. Y. Park, J. H. Sung, and D. H. Kim. 2003. Purification and characterization of α-L-arabinopyranosidase and α-L-arabinofuranosidase from Bifidobacterium breve K-110, a human intestinal anaerobic bacterium metabolizing ginsenoside Rb2 and Rc. Appl. Environ. Microbiol. 69:7116-7123.
24. Tartoff, K. D., and C. A. Hobbs. 1987. Improved media for growing plasmid and cosmid clones. Bethesda Res. Lab. Focus. 9:12-14.
25. Taylor, E. J., et al. 2006. Structural insight into the ligand specificity of a thermostable family 51 arabinofuranosidase, Araf51, from Clostridium thermocellum. Biochem. J. 395:31-37.
26. Yu, N. Y., et al. 2010. PSORTb 3.0: improved protein subcellular localization prediction with refined localization subcategories and predictive capabilities for all prokaryotes. Bioinformatics 26:1608-1615.