Cloning and expression of the β-galactosidase genes from Lactobacillus reuteri in Escherichia coli

Journal of Biotechnology

Volumn 129, Issue 4, 2007, Pages 581-591

  Nguyen, Thu Ha ^a,b   Splechtna, Barbara ^a,b   Yamabhai, Montarop ^c   Haltrich, Dietmar ^b   Peterbauer, Clemens ^b  

^a RESEARCH CENTRE APPLIED BIOCATALYSIS   (Austria)

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

^c SURANAREE UNIVERSITY OF TECHNOLOGY   (Thailand)

Author keywords

Galactosidase; Lactobacillus; Recombinant expression; Transglycosylation

Indexed keywords

LACTOBACILLUS REUTERI; RECOMBINANT EXPRESSION; RNA POLYMERASE; TRANSGLYCOSYLATION; TRANSLATIONAL COUPLING;

AMINO ACIDS; ENZYME KINETICS; ESCHERICHIA COLI; GENE ENCODING; POLYPEPTIDES; RNA;

CLONING;

BETA GALACTOSIDASE; RECOMBINANT ENZYME; RNA POLYMERASE; T7 RNA POLYMERASE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; ENZYME PURIFICATION; ESCHERICHIA COLI; GENE; GENE EXPRESSION SYSTEM; GENE OVEREXPRESSION; GLYCOSYLATION; LACL GENE; LACM GENE; LACTOBACILLUS REUTERI; MOLECULAR CLONING; MOLECULAR WEIGHT; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROMOTER REGION; REACTION ANALYSIS; SEQUENCE ANALYSIS;

AMINO ACID SEQUENCE; BASE SEQUENCE; BETA-GALACTOSIDASE; CLONING, MOLECULAR; DNA, BACTERIAL; ESCHERICHIA COLI; GENE AMPLIFICATION; GENE EXPRESSION REGULATION, BACTERIAL; GENE EXPRESSION REGULATION, ENZYMOLOGIC; LACTOBACILLUS REUTERI; POLYMERASE CHAIN REACTION; RECOMBINANT PROTEINS;

ESCHERICHIA COLI; LACTOBACILLUS; LACTOBACILLUS REUTERI;

EID: 34247104532     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2007.01.034     Document Type: Article

References (29)

1. Benno Y., Endo K., Mizutani T., Namba Y., Komori T., and Mituoka T. Comparison of fecal microflora of elderly persons in rural and urban areas of Japan. Appl. Environ. Microbiol. 55 (1989) 1100-1105
2. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
3. Cummings J.H., Macfarlane G.T., and Englyst H.N. Prebiotic digestion and fermentation. Am. J. Clin. Nutr. 73 Suppl. (2001) 415S-420S
4. Cupples C.G., Miller J.H., and Huber R.E. Determination of the roles of Glu-461in β-galactosidase (Escherichia coli) using site-specific mutagenesis. J. Biol. Chem. 265 (1990) 5512-5518
5. David S., Stevens H., van Riel M., Simons G., and de Vos W.M. Leuconostoc lactis β-galactosidase is encoded by two overlapping genes. J. Bacteriol. 174 (1992) 4475-4481
6. De Man J.D., Rogosa M., and Sharpe M.E. A medium for the cultivation of Lactobacilli. J. Appl. Bacteriol. 23 (1960) 130-135
7. Fortina M.G., Ricci G., Mora D., Guglielmetti S., and Manichini P.L. Unusual organization for lactose and galactose gene clusters in Lactobacillus helveticus. Appl. Environ. Microbiol. 69 (2003) 3238-3243
8. Gebler J.C., Aebersold R., and Withers S.G. Glu-537, not Glu-461, is the nucleophile in the active site of (lacZ) β-galactosidase from Escherichia coli. J. Biol. Chem. 267 (1992) 11126-11130
9. Germond J.-E., Lapierre L., Delley M., Mollet B., Felis G.E., and Dellaglio F. Evolution of the bacterial species Lactobacillus delbrueckii: a partial genomic study with reflections on prokaryotic species concept. Mol. Biol. Evol. 20 (2003) 93-104
10. Gibson G.R., and Roberfroid M.B. Dietary modulation of the human colonic microbiota: introducing the concept of prebiotics. J. Nutr. 125 (1995) 1401-1412
11. Henrissat B. A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 280 (1991) 309-316
12. Jacobson R.H., Zhang X.-J., DuBose R.F., and Matthews B.W. Three-dimensional structure of β-galactosidase from E. coli. Nature 369 (1994) 761-766
13. Kabuki T., Saito T., Kawai Y., Uemura J., and Itoh T. Production, purification and characterization of reutericin 6, a bacteriocin with lytic activity produced by Lactobacillus reuteri LA6. Int. J. Food Microbiol. 34 (1997) 145-156
14. Kalnins A., Otto K., Ruther U., and Muller-Hill B. Sequence of the lacZ gene of Escherichia coli. EMBO J. 2 (1983) 593-597
15. Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., Kuipers O.P., Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W., Stiekema W., Lankhorst R.M., Bron P.A., Hoffer S.M., Groot M.N., Kerkhoven R., de Vries M., Ursing B., de Vos W.M., and Siezen R.J. Complete genome sequence of Lactobacillus plantarum WCFS1. Proc. Natl. Acad. Sci. U.S.A. 100 (2003) 1990-1995
16. Kunst A., Draeger B., and Ziegernhorn J. Colorimetric methods with glucose oxidase and peroxidase. In: Bergmeyer H.U., Bergmeyer J., and Graßl M. (Eds). Methods of Enzymatic Analysis. 3rd ed. (1988), VCH Publishers, Weinheim, Germany 178-185
17. Mizobuchi M., and Frohman L.A. Rapid amplification of genomic DNA ends. Biotechniques 15 (1993) 214-216
18. Nicholas, K.B., Nicholas, Jr., H.B., Deerfield, II, D.W., 1997. GeneDoc: Analysis and Visualization of Genetic Variation. EMBNEW.NEWS 4, 14. http://www.psc.edu/biomed/genedoc.
19. Nakayama T., and Amachi T. β-Galactosidase, enzymology. In: Flickinger M.C., and Drew S.W. (Eds). Encyclopedia of Bioprocess Technology: Fermentation, Biocatalysis, and Bioseparation 3 (1999), John Wiley and Sons, New York, NY 1291-1305
20. Nguyen T.-H., Splechtna B., Steinböck M., Kneifel W., Lettner H.P., Kulbe K.D., and Haltrich D. Purification and characterization of two novel β-galactosidases from Lactobacillus reuteri. J. Agric. Food Chem. 54 (2006) 4989-4998
21. Obst M., Meding E.R., Vogel R.F., and Hammes W.P. Two genes encoding the β-galactosidase of Lactobacillus sake. Microbiology 141 (1995) 3059-3066
22. Pivarnik L.F., Senegal A.G., and Rand A.G. Hydrolytic and transgalactosylic activities of commercial β-galactosidase (lactates) in food processing. In: Kinsella J.E., and Taylor S.L. (Eds). Advances in Food and Nutrition Research vol. 38 (1995), Academic Press 1-102
23. Pridmore R.D., Berger B., Desiere F., Vilanova D., Barretto C., Pittet A.-C., Zwahlen M.-C., Rouvet M., Barrangou R., Altermann E., Mollet B., Mercenier A., Klaenhammer T., Arigoni F., and Schell M.A. The genome sequence of the probiotic intestinal bacterium Lactobacillus johnsonii NCC 533. Proc. Natl. Acad. Sci. U.S.A. 101 (2004) 2512-2517
24. Rastall R.A., and Maitin V. Prebiotics and synbiotics: towards the next generation. Curr. Opin. Biotechnol. 13 (2002) 490-496
25. Ring M., and Huber R.E. Multiple replacements establish the importance of Tyrosine-503 in β-galactosidase (Escherichia coli). Arch. Biochem. Biophys. 283 (1990) 342-350
26. Splechtna B., Nguyen T.-H., Steinböck M., Kulbe K.D., Lorenz W., and Haltrich D. Production of prebiotic galacto-oligosaccharides from lactose using β-galactosidases from Lactobacillus reuteri. J. Agric. Food Chem. 54 (2006) 4999-5006
27. Sung H.W., Chen C.N., Liang H.F., and Hong M.H. A natural compound (reuterin) produced by Lactobacillus reuteri for biological-tissue fixation. Biomaterials 24 (2003) 1335-1347
28. Suzuki, M., Saito, T., Konno, K., Kamio, Y., Itoh, T., 1997. β-Galactosidase from Lactobacillus acidophilus JCM1229 is consisted of two nonidentical subunits (unpublished). EMBL/GenBank/DDBJ Databases, link: http://us.expasy.org/cgi-bin/niceprot.pl?O07684.
29. Thompson, J.D., Gibson, T.J., Plewniak, F., Jeanmougin, F., Higgins, D.G., 1997. The ClustalX windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 24, 4876-4882 (link: http://bips.u-strasbg.fr/en/Documentation/ClustalX/).