63
Views
19
CrossRef citations to date
0
Altmetric
Original Article

Characterization of the L. manihotivorans α-Amylase Gene

, , &
Pages 27-37 | Received 30 Jun 2000, Published online: 11 Jul 2009

References

  • Agati A., Guyot J. P., Morlon-Guyot J., Hounhouigan J. Isolation and characterization of new amylolytic strains of Lactobacillus fermentum from fermented maize doughs (mawè and ogi) from Benin. Journal of Applied Microbiology 1998; 85: 512–520
  • Aguilar G, Morlon-Guyot J., Trejo-Aguilar B., Guyot J-P. Purification and characterization of an extracellular α-amylase produced by Lactobacillus manihotivo-rans LMG 10810T, an amylolytic lactic acid bacterium. Enzyme and Microbial Technology 2000; 27: 406–416
  • Altschul S. F., Gish W., Miller W., Myers E. W., Lipman D. J. Basic local alignment search tool. Journal of Molecular Biology 1990; 215: 403–10
  • Bohak I., Back W., Richter L., Eirman M., Ludwing W., Schleifer K. H. Lactobacillus amylolyticus sp nov., isolated from beer malt and beer wort. Systematic and Applied Microbiology 1998; 21: 360–364
  • Burgess-Cassler A., Imam S. Partial purification and comparative characterization of α-amylase secreted by Lactobacillus amylovorus. Current Microbiology 1991; 23: 207–213
  • Castillo C, Gomez Suarez M., Morlon-Guyot J. Comparison of amylolytic properties of Lactobacillus amylovorus and of Lactobacillus amylophilus. Applied Microbiology and Biotechnology 1993; 40: 266–269
  • Dayhoff M. O. Atlas of protein sequence and structure. National Biomedical Research Foundation, Washington, D.C. 1979; volume 5, Supplement 3
  • De Man J. C., Rogosa M., Sharpe M. E. A medium for the cultivation of lactobacilli. Journal of Applied Bacteriology 1960; 23: 130–135
  • Dufour D., Brabet C, Zakhia N., Chuzel G. Influence de la fermentation et du séchage solaire sur l'acquisition du pouvoir de panification de ľamidon aigre de manioc. Transformations alimentaires du Manioc, T. A. Egbe, A. Brauman, D. Griffon, S. S. Treche. ORSTOM Editions, Paris 1995; 399–416
  • Felsenstein J. PHYLIP (phylogenetic inference package), version 3.51c. Departement of genetics, University of Washington, Seattle 1993
  • Fitzsimons A., Hols P., Jore J., Leer R. J., O'Connell M., Delcour J. Development of an amylolytic Lactobacillus plantarum silage strain expressing the Lactobacillus amylovorus α-amylase gene. Applied and Environmental Microbiology 1994; 60: 3529–3535
  • Gasson M. J., Davies F. L. High frequency conjugation associated with Steptococcus lactis doner cell aggregation. Journal of Bacteriology 1980; 143: 1260–1264
  • Giraud E., Brauman A., Keleke S., Lelong B., Raim-Bault M. Isolation and physiological study of an amylolytic strain of Lactobacillus plantarum. Applied Microbiology and Biotechnology 1991; 36: 379–383
  • Giraud E., Champailler A., Raimbault M. Degradation of raw starch by a wild amylolytic strain of Lactobacillus plantarum. Applied and Environmental Microbiology 1993; 60: 4319–4323
  • Giraud E., Cuny G. Molecular characterization of the α-amylase genes of Lactobacillus plantarum A6 and Lactobacillus amylovorus reveals an unusual 3′ end structure with direct tandem repeats and suggests a common evolutionary origin. Gene 1997; 198: 149–157
  • Guyot J. P., Calderon M., Morlon-Guyot J. Effect of pH control on lactic acid fermentation of starch by Lactobacillus manihotivorans LMG 18010T. Journal of Applied Microbiology 2000; 88: 176–182
  • Hueck C. J., Hillen W. Catabolite repression in Bacillus subtilis a global regulatory mechanism for the gram-positive bacteria?. Molecular Microbiology 1995; 15: 395–401
  • Iefuji H, Chino M., Kato M., Iimura Y. Raw-starch-digesting and thermostable α-amylase from the yeast Cryptococcus sp. S-2: Purification, characterization, cloning and sequencing. Biochemical Journal 1996; 318: 989–996
  • Jack R. W., Tagg J. R., Ray B. Bacteriocins of gram-positive bacteria. Microbiological Reviews 1995; 59: 171–200
  • Jore J. P.M., DeParasis J. Studies on the α-amylase of Lactobacillus amylovorus as a model for heterologous protein secretion by lactobacilli. FEMS Microbiological Reviews 1993; 12: 26
  • McClelland M., Jones R., Patel Y., Nelson M. Restriction endonucleases for pulsed field mapping of bacterial genomes. Nucleic Acids Research 1987; 15: 5985–6005
  • Morlon-Guyot J., Guyot J. P., Pot B., Jacobé de Haut I., Raimbault M. L. manihotivorans sp. nov., a new starch-hydrolysing lactic acid bacterium isolated from cassava sour starch fermentation. International Journal of Systematic Bacteriology 1997; 48: 1101–1109
  • Nakamura L. K. Lactobacillus amylovorus, a new starch hydrolysing species from cattle waste-corn fermentations. International Journal of Systematic Bacteriology 1981; 31: 56–63
  • Nakamura L. K., Crowell C D. Lactobacillus amylophilus, a new starch-hydrolysing species from swine waste-corn fermentation. Development In Industrial Microbiology 1979; 20: 535–540
  • Olympia M., Fukuda H., Ono H., Kaneko Y., Takano M. Characterization of starch-hydrolyzing lactic acid bacteria isolated from a fermented fish and rice food, burong isda, and its amylolytic enzyme. Journal of Fermentation and Bioengineering 1995; 80: 124–130
  • Rodriguez Sanoja R., Morlon-Guyot J., Jore J., Pintado J., Juge N., Guyot J. P. Comparative characterization of complete and truncated forms of Lactobacillus amylovorus α-amylase and role of the C-terminal direct repeats in raw starch binding. Applied Environmental Microbiology, 66: 3350–3356
  • Rogers J. C. Two barley α-amylase gene families are regulated differently in aleurone cells. Journal of Biological Chemistry 1985; 221: 3731–3738
  • Rumbak E., Rawlings D. E., Lindsey G. G., Woods D. R. Cloning, nucleotide sequence, and enzymatic characterization of an α-amylase from the ruminal bacterium Butyvibrio fibrisolvens H17c. Journal of Bacteriology 1991; 173: 4203–211
  • Saitou N., Nei M. The neighbour-joining method: a new method for reconstructing phylogenetic trees. Molecular and Biological Evolution 1987; 4: 406–425
  • Satoh E., Uchimura T., Kudo T., Komagata K. Purification, characterization, and nucleotide sequence of an intracellular maltotriose-producing alpha-amylase from Streptococcus bovis 148. Applied Environmental Microbiology 1997; 63: 4941–4944
  • Svensson B., Jespersen H., Sierks M. R., MacGregor E. A. Sequence homology between putative raw-starch binding domains from different starch-degrading enzymes. Biochemical Journal 1989; 264: 309–11
  • Thompson J. D., Higgins D. G., Gibson T. J. CLUS-TAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice. Nucleic Acids Research 1994; 22: 4673–4680
  • von Heijne G. Signal sequences: the limits of variation. Journal of Molecular Biology 1985; 184: 99–105
  • Wind R. D., Liebl W., Buitelaar R. M., Penninga D., Spreina A., Dijkhuinen L., Bahl H. Cyclo-dextrin formation by the thermostable α-amylase of Thermoanaerobacterium thermosulfurigenes EMI and reclassification of the enzyme as a cyclodextrin glycosyl-transferase. Applied and Environmental Microbiology 1995; 61: 1257–1265
  • Wren B. W. A family of clostridial and streptococcal ligand-binding proteins with conserved C-terminal repeat sequences. Molecular Microbiology 1991; 5: 797–803
  • Yang M., Galizzi A., Henner D. J. Nucleotide sequence of the amylase gene from Bacillus subtilis. Nucleic Acids Research 1983; 11: 237–249

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.