Alpha-amylase starch binding domains: Cooperative effects of binding to starch granules of multiple tandemly arranged domains

Applied and Environmental Microbiology

Volumn 73, Issue 12, 2007, Pages 3833-3837

  Guillen D ^a   Santiago, M ^a,b   Linares, L ^a   Perez R ^a   Morlon, J ^a,c   Ruiz, B ^a   Sanchez S ^a   Rodriguez Sanoja R ^a  

^a INSTITUTO DE INVESTIGACIONES BIOMÉDICAS   (Mexico)

^b UNIVERSIDAD AUTÓNOMA DE BAJA CALIFORNIA   (Mexico)

^c UNIVERSITÉ DE MONTPELLIER   (France)

Author keywords

[No Author keywords available]

Indexed keywords

ADDITIVES; ADSORPTION; BACTERIA; BINDING SITES; PEPTIDES; SOLUBILITY;

LACTOBACILLUS AMYLOVORUS; PROTEIN BINDING ASSAYS; STARCH BINDING DOMAIN (SBD);

STARCH;

AMYLASE; STARCH;

ADSORPTION; AMINO ACID; ASSAY; BACTERIUM; ENZYME; PEPTIDE; PROTEIN; STARCH;

ADSORPTION; ALPHA AMYLASE STARCH BINDING DOMAIN; AMINO ACID SEQUENCE; ARTICLE; BINDING AFFINITY; BINDING ASSAY; LACTOBACILLUS AMYLOVORUS; NONHUMAN; NUCLEOTIDE SEQUENCE; PROCESS OPTIMIZATION; PROTEIN CARBOHYDRATE INTERACTION; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; SEQUENCE ANALYSIS;

ADSORPTION; ALPHA-AMYLASE; DNA PRIMERS; ELECTROPHORESIS, POLYACRYLAMIDE GEL; LACTOBACILLUS ACIDOPHILUS; PLASMIDS; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; STARCH;

LACTOBACILLUS AMYLOVORUS;

EID: 34250810801     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.02628-06     Document Type: Article

References (28)

1. Belshaw, N. J., and G. Williamson. 1990. Production and purification of a granular-starch-binding domain of glucoamylase 1 from Aspergillus niger. FEBS Lett. 269:350-353.
2. Blakesley, R. W., and J. A. Boezi. 1977. A new staining technique for protein in polyacrylamide gels using Coomassie Brilliant Blue G-250. Anal. Biochem. 82:580-582.
3. Bolam, D. N., A. Ciruela, S. McQueen-Mason, P. Simpson, M. P. Williamson, J. E. Rixon, A. Boraston, G. P. Hazlewood, and H. J. Gilbert. 1998. Pseudomonas cellulose-binding domains mediate their effects by increasing enzyme substrate proximity. Biochem. J. 331:775-781.
4. Bolam, D. N., H. Xie, P. White, P. J. Simpson, S. M. Hancock, M. P. Williamson, and H. J. Gilbert. 2001. Evidence for synergy between family 2b carbohydrate binding modules in Cellulomonas fimi xylanase 11A. Biochemistry 40:2468-2477.
5. Boraston, A. B., M. Healey, J. Klassen, E. Ficko-Blean, A. Lammerts van Bueren, and V. Law. 2006. A structural and functional analysis of α-glucan recognition by family 25 and 26 carbohydrate-binding modules reveals a conserved mode of starch recognition. J. Biol. Chem. 281:587-598.
6. Boraston, A. B., B. W. McLean, G. Chen, A. Li, R. A. Warren, and D. G. Kilburn. 2002. Co-operative binding of triplicate carbohydrate binding modules from a thermophilic xylanase. Mol. Microbiol. 43:187-194.
7. 3 binding domain, and Trichoderma reesei CBHI on avicel and bacterial microcrystalline cellulose. Biores. Technol. 60:169-178.
8. Combet, C., C. Blanchet, C. Geourjon, and G. Deléage. 2000. NPS@: network protein sequence analysis. Trends Biochem. Sci. 25:147-150.
9. De Man, J. C., M. Rogosa, and M. E. Sharpe. 1960. A medium for the cultivation of lactobacilli. J. Appl. Bacteriol. 23:130-135.
10. Florencio, J., D. Eiras-Stofella, C. Soccol, M. Raimbault, J. P. Guyot, and J. Fontana. 2000. Lactobacillus plantarum amylase acting on crude starch granules. Appl. Biochem. Biotechnol. 84:721-730.
11. Giraud, E., and G. Cuny. 1997. 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 198:149-157.
12. Janeček, S., B. Svensson, and E. A. MacGregor. 2003. Relation between domain evolution, specificity, and taxonomy of the α-amylase family members containing a C-terminal starch binding-domain. Eur. J. Biochem. 270:635-645.
13. Janeček, S., and J. Ševčik. 1999. The evolution of starch-binding domain. FEBS Lett. 456:119-125.
14. Kyriacou, A., R. Neufeld, and C. R. MacKenzie. 1988. Effect of physical parameters on the adsorption characteristics of fractionated Trichoderma reesei cellulase components. Enzyme Microb. Technol. 10:675-681.
15. Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
16. Leloup, V. M., P. Colonna, and S. G. Ring. 1991. α-Amylase adsorption on starch crystallites. Biotechnol. Bioeng. 38:127-134.
17. Linder, M., I. Salovuori, L. Ruohonen, and T. Teeri. 1996. Characterization of a double cellulose binding domain. J. Biol. Chem. 271:21268-21272.
18. Machovič, M., B. Svensson, E. A. MacGregor, and S. Janeček. 2005. A new clan of CBM families based on bioinformatics of starch-binding domains from families CBM20 and CBM21. FEBS J. 272:5497-5513.
19. Mihlbachler, K., M. A. De Jesus, K. Kaczmarski, M. J. Sepaniak, A. Seidel-Morgenstern, and G. Guiochon. 2006. Adsorption behavior of the (+/-)-Troger's base enantiomers in the phase system of a silica-based packing coated with amylose tri(3,5-dimethyl carbamate) and 2-propanol and molecular modeling interpretation. J. Chromatogr. A 1113:148-161.
20. Morlon-Guyot, J., F. Mucciolo-Roux, R. Rodríguez-Sanoja, and J. P. Guyot. 2001. Characterization of the L. manihotivorans α-amylase gene. DNA Seq. 12:27-37.
21. Nölling, J., G. Breton, M. V. Omelchenko, K. S. Makarova, Q. Zeng, R. Gibson, H. M. Lee, J. A. Dubois, D. Qiu, and J. Hitti. 2001. Genome sequence and comparative analysis of the solvent-producing bacterium Clostridium acetobutylicum. J. Bacteriol. 183:4823-4838.
22. Rodríguez-Sanoja, R., J. Morlon, J. Jore, J. Pintado, N. Juge, and J. P. Guyot. 2000. Comparative characterization of complete and truncated forms of Lactobacillus amylovorus α-amylase and role of the C-terminal direct repeats in raw starch binding. Appl. Environ. Microbiol. 66:3350-3356.
23. Rodríguez-Sanoja, R., N. Oviedo, and S. Sánchez. 2005. Microbial starch-binding domain. Curr. Opin. Microbiol. 8:260-267.
24. Rodríguez-Sanoja, R., B. Ruiz, J. P. Guyot, and S. Sánchez. 2005. Starch binding domain affects catalysis in two Lactobacillus α-amylases. Appl. Environ. Microbiol. 71:297-302.
25. Sambrook, J., E. F. Fritsch, and T. Maniatis. 1989. Molecular cloning: a laboratory manual, 2nd ed. Cold. Spring Harbor Laboratory, Cold Spring Harbor, NY.
26. Santiago, M., L. Linares, S. Sanchez, and R. Rodríguez- Sanoja. 2005. Functional characteristics of the starch binding domain of Lactobacillus amylovorus α-amylase. Biologia (Bratisl.) 60:111-114.
27. Sumitani, J., T. Tottori, T. Kawaguchi, and M. Arai. 2000. New type of starch-binding domain: the direct repeat motif in the C-terminal region of Bacillus sp. no. 195 α-amylase contributes to starch binding and raw starch degrading. Biochem. J. 350:477-484.
28. Williamson, G., N. J. Belshaw, and M. P. Williamson. 1992. O-Glycosylation in Aspergillus glucoamylase. Conformation and role in binding. Biochem. J. 282:423-428.