Thermostability enhancement and change in starch hydrolysis profile of the maltohexaose-forming amylase of Bacillus stearothermophilus US100 strain

Biochemical Journal

Volumn 394, Issue 1, 2006, Pages 51-56

  Ben Ali, Mamdouh ^a   Khemakhem, Bassem ^a   Robert, Xavier ^b   Haser, Richard ^b   Bejar, Samir ^a  

^a CENTRE DE BIOTECHNOLOGIE DE SFAX   (Tunisia)

^b UNIVERSITÉ LYON 1   (France)

Author keywords

amylase; Bacillus stearothermophilus; Starch hydrolysis profile; Thermostability

Indexed keywords

BACTERIA; BIOCHEMISTRY; HYDROLYSIS; MUTAGENESIS; THERMOSTATS;

Α-AMYLASE; BACILLUS STEAROTHERMOPHILUS; STARCH HYDROLYSIS PROFILE; THERMOSTABILITY;

ENZYMES;

AMYLASE; MALTOSE; MALTOTRIOSE; STARCH;

ARTICLE; BACTERIAL STRAIN; DNA ISOLATION; GEOBACILLUS STEAROTHERMOPHILUS; HYDROLYSIS; MUTAGENESIS; MUTATION; NONHUMAN; PLASMID; PRIORITY JOURNAL; PROTEIN STRUCTURE; THERMAL STIMULATION; THERMOSTABILITY; WILD TYPE;

AMINO ACID SUBSTITUTION; AMYLASES; BACILLUS STEAROTHERMOPHILUS; CALCIUM; ENZYME STABILITY; HEAT; HYDROLYSIS; MODELS, MOLECULAR; MUTATION; OLIGOSACCHARIDES; PROTEIN STRUCTURE, TERTIARY; STARCH;

BACILLUS LICHENIFORMIS; BACTERIA (MICROORGANISMS); GEOBACILLUS STEAROTHERMOPHILUS;

EID: 32944455102     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20050726     Document Type: Article

References (36)

1. Davies, G. and Henrissat, B. (1995) Structures and mechanisms of glycosyl hydrolases. Structure 3, 853-859
2. Svensson, B., Tovborg Jensen, M., Mori, H., Sass Bak-Jensen, K., Bønsager, B., Nielsen, P. K., Birte Kramhøft, B., Praetorius-Ibba, M., Nøhr, J., Juge, N. et al. (2002) Fascinating facets of function and structure of amylolytic enzymes of glycoside hydrolase family 13. Biologia (Bratislava) 57 (Suppl. 11), 5-19
3. Janecek, S. (2002) How many conserved sequence regions are there in the α-amylase family? Biologia (Bratislava) 57 (Suppl. 11), 29-41
4. Nielsen, J. E, and Borchert, T. V. (2000) Protein engineering of bacterial α-amylases. Biochim. Biophys. Acta. 1543, 253-274
5. Marchal, L. M., Beeftink, H. H. and Tramper, J. (1999) Towards a rational design of commercial maltodextrins. Trends Food Sci. Tech. 10, 345-355
6. Kanai, R., Haga, K., Akiba, T., Yamane, K. and Harata, K. (2004) Biochemical and crystallographic analyses of maltohexaose-producing amylase from alkalophilic Bacillus sp. 707. Biochemistry 44, 14047-14056
7. Momma, M. and Fujimoto, Z. (2004) Expression, crystallization and preliminary X-ray crystallographic studies of Klebsiella pneumoniae maltohexaose-producing α-amylase. Acta Crystallogr. Sect. D Biol. Crystallogr. 60, 2352-2354
8. Mezaki, Y., Katsuya, Y., Kubota, M. and Matsuura, Y. (2001) Crystallization and structural analysis of intact maltotetraose-forming exo-amylase from Pseudomonas stutzeri. Biosci. Biotechnol. Biochem. 1, 222-225
9. Buisson, G., Duee, E., Haser, R. and Payan, F. (1987) Three dimensional structure of porcine pancreatic α-amylase at 2.9Å resolution. Role of calcium in structure and activity. EMBO J. 6, 3909-3916
10. Declerck, N., Machius, M., Joyet, P., Wiegand, G., Huber, R. and Gaillardin, C. (2002) Engineering the thermostability of Bacillus licheniformis α-amylase. Biologia (Bratislava) 57 (Suppl. 11), 203-211
11. Joyet, P., Declerck, N. and Gaillardin, C. (1992) Hyperthermostable variants of a highly thermostable α-amylase. Biotechnology 10, 1579-1583
12. Declerck, N., Joyet, P., Trosset, J. Y., Garnier, J. and Gaillardin, C. (1995) Hyperthermostable mutants of Bacillus licheniformis α-amylase: multiple amino acid replacements and molecular modelling. Protein Eng. 8, 1029-1037
13. Declerck, N., Machius, M., Chambert, R., Wiegand, G., Huber, R. and Gaillardin, C. (1997) Hyperthermostable mutants of Bacillus licheniformis α-amylase: thermodynamic studies and structural interpretation. Protein Eng. 10, 541-549
14. Declerck, N., Machius, M., Joyet, R, Wiegand, G., Huber, R. and Gaillardin, C. (2003) Hyperthermostabilization of Bacillus licheniformis α-amylase and modulation of its stability over a 50°C temperature range. Protein Eng. 16, 287-293
15. Igarashi, K., Hagihara, H. and Ito, S. (2003) Protein engineering of detergent α-amylases. Trends Glycosci. Glycotechnol. 82, 101-114
16. Ben Ali, M., Mezghani, M. and Bejar, S. (1999) A thermostable maltohexaose producing amylase from a new isolated B. stearothermophilus: study of activity and molecular cloning of the corresponding gene. Enzyme Microb. Tech. 24, 584-589
17. Ben Ali, M., Mhiri, S., Mezghani, M. and Bejar, S. (2001) Purification and sequence analysis of the atypical maltohexaose-forming α-amylase of the B. stearothermophilus US100. Enzyme Microb. Technol. 28, 537-542
18. Jørgensen, P. L., Poulsen, G. B. and Diderichsen, B. (1991) Cloning of a chromosomal α-amylase gene from Bacillus stearothermophilus. FEMS Microbiol. Lett. 77, 271-275
19. Miller, G. L. (1959) Use of dinitrosalicylic acid reagent for determination of reducing sugars. Anal. Chem. 31, 426-428
20. Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254
21. 4. Nature (London) 227, 680-685
22. Sambrook, J., Fritsch, E. F. and Maniatis, T. (1989) Molecular Cloning: A Laboratory Manual, Cold Spring Harbor Laboratory, Cold Spring Harbor
23. Ausubel, F. M., Brent, R., Kingston, R. E., Moore, D. D., Seidman, J. G., Smith, J. A. and Struhl, K. (1993) Current Protocols in Molecular Biology, Greene Publishing Associates and Wiley, New York
24. Schwede, T., Kopp, J., Guex, N. and Peitsch, M. C. (2003) SWISS-MODEL: an automated protein homology-modelling server. Nucleic Acids Res. 31, 3381-3385
25. Suvd, D., Takase, K., Fujimoto, Z., Matsumura, M. and Mizuno, H. (2000) Purification, crystallization and preliminary X-ray crystallographic study of α-amylase from Bacillus stearothermophilus. Acta Crystallogr. Sect. D Biol. Crystallogr. 56, 200-202
26. Brzozowski, A. M., Lawson, D. M., Turkenburg, J. P., Bisgaard-Frantzen, H., Svendsen, A., Borchert, T. V., Dauter, Z., Wilson, K. S. and Davies, G. J. (2000) Structural analysis of a chimeric bacterial α-amylase. Biochemistry 39, 9099-9107
27. Machius, M., Wiegand, G. and Huber, R. (1995) Crystal structure of calcium-depleted Bacillus licheniformis α-amylase at 2.2 Å resolution. J. Mol. Biol. 246, 545-559
28. Machius, M., Declerck, N., Huber, R. and Wiegand, G. (1998) Activation of Bacillus licheniformis α-amylase through a disorder → order transition of the substrate-binding site mediated by a calcium-sodium-calcium metal triad. Structure 6, 281-292
29. Suvd, D., Fujimoto, Z., Takase, K., Matsumura, M. and Mizuno, H. (2001) Crystal structure of Bacillus stearothermophilus α-amylase: possible factors determining the thermostability. J. Biochem. (Tokyo) 129, 461-468
30. Emori, M., Takagi, M., Maruo, B. and Yano, K. (1990) Molecular cloning, nucleotide sequencing, and expression of the Bacillus subtilis (natto) IAM1212 α-amylase gene, which encodes an α-amylase structurally similar to but enzymatically distinct from that of B. subtilis 2633. J. Bacteriol. 172, 4901-4908
31. Suzuki, Y., Ito, N., Yuuki, T., Yamagata, H. and Udaka, S. (1989) Amino acid residues stabilizing a Bacillus α-amylase against irreversible thermoinactivation. J. Biol. Chem. 264, 18933-18938
32. Igarashi, K., Hatada, Y, Ikawa, K., Araki, H., Ozawa, T., Kobayashi, T., Ozaki, K. and Ito, S. (1998) Improved thermostability of an arginine-glycine residue is caused by enhanced calcium binding. Biochem. Biophys. Res. Commun. 248, 372-377
33. Bisgaard-Frantzen, H., Svendsen, A., Norman, B., Pedersen, S., Kjaerulff, S., Outtrup, H. and Borchert, T. V. (1999) Development of industrially important α-amylases. J. Appl. Glycosci. 46, 199-206
34. Feller, G., Payan, F., Theys, F., Qian, M., Haser, R. and Gerday, C. (1994) Stability and structural analysis of α-amylase from the antarctic psychrophile Alteromonas haloplanctis A23. Eur. J. Biochem, 222, 441-447
35. Aghajari, N., Feller, G., Gerday, C. and Haser, R. (1998) Structures of the psychrophilic Alteromonas haloplanctis α-amylase give sights into cold adaptation at a molecular level. Structure 6, 1503-1516
36. D'Amico, S., Gerday, C. and Feller, G. (2002) Structural determinants of cold adaptation and stability in a psychrophilic α-amylase. Biologia (Bratislava) 57 (Suppl. 11), 211-219