Expression and characterisation of the catalytic domain of an archaeal family 57 pullulanase type II

Biologia - Section Cellular and Molecular Biology

Volumn 57, Issue SUPPL. 11, 2002, Pages 155-162

  Chang Pi Hin, Florent ^a   Erra Pujada, Marta ^a   Dauchez, Manuel ^b   Debeire, Philippe ^a   Duchiron, Francis ^a   O'Donohue, Michael J ^a  

^a UMR614 FARE   (France)

^b Lab Spectroscopies Struct B   (France)

Author keywords

Acarbose; F 57; Glycosyl hydrolase; Pullulanase; Thermococcales; Thermostable

Indexed keywords

ARCHAEA; THERMOCOCCALES; THERMOCOCCUS; THERMOCOCCUS HYDROTHERMALIS;

EID: 0346367471     PISSN: 13356399     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (47)

1. ALIX, A. J. 1995. Global and local secondary structures of globular proteins: linking spectroscopies and predictions, pp. 89-90. In: Merlin, J. C., Turrell, S. & Huvenne, J. P. (eds) Spectroscopy of Biomolecules, Kluwer Academic Publishers, Dordrecht.
2. ALIX, A. J. P. 1997. Molecular modeling of globular proteins: strategy ID to 3D: secondary structures and epitopes, pp. 121-151. In: VERGOTEN, G. & THEOPHANIDES, T. (eds) Biomolecular Structure and Dynamics, Kluwer Academic Publishers, Dordrecht.
3. ALIX, A. J. P. 1999. Predictive estimation of protein linear epitopes by using the program PEOPLE. Vaccine 18: 311-314.
4. ARA, K., SAEKI, K., IGARASHI, K., TAKAIWA, M., UEMURA, T., HAGIARA, H., KAWAI, S. & ITO, S. 1995. Purification and characterization of an alkaline amylopullulanase with both α(1,4) and α(1,6) hydrolytic activity from alkalophilic Bacillus sp. KSM-1378. Biochim. Biophys. Acta 1243: 315-324.
5. BENDER, H. & WALLENFELS, K. 1966. Pullulanase (an amylopectin and glycogen debranching enzyme) from Aerobacter aerogenes. Methods Enzymol. 8: 555-559.
6. BERNFELD, P. 1955. Amylases α and β. Methods Enzymol. 1: 149-150.
7. BERTOLDO, C., DUFFNER, F., JORGENSEN, P. L. & ANTRANIKIAN, G. 1999. Pullulanase type I from Fervidobacterium pennavorans Ven5: cloning, sequencing, and expression of the gene and biochemical characterization of the recombinant enzyme. Appl. Environ. Microbiol. 65: 2084-2091.
8. BUISSON, G., DUEE, E., HASER, R. & PAYAN, F. 1987. Three-dimensional structure of porcine pancreatic α-amylase at 2.9 A resolution. Role of calcium in structure and activity. EMBO J. 6: 3909-3916.
9. CHEORL-HO, K., NASHIRU, O. & KO, J. H. 1996. Purification and biochemical characterisation of pullulanase type I from Thermus caldophilus GK-4. FEMS Microbiol. Lett. 138: 147-152.
10. CHOU, P. Y. & FASMAN, G. D. 1978. Empirical predictions of protein conformation. Ann. Rev. Biochem. 47: 251-276.
11. CORNISH-BOWDEN, A. 1995. Fundamentals of Enzyme Kinetics. Portland Press, London, 343 pp.
12. CRABB, W. D. & SHETTY, J. K. 1999. Commodity scale production of sugars from starches. Curr. Opin. Microbiol. 2: 252-256.
13. DEBELLE, L., ALIX, A. J., WEI, S. M., JACOB, M. P., HUVENNE, J. P., BERJOT, M. & LEGRAND, P. 1998. The secondary structure and architecture of human elastin. Eur. J. Biochem. 258: 533-539.
14. DONG, G., VIEILLE, C. & ZEIKUS, J. G. 1997. Cloning, sequencing, and expression of the gene encoding amylopullulanase from Pyrococcus furiosus and biochemical characterization of the recombinant enzyme. Appl. Environ. Microbiol. 63: 3577-3584.
15. DUFFNER, F., BERTOLDO, C., ANDERSEN, J. T., WAGNER, K. & ANTRANIKIAN, G. 2000. A new thermoactive pullulanase from Desulfurococcus mucosus: cloning, sequencing, purification, and characterization of the recombinant enzyme after expression in Bacillus subtilis. J. Bacteriol. 182: 6331-6338.
16. ERRA-PUJADA, M., CHANG-PI-HIN, F., DEBEIRE, P., DUCHIRON, F. & O'DONOHUE, M. J. 2001. Purification and properties of the catalytic domain of the thermostable pullulanase type II from Thermococcus hydrothermalis. Biotechnol. Lett. 23: 1273-1277.
17. ERRA-PUJADA, M., DEBEIRE, P., DUCHIRON, F. & O'DONOHUE, M. J. 1999. The type II pullulanase of Thermococcus hydrothermalis: molecular characterization of the gene and expression of the catalytic domain. J. Bacteriol. 181: 3284-3287.
18. FORD, C. 1999. Improving operating performance of glucoamylase by mutagenesis. Curr. Opin. Biotechnol. 10: 353-357.
19. GANTELET, H. & DUCHIRON, F. 1998. Purification and properties of a thermoactive and thermostable pullulanase from Thermoccocus hydrothermalis, a hyperthermophilic archeon isolated from deep sea hydrothermal vent. Appl. Microbiol. Biotechnol. 49: 770-777.
20. GANTELET, H. & DUCHIRON, F. 1999. A new pullulanase from hyperthermophilic archaeon for starch hydrolysis. Biotechnol. Lett. 21: 71-75.
21. GANTELET, H., LADRAT, C., GODFROY, A., BARBIER, G. & DUCHIRON, F. 1998. Characteristics of pullulanases from extremly thermophilic archaca isolated from deep-sea hydrothermal vents. Biotechnol. Lett. 20: 819-823.
22. GIBRAT, J. F., GARNIER, J. & ROBSON, B. 1987. Furtheer developments of protein secondary structure prediction using information theory: new parameters and consideration of residue pairs. J. Mol. Biol. 198: 425-443.
23. GODFROY, A., LESONGEUR, F., RAGUENES, G., QUERELLOU, J., ANTOINE, E., MEUNIER, J. R., GUEZENNEC, J. & BARBIER, G. 1997. Thermoccocus hydrothermalis sp. nov., a new hyperthermophilic archaeon isolated from a deep sea hydrothermal vent. Int. J. Syst. Bacteriol. 47: 622-626.
24. GOKHALE, R. S., RAY, S. S., BALARAM, H. & BALARAM, P. 1999. Unfolding of Plasmodium falciparum triosephosphate isomerase in urea and guanidinium chloride: evidence for a novel disulfide exchange reaction in a covalently cross-linked mutant. Biochemistry 38: 423-431.
25. JANECEK, S. 1997. α-Amylase family: molecular biology and evolution. Prog. Biophys. Mol. Biol. 67: 67-97.
26. JANECEK, S. 1998. Sequence of archaeal Methanococcus jannaschii α-amylase contains features of families 13 and 57 of glycosyl hydrolases: a trace of their common ancestor? Folia Microbiol. (Praha) 43: 123-128.
27. JANECEK, S., SVENSSON, B. & HENRISSAT, B. 1997. Domain evolution in the α-amylase family. J. Mol. Evol. 45: 322-331.
28. KIDBY, D. K. & DAVIDSON, D. J. 1973. A convenient ferricyanide estimation of reducing sugars in the nanomole range. Anal. Biochem. 55: 321-325.
29. KIM, C. H., NASHIRU, O. & Ko, J. H. 1996. Purification and biochemical characterization of pullulanase type I from Thermus caldophilus GK-24. FEMS Microbiol. Lett. 138: 147-152.
30. KURIKI, T. & IMANAKA, T. 1999. The concept of the α-amylase family: structural similarity and common catalytic mechanism. J. Biosci. Bioeng. 87: 557-565.
31. KUSANO, S., TAKAHASHI, S., FUJIMOTO, D. & SAKANO, Y. 1990. Effects of reduced malto-oligosaccharides on the thermal stability of pullulanase from Bacillus acidopullulyticus. Carbohydr. Res. 199: 83-89.
32. LEVEQUE, E., JANECEK, S., HAYE, B. & BELARBI, A. 2000. Thermophilic archaeal amylolytic enzymes. Enz. Microb. Technol. 26: 3-14.
33. MAKHATADZE, G. I. 1999. Thermodynamics of protein interactions with urea and guanidinium hydrochloride. J. Phys. Chem. B103: 4781-4785.
34. MATHUPALA, S. & ZEIKUS, J. G. 1993. Improved purification and biochemical characterisation of extracellular amylopullulanase from Thermoanaerobacter ethanolicus 39E. Appl. Microbiol. Biotechnol. 39: 487-493.
35. MATSUURA, Y., KUSUNOKI, M., HARADA, W. & KAKUDO, M. 1984. Structure and possible catalytic residues of Taka-amylase A. J. Biochem. 95: 697-702.
36. MATSUURA, Y., KUSUNOKI, M., HARADA, W., TANAKA, N., IGA, Y., YASUOKA, N., TODA, H., NARITA, K. & KAKUDO, M. 1980. Molecular structure of Taka-amylase A. I. Backbone chain folding at 3 A resolution. J. Biochem. 87: 1555-1558.
37. MCKENZIE, H. A. 1969. pH and Buffers, pp. 476-506. In: DAWSON, R. M. C., ELLIOT, D. C., ELLIOT, W. H. & JONES, K. M. (eds) Data for Biochemical Research, Oxford University Press, Oxford.
38. RÜDIGER, A., JORGENSEN, P. L. & ANTRANIKIAN, G. 1995. Isolation and characterization of a heat-stable pullulanase from the hyperthermophilic archaeon Pyroccocus woesei after cloning and expression of its gene in Escherichia coli. Appl. Environ. Microbiol. 61: 567-575.
39. SAHA, B. C., MATHUPALA, S. P. & ZEIKUS, J. G. 1988. Purification and characterization of a highly thermostable novel pullulanase from Clostridium thermohydrosulfuricum. Biochem. J. 252: 343-348.
40. SHAW, A., BOTT, R. & DAY, A. G. 1999. Protein engineering of α-amylase for low pH performance. Curr. Opin. Biotechnol. 10: 349-352.
41. SMITH, J. S. & SCHOLTZ, J. M. 1996. Guanidine hydrochloride unfolding of peptide helices: separation of denaturant and salt effects. Biochemistry 35: 7292-7297.
42. SPREINAT, A. & ANTRANIKIAN, G. 1990. Purification and properties of a thermostable pullulanase from Clostridium thermosulfurogenes EM1 which hydrolyses both α-1,6 and α-1,4-glycosidic linkages. Appl. Microbiol. Biotechnol. 33: 511-518.
43. SUNNA, A., MORACCI, M., ROSSI, M. & ANTRANIKIAN, G. 1997. Glycosyl hydrolases from hyperthermophiles. Extremophiles 1: 2-13.
44. SUZUKI, Y., HATAGAKI, K. & ODA, H. 1991. A hyperthermostable pullulanase produced by an extreme thermophile, Bacillus flavocaldarius KP 1228, and evidence for the proline theory of increasing protein thermostability. Appl. Microbiol. Biotechnol. 34: 707-714.
45. SVENSSON, B. 1994. Protein engineering in the α-amylase family: catalytic mechanism, substrate specificity, and stability. Plant Mol. Biol. 25: 141-157.
46. SVENSSON, B. & SIERKS, M. R. 1992. Roles of the aromatic side chains in the binding of substrates, inhibitors, and cyclomalto-oligosaccharides to the glucoamylase from Aspergillus niger probed by perturbation difference spectroscopy, chemical modification, and mutagenesis. Carbohydr. Res. 227: 29-44.
47. WILCOX, E. R. & WHITAKER, J. R. 1984. Some aspects of the mechanism of complexation of red kidney bean α-amylase inhibitor and α-amylase. Biochemistry 23: 1783-1791.