Kinetic study of the thermal denaturation of a hyperthermostable extracellular α-amylase from Pyrococcus furiosus

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1834, Issue 12, 2013, Pages 2600-2605

  Brown, I ^a   Dafforn, T R ^a   Fryer, P J ^a   Cox, P W ^a  

^a UNIVERSITY OF BIRMINGHAM   (United Kingdom)

Author keywords

Amylase; Denaturation; Pyrococcus furiosus; Sterilisation; TTI

Indexed keywords

AMYLASE;

ARTICLE; CIRCULAR DICHROISM; DENATURATION; DIFFERENTIAL SCANNING CALORIMETRY; ENZYME KINETICS; INFRARED SPECTROSCOPY; NONHUMAN; PRIORITY JOURNAL; PYROCOCCUS FURIOSUS; TEMPERATURE; THERMOSTABILITY;

PYROCOCCUS FURIOSUS;

EID: 84884964623     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2013.09.008     Document Type: Article

References (28)

1. S. Cavagnero, D. Debe, Z. Zhou, M. Adams, and S. Chan Kinetic role of electrostatic interactions in the unfolding of hyperthermophilic and mesophilic rubredoxins Biochemistry 37 1998 3369 3376 (Pubitemid 28125564)
2. D. Perl, C. Welker, T. Schindler, K. Schroder, M. Marahiel, and R. Jaenicke Conversion of rapid two-state folding in mesophilic, thermophilic and hyperthermophilic cold shock proteins Nat. Struct. Biol. 5 1998 229 235 (Pubitemid 28113755)
3. J. Kaushik, K. Ogasahara, and K. Yutani The unusually slow relaxation kinetics of the folding-unfolding of pyrrolidone carboxyl peptidase from a hyperthermophile, Pyrococcus furiosus J. Mol. Biol. 316 2002 991 1003 (Pubitemid 34722136)
4. R. Jaenicke Protein stability and molecular adaptation to extreme conditions Eur. J. Biochem. 202 1991 715 728
5. R. Jaenicke Stability and stabilisation of globular proteins in solution J. Biotechnol. 79 2000 193 203 (Pubitemid 30365192)
6. R. Daniel The upper limits of enzyme thermal stability Enzyme Microb. Technol. 19 1996 74 79 (Pubitemid 26202574)
7. R. Jaenicke What ultrastable globular proteins teach us about protein stabilization Biochem. Mosc. 63 1998 312 321 (Pubitemid 128588269)
8. R. Jaenicke, and G. Bohm The stability of proteins in extreme environments Curr. Opin. Struct. Biol. 8 1998 738 748 (Pubitemid 29004672)
9. R. Koch, A. Spreinat, K. Lemke, and G. Antranikian Purification and properties of a hyperthermoactive alpha-amylase from the archaeobacterium Pyrococcus woesei Arch. Microbiol. 155 1991 572 578
10. A. Linden, O. Mayans, W. Meyer-Klaucke, G. Antranikian, and M. Wilmanns Differential regulation of a hyperthermophilic alpha-amylase with a novel (Ca, Zn) two metal centre by zinc J. Biol. Chem. 278 2003 9875 9884 (Pubitemid 36800491)
11. R. Hiller, Z. Zhou, M. Adams, and S. Englander Stability and dynamics in a hyperthermophilic protein with melting temperature close to 200 C Proc. Natl. Acad. Sci. U. S. A. 94 1997 11329 11332 (Pubitemid 27450998)
12. M. Vihinen, and P. Mantsala Microbial amylolytic enzymes Crit. Rev. Biochem. Mol. Biol. 24 1989 329 418
13. H. Guzman-Maldonado, and L. Paredes Amylolytic enzymes and products derived from starch: a review Crit. Rev. Food Sci. 1995 1995 373 403
14. K. Mehauden, P.W. Cox, S. Bakalis, M. Simmons, G. Tucker, and P.J. Fryer A novel method to evaluate the applicability of time temperature integrators to different temperature profiles Innov. Food Sci. Emerg. 8 4 2007 507 514 (Pubitemid 350087797)
15. G.S. Tucker, H.M. Brown, P.J. Fryer, P.W. Cox, I.I. Poole, and H.S. Lee A sterilisation time-temperature integrator based on amylase from the hyperthermophilic organism Pyrococcus furiosus Innov. Food Sci. Emerg. 8 2007 63 72 (Pubitemid 46217244)
16. R. Koch, P. Zablowski, A. Spreinat, and G. Antranikian Extremely thermostable amylolytic enzyme from the archaebacterium Pyrococcus furiosus FEMS Microbiol. Lett. 71 1990 21 26 (Pubitemid 20256268)
17. S.H. Brown, H.R. Costantino, and R.M. Kelly Characterization of amylolytic enzyme-activities associated with the hyperthermophilic archaebacterium Pyrococcus-furiosus Appl. Environ. Microbiol. 56 1990 1985 1991 (Pubitemid 20218567)
18. K.A. Laderman, B.R. Davis, H.C. Krutzsch, M.S. Lewis, Y.V. Griko, P.L. Privalov, and C.B. Anfinsen The purification and characterization of an extremely thermostable alpha-amylase from the hyperthermophilic archaebacterium Pyrococcus furiosus J. Biol. Chem. 268 1993 24394 24401 (Pubitemid 23335432)
19. G. Schut, S. Brehm, S. Datta, and M. Adams Whole-genome DNA microarray analysis of a hyperthermophile and archaeon: Pyrococcus furiosus grown on carbohydrates or peptides J. Bacteriol. 185 2003 3935 3947 (Pubitemid 36735945)
20. R. Lumry, and H. Eyring Conformation changes of proteins J. Phys. Chem. 58 1954 110 120
21. C. Tanford The Hydrophobic Effect 1973 Wiley New York
22. A. Klibanov Adv App Microbiol vol. 29 1983 Academic Press New York
23. I. Brown, G.S. Tucker, P.J. Fryer, and P.W. Cox Industrially Relevant Canning Trials with a Sterilisation Time-Temperature Integrator Food and Bioprocess Technology 2012 December
24. A. Nielsen, M. Pusey, C. Fuglsang, and P. Westh Proposed mechanism for the thermal denaturation of a recombinant Bacillus halmapalus alpha-amylase - the effect of calcium ions Biochim. Biophys. Acta 1652 2003 52 63 (Pubitemid 38234544)
25. L. Gianfreda, G. Marruci, N. Grizzuti, and G. Greco Acid phosphatase deactivation by a series mechanism Biotechnol. Bioeng. 26 1984 518 527 (Pubitemid 14590032)
26. S. Nury, and J. Meunier Molecular mechanisms of the irreversible thermal denaturation of guinea-pig liver transglutaminase Eur. J. Biochem. 180 1989 161 166 (Pubitemid 19080473)
27. M. Violet, and J. Meunier Kinetic study of the irreversible thermal denaturation of Bacillus licheniformis alpha-amylase J. Biochem. 263 1989 665 670 (Pubitemid 19276443)
28. S. Jorgensen, C. Vorgias, and G. Antranikian Cloning, sequencing, characterisation, and expression of an extracellular a-amylase from the hyperthermophilic archaeon Pyrococcus furiosus in Escherichia coli and Bacillus subtilis J. Biol. Chem. 272 26 1997 16335 16342 (Pubitemid 27276457)