Improvement of thermal stability of a mutagenised α-amylase by manipulation of the calcium-binding site

Enzyme and Microbial Technology

Volumn 53, Issue 6-7, 2013, Pages 406-413

  Ghollasi, Marzieh ^a   Ghanbari Safari, Maryam ^b   Khajeh, Khosro ^b  

^a KHARAZMI UNIVERSITY   (Iran)

^b TARBIAT MODARES UNIVERSITY   (Iran)

Author keywords

Amylase; Bacillus megaterium; Calcium; Mutagenesis; Thermostability

Indexed keywords

BACILLUS MEGATERIUM; CALCIUM BINDING; CALCIUM IONS; HALF LIVES; HYDROLYTIC ACTIVITIES; OPTIMUM TEMPERATURE; SITE DIRECTED MUTAGENESIS; THERMOSTABILITY;

BACTERIOLOGY; CALCIUM; MUTAGENESIS; STABILITY;

AMYLASES;

AMYLASE; CALCIUM; CALCIUM ION; HYDROLASE; STARCH;

AMINO ACID SUBSTITUTION; ARTICLE; CALCIUM BINDING; CIRCULAR DICHROISM; DNA ISOLATION; ENZYME INACTIVATION; ENZYME STABILITY; FLUORESCENCE SPECTROSCOPY; NUCLEOTIDE SEQUENCE; PHYLOGENETIC TREE; PROTEIN STRUCTURE; SITE DIRECTED MUTAGENESIS; THERMOSTABILITY; WILD TYPE;

BACILLUS MEGATERIUM; HALOTHERMOTHRIX ORENII;

BACILLUS MEGATERIUM; CALCIUM; MUTAGENESIS; THERMOSTABILITY; Α-AMYLASE;

ALPHA-AMYLASES; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; BACILLUS MEGATERIUM; BACTERIAL PROTEINS; BINDING SITES; CALCIUM; ENZYME STABILITY; HALF-LIFE; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; MUTANT PROTEINS; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; TEMPERATURE;

EID: 84886446409     PISSN: 01410229     EISSN: 18790909     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2013.09.001     Document Type: Article

References (47)

1. MacGregor E.A., Janecek S., Svensson B. Relationship of sequence and structure to specificity in the α-amylase family of enzymes. Biochimica et Biophysca Acta 2001, 1546:1-20.
2. Nakajima R., Imanaka T., Aiba S. Comparison of amino acid sequences of eleven different α-amylases. Applied Microbiology and Biotechnology 1986, 23:355-360.
3. Kuriki T., Imanaka T. The concept of the α-amylase family: structural similarity and common catalytic mechanism. Journal of Bioscience and Bioengineering 1999, 87:557-565.
4. 8-barrel glycosyl hydrolases suggested by similarity of their fifth conserved sequence region. FEBS Letters 1995, 377:6-8.
5. Janeček S. Amylolytic enzymes-focus on the alpha-amylases from archaea and plants. Nova Biotechnologica 2009, 9:5-25.
6. Janeček S. How many conserved sequence regions are there in the amylase family?. Biologia, Bratislava 2002, 57(Suppl. 11):29-41.
7. Oslancova A., Janecek S. Oligo-1,6-glucosidase and neopullulanase enzyme subfamilies from the a-amylase family defined by the fifth conserved sequence region. Cellular and Molecular Life Sciences 2002, 59:1945-1959.
8. Janecek S. α-Amylase family: molecular biology and evolution. Progress in Biophysics and Molecular Biology 1997, 67:67-97.
9. David M.H., Gunther H., Roper H. Catalytic properties of Bacillus megaterium amylase. Starch 1987, 39:436-440.
10. Park K.H., Kim T.J., Cheong T.K., Kim J.W., Oh B.H., Svensson B. Structure, specificity and function of cyclomaltodextrinase, a multispecific enzyme of the α-amylase family. Biochimica Biophysica Acta 2000, 1478:165-185.
11. Yazdani M., Naderi-Manesh H., Khajeh K., Soudi M.R., Asghari S.M., Sharifzadeh M. Isolation and characterization of a novel gamma-radiation-resistant bacterium from hot spring in Iran. Journal of Basic Microbiology 2009, 49:119-127.
12. Declerck N., Machius M., Joyet P., Wiegand G., Huber R., Gaillardin C. Hyperthermostabilization of Bacillus licheniformis α-amylase and modulation of its stability over a 50°C temperature range. Protein Engineering 2003, 16:287-293.
13. Tan T.C., Mijts B.N., Swaminathan K., Patel B.K.C., Divne C. Crystal structure of the polyextremophilic alpha-amylase AmyB from Halothermothrix orenii: details of a productive enzyme-substrate complex and an N domain with a role in binding raw starch. Journal of Molecular Biology 2008, 378:850-868.
14. Tan T.C., Yien Y.Y., Patel B.K.C., Mijts B.N., Swaminathan K. Crystallization of a novel α-amylase, AmyB, from the thermophilic halophile Halothermothrix orenii. ACTA Crystallographica 2003, D59:2257-2258.
15. Sivakumar N., Li N., Tang J.W., Patel B.K.C., Swaminathan K. Crystal structure of AmyA lacks acidic surface and provide insights into protein stability at poly-extreme condition. FEBS Letters 2006, 580:2646-2652.
16. Liu Y., Shen W., Shi G.Y., Wang Z.X. Role of the calcium-binding residues Asp231, Asp233, and Asp438 in Alpha-Amylase of Bacillus amyloliquefaciens as revealed by mutational analysis. Current Microbiology 2010, 60:162-166.
17. Lee S., Mouri Y., Minoda M., Oneda H., Inouye K. Comparison of the wild-type alpha-amylase and its variant enzymes in Bacillus amyloliquefaciens in activity and thermal stability, and insights into engineering the thermal stability of Bacillus alpha-amylase. Journal of Biochemistry 2006, 139:1007-1015.
18. Majzlova K., Pukajova Z., Janecek S. Tracing the evolution of the α-amylase subfamily GH13_36 covering the amylolytic enzymes intermediate between oligo-1,6-glucosidases and neopullulanases. Carbohydrate Research 2013, 367:48-57.
19. Lumry R., Eyring H. Conformational changes of proteins. Journal of Physical Chemistry 1954, 58:110-120.
20. Sambrook J., Russell D.W. Molecular cloning: a laboratory manual 2001, Cold Spring Harbor, New York. 3rd ed.
21. Owen R.J., Borman P. A rapid biochemical method for purifying high molecular weight bacterial chromosomal DNA for restriction enzyme analysis. Nucleic Acids Research 1987, 15:3631-3632.
22. Ghollasi M., Khajeh K., Naderi-Manesh H., Ghasemi A. Engineering of a bacillus α-amylase with improved thermostability and calcium independency. Applied Biochemistry and Biotechnology 2010, 162:444-459.
23. Fisher C.L., Pei G.K. Modification of a PCR-based site-directed mutagenesis method. BioTechniques 1997, 23:570-574.
24. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry 1976, 72:248-254.
25. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
26. Miller G.L. Use of dinitrosalicylic acid reagent for determination of reducing sugar. Analytical Chemistry 1959, 31:426-428.
27. Ahmadi A. Purification of α-amylase from Bacillus sp. GHA1 and its partial characterization. Journal of the Iranian Chemical Society 2010, 7:432-440.
28. Arrhenius S. Über die Reaktionsgeschwindigkeit bei der Inversion von Rohrzucker durch Säuren. Zeitschrift Fur Physikalische Chemie 1889, 4:226-248.
29. Mijts B.N., Patel B.K.C. Cloning, sequencing and expression of an α-amylase gene, amyA, from the thermophilic halophile Halothermothrix orenii and purification and characterization of the recombinant enzyme. Microbiology 2002, 148:2343-2349.
30. Bloemendal M., Johnson W.C. Structural information on proteins from CD spectroscopy: possibilities and limitations. Physical methods to characterize pharmaceutical proteins. 1995, 65-100. Plenum Press, New York. J.N. Herron, W. Jiskoot, D.J.A. Crommelin (Eds.).
31. Lin L.L., Huang C.C., Lo H.F. Impact of Arg210-Ser211 deletion on thermostability of a truncated Bacillus sp. strain TS-23 α-amylase. Process Biochemistry 2008, 43:559-565.
32. Danson M.J., Hough D.W., Russell R.J., Taylor G.L., Pearl L. Enzyme thermostability and thermoactivity. Protein Engineering 1996, 9:629-630.
33. Laidler K.J. Influence of ionic strength. Chemical Kinetics 1987, 197-201. Harper Collins Publisher, New York. 3rd ed.
34. Takase K. Effect of mutation of an amino acid residue near the catalytic site on the activity of Bacillus stearothermophilus α-amylase. European Journal of Biochemistry 1993, 211:899-902.
35. Collins T., Meuwis M.A., Gerday C., Feller G. Activity, stability and flexibility in glycosidase adapted to extreme thermal environments. Journal of Molecular Biology 2003, 328:419-428.
36. Dunitz J.D. The entropic cost of bound water in crystals and biomolecules. Science 1994, 264:670.
37. Tanaka A., Hoshino E. Secondary calcium-binding parameter of bacillus amyloliquefaciens α-amylase obtained from inhibition kinetics. Journal of Bioscience and Bioengineering 2003, 96:262-267.
38. Tanaka A., Hoshino E. Calcium-binding parameter of Bacillus amyloliquefaciens alpha-amylase determined by inactivation kinetics. Biochemistry Journal 2002, 364:635-639.
39. Feller G., D'Amico D., Gerday C. Thermodynamic stability of a cold-active α-amylase from the antarctic bacterium alteromonas haloplanctis. Biochemistry Journal 1999, 38:4613-4619.
40. Vieille C., Zeikus J.G. Thermozymes: identifying molecular determinants of protein structural and functional stability. Trends in Biotechnology 1996, 14:183-190.
41. 2+ binding by α-lactalbumin. Journal of Biological Chemistry 1986, 261:8824-8829.
42. Igarashi K., Hatada Y., Ikawa K., Araki H., Ozawa T., Kobayashi T., Ozaki K., Ito S. Improved thermostability of a Bacillus α-amylase by deletion of an arginine-glycine residue is caused by enhanced calcium binding. Biochemical and Biophysical Research Communications 1998, 248:372-377.
43. Ohnishi H., Sakai H., Nosoh Y., Sekiguchi T. Protein engineering for thermostability. Trends in Biotechnology 1996, 19:16-20.
44. Jaenicke R., Schurig H., Beaucamp N., Ostendorp R. Structure and stability of hyperstable proteins: glycolytic enzymes from hyperthermophilic bacterium Thermotoga maritime. Advances in Protein Chemistry 1996, 48:181-269.
45. Sadeghi L., Khajeh K., Mollania N., Dabirmanesh B., Ranjbar B. Extra EF Hand Unit (DX) mediated stabilization and calcium independency of α-amylase. Molecular Biotechnology 2013, 53:270-277.
46. Watanabe K., Masuda T., Ohashi H., Mihara H., Suzuki Y. Multiple proline substitutions cumulately thermostabilize Bacillus cerues ATCC7064 oligo-1,6-glucosidae: Irrefragable proof supporting the proline rule. European Journal of Biochemistry 1994, 226:277-283.
47. Burmeister W.P., Ruigrok R.W., Cusack S. The 2.2Å resolution crystal structure of influenza B neuraminidase and its complex with sialic acid. EMBO Journal 1992, 11:49-56.