Site-directed mutagenesis of methionine residues for improving the oxidative stability of α-amylase from Thermotoga maritima

Journal of Bioscience and Bioengineering

Volumn 116, Issue 4, 2013, Pages 449-451

  Ozturk, Handan ^a   Ece, Selin ^a   Gundeger, Ersin ^a   Evran, Serap ^a  

^a EGE UNIVERSITY   (Turkey)

Author keywords

Amylase; Oxidative stability; Protein engineering; Site directed mutagenesis of methionine; Thermotoga maritima

Indexed keywords

ALANINE RESIDUES; METHIONINE RESIDUES; OXIDATIVE STABILITY; PROTEIN ENGINEERING; RESIDUAL ACTIVITY; SITE DIRECTED MUTAGENESIS; THERMOTOGA MARITIMA; WILD-TYPE ENZYMES;

AMYLASES; OXIDATION RESISTANCE;

AMINO ACIDS;

ALANINE; AMYLASE; METHIONINE;

ARTICLE; ENZYME ACTIVITY; ENZYME INACTIVATION; ENZYME STABILITY; GENE MUTATION; MUTANT; NONHUMAN; OXIDATION; SITE DIRECTED MUTAGENESIS; THERMOSTABILITY; THERMOTOGA MARITIMA; WILD TYPE;

THERMOTOGA MARITIMA;

OXIDATIVE STABILITY; PROTEIN ENGINEERING; SITE-DIRECTED MUTAGENESIS OF METHIONINE; THERMOTOGA MARITIMA; Α-AMYLASE;

ALANINE; ALPHA-AMYLASES; ENZYME STABILITY; HYDROGEN PEROXIDE; METHIONINE; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; OXIDATION-REDUCTION; THERMOTOGA MARITIMA;

EID: 84883286810     PISSN: 13891723     EISSN: 13474421     Source Type: Journal    
DOI: 10.1016/j.jbiosc.2013.04.018     Document Type: Article

References (14)

1. Prakash O., Jaiswal N. Alpha-amylase: an ideal representative of thermostable enzymes. Appl. Biochem. Biotechnol. 2010, 160:2401-2414.
2. Fujinami S., Fujisawa M. Industrial applications of alkaliphiles and their enzymes-past, present and future. Environ. Technol. 2010, 31:845-856.
3. Kim Y.H., Berry A.H., Spencer D.S., Stites W.E. Comparing the effect on protein stability of methionine oxidation versus mutagenesis: steps toward engineering oxidative resistance in proteins. Protein Eng. 2001, 14:343-347.
4. Ballschmiter M., Futterer O., Liebl W. Identification and characterization of a novel intracellular alkaline alpha-amylase from the hyperthermophilic bacterium Thermotoga maritima MSB8. Appl. Environ. Microbiol. 2006, 72:2206-2211.
5. Dickmanns A., Ballschmiter M., Liebl W., Ficner R. Structure of the novel alpha-amylase AmyC from Thermotoga maritima. Acta Crystallogr. D Biol. Crystallogr. 2006, 62:262-270.
6. Sarkar G., Sommer S.S. The "megaprimer" method of site-directed mutagenesis. Biotechniques 1990, 8:404-407.
7. Bradford M.M. Arapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72:248-254.
8. Miller G.L. Use of dinitrosalicylic acid reagent for determination of reducing sugar. Anal. Chem. 1959, 31:426-428.
9. Yang H., Liu L., Li J., Du G., Chen J. Structure-based replacement of methionine residues at the catalytic domains with serine significantly improves the oxidative stability of alkaline amylase from alkaliphilic Alkalimonas amylolytica. Biotechnol. Prog. 2012, 28:1271-1277.
10. Roger Chien H.C., Hsu C.L., Hu H.Y., Wang W.C., Hsu W.H. Enhancing oxidative resistance of Agrobacterium radiobacter N-carbamoyl d-amino acid amidohydrolase by engineering solvent-accessible methionine residues. Biochem. Biophys. Res. Commun. 2002, 297:282-287.
11. Lin L.L., Lo H.F., Chiang W.Y., Hu H.Y., Hsu W.H., Chang C.T. Replacement of methionine 208 in a truncated Bacillus sp. TS-23 alpha-amylase with oxidation-resistant leucine enhances its resistance to hydrogen peroxide. Curr. Microbiol. 2003, 46:211-216.
12. Khemakhem B., Ali M.B., Aghajari N., Juy M., Haser R., Bejar S. Engineering of the alpha-amylase from Geobacillus stearothermophilus US100 for detergent incorporation. Biotechnol. Bioeng. 2009, 102:380-389.
13. Kuo L.Y., Hwang G.Y., Yang S.L., Hua Y.W., Chen W., Lin L.L. Inactivation of Bacillus stearothermophilus leucine aminopeptidase II by hydrogen peroxide and site-directed mutagenesis of methionine residues on the enzyme. Protein J. 2004, 23:295-302.
14. Guex N., Peitsch M.C. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 1997, 18:2714-2723.