Thermostability improvement of maltogenic amylase MAUS149 by error prone PCR

Journal of Biotechnology

Volumn 168, Issue 4, 2013, Pages 601-606

  Ben Mabrouk, Sameh ^a   Zouari Ayadi, Dorra ^a   Ben Hlima, Hajer ^a   Bejar, Samir ^a  

^a UNIVERSITY OF SFAX   (Tunisia)

Author keywords

Error prone PCR; Maltogenic amylase; Site directed mutagenesis; Thermostability

Indexed keywords

ERROR PRONE PCR; MALTOGENIC AMYLASE; MUTANT ENZYMES; RANDOM MUTAGENESIS; SALT BRIDGES; SINGLE MUTATION; SITE DIRECTED MUTAGENESIS; THERMOSTABILITY;

AMYLASES; BACTERIOLOGY; HYDROGEN BONDS;

STABILITY;

AMYLASE; BACTERIAL ENZYME; MAUS149 PROTEIN; MUTANT PROTEIN; UNCLASSIFIED DRUG;

ANALYTICAL ERROR; ARTICLE; CONTROLLED STUDY; DNA SHUFFLING; ESCHERICHIA COLI; HALF LIFE TIME; HYDROGEN BOND; MOLECULAR MODEL; MUTAGENESIS; MUTANT; NONHUMAN; PHYSICAL CHEMISTRY; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; PROTEIN STRUCTURE; SITE DIRECTED MUTAGENESIS; TEMPERATURE ACCLIMATIZATION; THERMOSTABILITY; WILD TYPE;

BACILLUS SP.;

CD; CYCLODEXTRIN; ERROR PRONE PCR; MA-A27; MALTOGENIC AMYLASE; MALTOGENIC AMYLASE US149; MAU149; MUTATED MALTOGENIC AMYLASE OF CLONE A27; SITE-DIRECTED MUTAGENESIS; THERMOSTABILITY;

AMINO ACID SEQUENCE; BACILLUS; ENZYME STABILITY; GLYCOSIDE HYDROLASES; HOT TEMPERATURE; MUTAGENESIS, SITE-DIRECTED; MUTATION; POLYMERASE CHAIN REACTION;

EID: 84888833713     PISSN: 01681656     EISSN: 18734863     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2013.08.026     Document Type: Article

References (30)

1. Abe A., Tonozuka T., Sakano Y., Kamitori S. Complex structures of Thermoactinomyces vulgaris R-47 a-amylase 1 with malto-oligosaccharides demonstrate the role of domain N acting as a starch-binding domain. J. Mol. Biol. 2004, 335:811-822.
2. Altschul S.F., Madden T.L., Schaffer A.A., Zhang J., Zhang Z., Miller W., Lipman D.J. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res. 1997, 25:3389-3402.
3. Baek J.S., Kim H.Y., Yoo S.S., Cheong T.K., Kim M.J., Lee S.B., Abbott T.P., Song H.J., Rhyu M.R., Oh B.H., Park K.H. Synthesis of acarbose transfer products by Bacillus stearothermophilus maltogenic amylase with simmondsin. Ind. Crop. Prod. 2000, 12:173-182.
4. Ben Mabrouk S., Ben Messaoud E., Zouari A.D., Jemli S., Roy A., Mezghani M., Bejar S. Cloning and sequencing of an original gene encoding a maltogenic amylase from Bacillus sp. US149 strain and characterization of the recombinant activity. Mol. Biotechnol. 2008, 38:211-219.
5. Ben Messaoud E., Ben Mabrouk S., Jemli S., Bejar S. Cloning and sequencing of the amylase gene from Bacillus subtilis US116 strain encoding an enzyme closely identical to that from Bacillus amyloliquefaciens but distinct in thermal stability. J. Food Biochem. 2010, 10.1111/j.1745-4514.2009.00277.X.
6. Cantarel B.L., Coutinho P.M., Rancurel C., Bernard T., Lombard V., Henrissat B. The carbohydrate-active enzymes database (CAZy): an expert resource for glycogenomics. Nucleic Acids Res. 2009, 37:D233-D238.
7. Grinberg A.V., Bernhardt R. Contribution of a salt bridge to the thermostability of adrenodoxin determined by site-directed mutagenesis. Arch. Biochem. Biophys. 2001, 396:25-34.
8. Gujral H.S., Haros M., Rossell C.M. Starch hydrolyzing enzymes for retarding the staling of rice bread. Cereal Chem. 2003, 80:750-754.
9. Haki G.D., Rakshit S.K. Developments in industrially important thermostable enzymes: a review. Bioresource Technol. 2003, 89:17-34.
10. Hondoh H., Kuriki T., Matsuura Y. Three-dimensional structure and substrate binding of Bacillus stearothermophilus neopullulanase. J. Mol. Biol. 2003, 326:177-188.
11. Hurley J.H., Baase W.A., Matthews B.W. Design and structural of alternative hydrophobic core packing arrangements in bacteriophage T4 lysozyme. J. Mol. Biol. 1992, 224:1143-1159.
12. Jones A., Lamsa M., Frandsen T.P., Spendler T., Harris P., Sloma A., Xu F., Nielsen J.B., Cherry J.R. Directed evolution of a maltogenic alpha-amylase from Bacillus sp. TS-25. J. Biotechnol. 2008, 134:325-333.
13. Khemakhem B., Ben Ali M., Aghajari N., Juy M., Haser R., Bejar S. The importance of an extra loop in the B-domain of an α-amylase from B. stearothermophilus US100. Biochem. Biophys. Res. Commun. 2009, 385:78-83.
14. Kim J.S., Cha S.S., Kim H.J., Kim T.J., Ha N.C., Oh S.T., Cho H.S., Cho M.J., Kim M.J., Lee H.S., Kim J.W., Choi K.Y., Park K.Y., Oh B.H. Crystal structure of a maltogenic amylase provides insights into a catalytic versatility. J. Biol. Chem. 1999, 274:26279-26286.
15. Kim J.W., Kim Y.H., Lee H.S., Yang S.J., Kim Y.W., Lee M.H., Kim J.W., Seo N.S., Park C.S., Park K.H. Molecular cloning and biochemical characterization of the first archaeal maltogenic amylase from the hyperthermophilic archaeon Thermoplasma volcanium GSS1. Biochim. Biophys. Acta 2007, 1774:661-669.
16. Kim Y.W., Choi J.H., Kim J.W., Park C., Kim J.W., Cha H., Lee S.B., Oh B.H., Moon T.W., Park K.H. Directed evolution of thermus maltogenic amylase toward enhanced thermal resistance. Appl. Environ. Microbiol. 2003, 69:4866-4874.
17. Lee H.S., Kim M.S., Cho H.S., Kim J.I., Kim T.J., Choi J.H., Park C., Lee H.S., Oh B.H., Park K.H. Cyclomaltodextrinase, neopullulanase, and maltogenic amylase are nearly indistinguishable from each other. J. Biol. Chem. 2002, 277:21891-21897.
18. Lim W.A., Farruggio D.C., Sauer R.T. Structural and energetic consequences of disruptive mutations in a protein core. Biochemistry 1992, 31:4324-4333.
19. Lim W.A., Hodel A., Sauer R.T., Richards F.M. The crystal structure of a mutant protein with altered but improved hydrophobic core packing. Proc. Natl. Acad. Sci. U.S.A. 1994, 91:423-427.
20. Liu R., Baase W.A., Matthews B.W. The introduction of strain and its effects on the structure and stability of T4 lysozyme. J. Mol. Biol. 2000, 295:127-145.
21. Malabendu J., Chiranjit M., Saptadip S., Bikas R.P., Syed S.I., Pradeep K.D.M., Keshab C.M. Salt-independent thermophilic α-amylase from Bacillus megaterium VUMB109: an efficacy testing for preparation of maltooligosaccharides. Ind. Crop. Prod. 2013, 41:386-391.
22. Miller G.L. Use of dinitrosalycilic acid reagent for determination of reducing sugars. Anal. Chem. 1959, 31:426-428.
23. Shim J.H., Kim Y.W., Kim T.J., Chae H.Y., Park J.H., Cha H.J., Kim J.W., Kim Y.R., Schaefer T., Spendler T., Moon T.W., Park K.H. Improvement of cyclodextrin glucanotransferase as an antistaling enzyme by error-prone PCR. Protein Eng. Des. Sel. 2004, 17:205-211.
24. Song J.K., Rhee J.S. Simultaneous enhancement of thermostability and catalytic activity of phospholipase A1 by evolutionary molecular engineering. Appl. Environ. Microbiol. 2000, 66:890-894.
25. Thompson J.D., Higgins D.G., Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position specific gap penalties and weight matrix choice. Nucleic Acids Res. 1994, 22:4673-4680.
26. Trevizano L.M., Ventorim R.Z., De Rezende S.T., Junior F.P.S., Guimarães V.M. Thermostability improvement of Orpinomyces sp. xylanase by directed evolution. J. Mol. Catal. B: Enzym. 2012, 81:12-18.
27. Van der Maarel M.J.E.C., Van der Veen B., Uitdehaag J.C.M., Leemhuis H., Dijkhuizen L. Properties and applications of starch-converting enzymesof the α-amylase family. J. Biotechnol. 2002, 94:137-155.
28. Vogt G., Woell S., Argos P. Protein thermal stability, hydrogen bonds, and ion pairs. J. Mol. Biol. 1997, 269:631-643.
29. Yanase M., Takata H., Fujii K., Takaha T., Kuriki T. Cumulative effect of amino acid replacements results in enhanced thermostability of potato type l α-glucan phosphorylase. Appl. Environ. Microbiol. 2005, 71:5433-5439.
30. Yoon J.W., Jeon E.J., Jung I.H., Min M.J., Lee H.Y., Kim M.J., Baek J.S., Lee H.S., Park C.S., Oh S., Park K.H., Moon T.W. Maltosyl-erythritol, a major transglycosylation product of erythritol by Bacillus stearothermophilus maltogenic amylase. Biosci. Biotechnol. Biochem. 2003, 67:525-531.