Engineering a de novo internal disulfide bridge to improve the thermal stability of xylanase from Bacillus stearothermophilus No. 236

Journal of Biotechnology

Volumn 127, Issue 2, 2007, Pages 300-309

  Jeong, Mi Young ^a,b   Kim, Sanguk ^c   Yun, Cheol Won ^a   Choi, Yong Jin ^a   Cho, Ssang Goo ^b  

^a Korea University   (South Korea)

^b Konkuk University   (South Korea)

^c Pohang University of Science and Technology (POSTECH)   (South Korea)

Author keywords

Bacillus stearothermophilus No. 236; Disulfide bridge; Endo l,4 xylanase; Thermostability

Indexed keywords

AMINO ACIDS; CARBOHYDRATES; CHEMICAL BONDS; ENZYME KINETICS; HYDROLYSIS; MUTAGENESIS; THERMODYNAMIC STABILITY;

BACILLUS STEARTHERMOPHILUS; CYSTEINE; DISULFIDE BRIDGE; MOLECULAR MODELS; THERMOPHILIC XYLANASES; XYLAN;

BACTERIA;

AMINO ACID; ASPARAGINE; BACTERIAL ENZYME; CYSTEINE; DISULFIDE; SERINE; XYLAN; XYLAN ENDO 1,3 BETA XYLOSIDASE;

ARTICLE; BIOTECHNOLOGY; CHEMICAL ENGINEERING; ENZYME ENGINEERING; ENZYME STABILITY; GENETIC CONSERVATION; GEOBACILLUS STEAROTHERMOPHILUS; GEOMETRY; HYDROLYSIS; MOLECULAR MODEL; NONHUMAN; PRIORITY JOURNAL; PROCESS DESIGN; THERMOSTABILITY;

AMINO ACID SEQUENCE; BACILLUS STEAROTHERMOPHILUS; DISULFIDES; ENDO-1,4-BETA XYLANASES; ENZYME STABILITY; HEAT; HYDROLYSIS; KINETICS; MOLECULAR SEQUENCE DATA; MUTANT PROTEINS; PROTEIN DENATURATION; PROTEIN ENGINEERING; PROTEIN STRUCTURE, SECONDARY; SULFHYDRYL COMPOUNDS; THERMODYNAMICS; TITRIMETRY; XYLANS;

GEOBACILLUS STEAROTHERMOPHILUS;

EID: 33846219593     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2006.07.005     Document Type: Article

References (29)

1. Beg Q.K., Kapoor M., Mahajan L., and Hoondal G.S. Microbial xylanases and their industrial applications: a review. Appl. Microbiol. Biotechnol. 56 (2001) 326-338
2. Betz S.F. Disulfide bonds and the stability of globular proteins. Protein Sci. 2 (1993) 1551-1558
3. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
4. Cho S.G., and Choi Y.J. Nucleotide sequence analysis of an endo-xylanase gene (xynA) from Bacillus stearothermophilus. J. Microbiol. Biotechnol. 5 (1995) 117-124
5. Cho S.G., and Choi Y.J. Overproduction, purification and characterization of Bacillus stearothermophilus endo-xylanase (XynA). J. Microbiol. Biotechnol. 6 (1996) 79-85
6. Dombkowski A.A. Disulfide by design: a computational method for the rational design of disulfide bonds in proteins. Bioinformatics 19 (2003) 1852-1853
7. Fenel F., Leisola M., Janis J., and Turunen O. A de novo designed N-terminal disulphide bridge stabilizes the Trichoderma reesei endo-1,4-beta-xylanase II. J. Biotechnol. 108 (2004) 137-143
8. Flory P.J. Theory of elastic mechanisms in fibrous proteins. J. Am. Chem. Soc. 78 (1956) 5222-5235
9. Gruber K., Klintschar G., Hayn M., Schlacher A., Steiner W., and Kratky C. Thermophilic xylanase from Thermomyces lanuginosus: high-resolution X-ray structure and modeling studies. Biochemistry 37 (1998) 13475-13485
10. Ha G.S., Choi I.D., and Choi Y.J. Carbon catabolite repression (CCR) of expression of the xylanaseA gene of Bacillus stearothermophilus No. 236. J. Microbiol. Biotechnol. 11 (2001) 131-137
11. Habeeb A.F.S.A. Reaction of protein sulfhydryl groups with Ellman's reagent. In: Hirs C.H.W., and Timasheff S.N. (Eds). Methods in Enzymology vol. 25 (1972), Academic Press, New York 457-464
12. Hakulinen N., Turunen O., Janis J., Leisola M., and Rouvinen J. Three-dimensional structures of thermophilic beta-1,4-xylanases from Chaetomium thermophilum and Nonomuraea flexuosa. Comparison of twelve xylanases in relation to their thermal stability. Eur. J. Biochem. 270 (2003) 1399-1412
13. Hinck A.P., Truckses D.M., and Markley J.L. Engineered disulfide bonds in staphylococcal nuclease: effects on the stability and conformation of the folded protein. Biochemistry 35 (1996) 10328-10338
14. 8-barrel protein by an engineered disulfide bridge. Eur. J. Biochem. 269 (2002) 1145-1153
15. Kulkarni N., Shendye A., and Rao M. Molecular and biotechnological aspects of xylanases. FEMS Microbiol. Rev. 23 (1999) 411-456
16. Kumar P.R., Eswaramoorthy S., Vithayathil P.J., and Viswamitra M.A. The tertiary structure at 1.59 A resolution and the proposed amino acid sequence of a family-11 xylanase from the thermophilic fungus Paecilomyces varioti bainier. J. Mol. Biol. 295 (2000) 581-593
17. Mansfeld J., Vriend G., Dijkstra B.W., Veltman O.R., Van den Burg B., Venema G., Ulbrich-Hofmann R., and Eijsink V.G. Extreme stabilization of a thermolysin-like protease by an engineered disulfide bond. J. Biol. Chem. 272 (1997) 11152-11156
18. Miller G.L. Use of dinitrosalicylic acid reagent for determination of reducing sugar. Anal. Chem. 31 (1959) 426-428
19. Pace C.N., Grimsley G.R., Thomson J.A., and Barnett B.J. Conformational stability and activity of ribonuclease T1 with zero, one, and two intact disulfide bonds. J. Biol. Chem. 263 (1988) 11820-11825
20. Poland D.C., and Scheraga H.A. Statistical mechanics of non-covalent bonds in polyamino acids. VIII. Covalents loops in proteins. Biopolymers 3 (1965) 379-399
21. Pollitt S., and Zalkin H. Role of primary structure and disulfide bond formation in beta-lactamase secretion. J. Bacteriol. 153 (1983) 27-32
22. Pons J., Planas A., and Querol E. Contribution of a disulfide bridge to the stability of 1,3-1,4-beta-d-glucan 4-glucanohydrolase from Bacillus licheniformis. Protein Eng. 8 (1995) 939-945
23. Prade R.A. Xylanases: from biology to biotechnology. Biotechnol. Genet. Eng. Rev. 13 (1996) 101-131
24. Schellman J.A. The thermodynamics of urea solutions and the heat of formation of the peptide hydrogen bond. C.R. Trav. Lab. Carlsberg [Chim] 29 (1955) 223-229
25. Song H.S., and Choi Y.J. Production of xylanase by Bacillus stearothermophilus. Kor. J. Appl. Microbiol. Bioeng. 17 (1989) 289-294
26. Turunen O., Etuaho K., Fenel F., Vehmaanpera J., Wu X., Rouvinen J., and Leisola M. A combination of weakly stabilizing mutations with a disulfide bridge in the alpha-helix region of Trichoderma reesei endo-1,4-beta-xylanase II increases the thermal stability through synergism. J. Biotechnol. 88 (2001) 37-46
27. Wakarchuk W.W., Campbell R.L., Sung W.L., Davoodi J., and Yaguchi M. Mutational and crystallographic analyses of the active site residues of the Bacillus circulans xylanase. Protein Sci. 3 (1994) 467-475
28. Wakarchuk W.W., Sung W.L., Campbell R.L., Cunningham A., Watson D.C., and Yaguchi M. Thermostabilization of the Bacillus circulans xylanase by the introduction of disulfide bonds. Protein Eng. 7 (1994) 1379-1386
29. Wong K.K., Tan L.U., and Saddler J.N. Multiplicity of beta-1,4-xylanase in microorganisms: functions and applications. Microbiol. Rev. 52 (1988) 305-317