Thermodynamic stability of two variants of xylanase (Xys1) from Streptomyces halstedii JM8

European Journal of Biochemistry

Volumn 253, Issue 2, 1998, Pages 462-468

  Ruz arribas, Alberto ^a   Zhadan, Galina G ^a,b   Kutyshenko, Victor P ^b,c   Santamaría, Ramon I ^a   Cortijo, Manuel ^c   Villar, Enrique ^a   Fernandez abalos, Jose M ^a   Calvete, Juan J ^d,e   Shnyrov, Valery L ^a,e  

^a UNIVERSITY OF SALAMANCA   (Spain)

^b INSTITUTE OF THEORETICAL AND EXPERIMENTAL BIOPHYSICS   (Russian Federation)

^c Instituto Pluridisciplinar   (Spain)

^d INSTITUTO DE QUÍMICA FÍSICA ROCASOLANO   (Spain)

^e UNIVERSITY OF VETERINARY MEDICINE HANNOVER   (Germany)

Author keywords

Circular dichroism; Differential scanning calorimetry; Fluorescence; Thermodynamic stability; Xylanase

Indexed keywords

XYLAN ENDO 1,3 BETA XYLOSIDASE;

ARTICLE; CIRCULAR DICHROISM; DIFFERENTIAL SCANNING CALORIMETRY; ENZYME CHEMISTRY; ENZYME STABILITY; FLUORESCENCE SPECTROSCOPY; NONHUMAN; PRIORITY JOURNAL; STREPTOMYCES; THERMODYNAMICS;

STREPTOMYCES; STREPTOMYCES HALSTEDII;

EID: 0032522782     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1998.2530462.x     Document Type: Article

References (25)

1. Gilbert, H. J. & Hazlewood, G. P. (1993) Bacterial cellulases and xylanases, J. Gen. Microbiol. 139, 187-194.
2. Henrissat, B. (1991) A classification of glycosyl hydrolases based on amino acid sequence similarities, Biochem. J. 280, 309-316.
3. Wong, K. K. Y., Tan, L. U. L. & Saddler, J. N. (1988) Multiplicity of β-1,4-xylanase in microorganisms: functions and applications. Microbiol. Rev. 52, 305-317.
4. Hazlewood, G. P. & Gilbert, H. J. (1993) Molecular biology of hemicellulases, in Hemicellulose and hemicellulases (Hazlewood, G. P. & Coughlan, M. P., eds) pp. 103-126, Portland Press, Cambridge.
5. Henrissat, B., Callebaut, I., Fabrega, S., Lehn, P., Mornon, J.-P. & Davies, G. (1995) Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases, Proc. Natl Acad. Sci. USA 92, 7090-7094.
6. Ko, E. P., Akatsnka, H., Moriyama, H., Shinmio, A., Hata, Y., Katsube, Y., Urabe, I. & Okada, H. (1992) Site-directed mutagenesis at aspartate and glutamate residues of xylanase from Bacillus pumilus. Biochem. J. 288, 117-121.
7. Moreau, A., Roerge, M., Manion, C., Shareck, F., Kluepfel, D. & Morosoli, R. (1994) Identification of two acidic residues involved in the catalysis of xylanase A from Streptomyces lividans. Biochem. J. 302, 291-295.
8. White, A., Withers, G., Gilkes, N. R. & Rose, D. R. (1995)Crystal structure of the catalytic domain of the β-1,4-glycanase Cex from Cellulomonas fimi. Biochemistry 33, 12546-12552.
9. Ruiz-Arribas, A., Santamaría, R. I., Zhadan, G. G., Villar, E. & Shnyrov, V. L. (1994) Differential scanning calorimetric study of the thermal stability of xylanase from Streptomyces halstedii JM8, Biochemistry 33, 13787-13791.
10. Ruiz-Arribas, A., Sánchez, P., Calvete, J. J., Fernández-Abalos, J. M. & Santamaría, R. I. (1997) Analysis of xysA, a gene from Streptomyces halstedii JM8 that encodes a 45-kilodalton modular xylanase, Xys1, Appl. Environ. Microbiol. 63, 2983-2988.
11. Ruiz-Arribas, A., Fernández-Abalos, J. M., Sánchcz, P., Garda, A. L. & Santamaría, R. I. (1995) Overproduction, purification, and biochemical characterization of a xylanase (Xys1) from Streptomyces halstedii JM8, Appl. Environ. Microbiol. 61, 2414-2419.
12. Hopwood, D. A., Bibb, J. M., Chater, K. F., Kieser, T., Bruton, C. J., Kieser, H. M., Lydiate, D. J., Smith, C. P., Ward, J. M. & Schrempf, H. (1985) Genetic manipulation of Streptomyces; a laboratory manual, John Innes Foundation, Norwich.
13. Sambrook, J., Fritsch, H. F. & Maniatis, T. (1989) Cloning: a laboratory manual, 2nd edn, Cold Spring Harbor Laboratory Press, Cold Spring Harbor NY.
14. Poole, D. M., Hazlewood, G. P., Huskinsson, N. S., Virden, R. & Gilbert, H. J. (1993) The role of conserved Trp residues in the interaction of a bacterial cellulose binding domain with its ligand, FEMS Microbiol. Lett. 106, 77-84.
15. Peterson, G. (1977) A simplification of the protein assay method of Lowry et al. which is more generally applicable, Anal. Biochem. 83, 346-356.
16. Deléage, G. & Roux, B. (1987) An algorithm for protein secondary structure prediction based on class prediction, Protein Eng, 1, 289-294.
17. Lin, L.-N., Mason, A. B., Woodworth, R. C. & Brandts, J. F. (1994) Calorimetric studies of serum transferrin and ovotransferrin, Estimates of domain interactions, and study of the kinetic complexities of ferric ion binding. Biochemistry 33, 1881-1888.
18. Permyakov, E. A. (1993) Luminiscence spectroscopy of proteins, CRC Press, Boca Raton FL.
19. Perczel, A., Hollosi, M., Tusnady, G. & Fasman, G. D. (1991) Convex constraint analysis: A natural deconvolution of circular dichroism curves of proteins, Protein Eng. 4, 669-679.
20. Becktel, W. J. & Schellman, J. A. (1987) Protein stability curves, Biopolymers 26, 1859-1877.
21. Pace, C. N. & Laurents, D. V. (1989) A new method for determining the heat capacity change for protein folding, Biochemistry 28, 2520-2525.
22. Privalov, P. L. & Khechinashvili, N. N. (1974) A thermodynamic approach to the problem of stabilization of globular protein structure: a calorimetric study, J. Mol. Biol. 86, 665-684.
23. Johnson, W. C. Jr (1990) Protein secondary structure and circular dichroism: a practical guide, Proteins Struct. Funct. Genet. 7, 205-214.
24. Privalov, P. L. & Gill, S. J. (1988) Stability of protein structure and hydrophobic interaction, Adv. Protein Chem. 39, 191-234.
25. Takahashi, K. & Sturtevant, J. M. (1981) Thermal denaturation of Streptomyces subtilisin inhibitor, subtilisin BPN', and the inhibitor-subtilisin complex, Biochemistry 20, 6185-6190.