Access the full text.
Sign up today, get DeepDyve free for 14 days.
W. Wakarchuk, R. Campbell, W. Sung, J. Davoodi, M. Yaguchi (1994)
Mutational and crystallographic analyses of the active site residues of the bacillus circulans xylanaseProtein Science, 3
R. Horton, H. Hunt, S. Ho, J. Pullen, L. Pease (1989)
Engineering hybrid genes without the use of restriction enzymes: gene splicing by overlap extension.Gene, 77 1
Hajime Shibuya, Satoshi Kaneko, Kiyoshi Hayashi (2000)
Enhancement of the thermostability and hydrolytic activity of xylanase by random gene shuffling.The Biochemical journal, 349 Pt 2
P. Biely (1985)
Microbial xylanolytic systemsTrends in Biotechnology, 3
A. Törrönen, A. Harkki, J. Rouvinen (1994)
Three‐dimensional structure of endo‐1,4‐beta‐xylanase II from Trichoderma reesei: two conformational states in the active site.The EMBO Journal, 13
M. Gibbs, K. Nevalainen, P. Bergquist, P. Bergquist (2001)
Degenerate oligonucleotide gene shuffling (DOGS): a method for enhancing the frequency of recombination with family shuffling.Gene, 271 1
O. Turunen, K. Etuaho, Fred Fenel, J. Vehmaanperä, Xiaoyan Wu, Juha Rouvinen, M. Leisola (2001)
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.Journal of biotechnology, 88 1
Akemi Arase, T. Yomo, I. Urabe, Y. Hata, Y. Katsube, H. Okada (1993)
Stabilization of xylanase by random mutagenesisFEBS Letters, 316
M. Bradford (1976)
A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding.Analytical biochemistry, 72
J. Sambrook, E. Fritsch, T. Maniatis (2001)
Molecular Cloning: A Laboratory Manual
A Arase, T Yomo, I Urabe, Y Hata, Y Kastube, H Okada (1993)
Stabilization by random mutagenesisFEBS Lett, 316
G. Harris, R. Pickersgill, I. Connerton, P. Debeire, J. Touzel, C. Breton, S. Pérez (1997)
Structural basis of the properties of an industrially relevant thermophilic xylanaseProteins: Structure, 29
D. Irwin, E. Jung, D. Wilson (1994)
Characterization and sequence of a Thermomonospora fusca xylanaseApplied and Environmental Microbiology, 60
Ute Krengel, B. Dijkstra (1996)
Three-dimensional structure of Endo-1,4-beta-xylanase I from Aspergillus niger: molecular basis for its low pH optimum.Journal of molecular biology, 263 1
N. Kulkarni, A. Shendye, M. Rao (1999)
Molecular and biotechnological aspects of xylanases.FEMS microbiology reviews, 23 4
S. Subramaniyan, P. Prema (2002)
Biotechnology of Microbial Xylanases: Enzymology, Molecular Biology, and ApplicationCritical Reviews in Biotechnology, 22
A. Sapag, J. Wouters, C. Lambert, P. Ioannes, J. Eyzaguirre, E. Depiereux (2002)
The endoxylanases from family 11: computer analysis of protein sequences reveals important structural and phylogenetic relationships.Journal of biotechnology, 95 2
D. Kluepfel, Tarja Lahtinen, A. Marzetti, A. Barbarosa, M. Moo-young (2002)
Interlaboratory testing of methods for assay of xylanase activity
U. Laemmli (1970)
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 227
G. Miller (1959)
Use of Dinitrosalicylic Acid Reagent for Determination of Reducing SugarAnalytical Chemistry, 31
A hybrid gene, btx, encoding a thermostable xylanase, Btx, was constructed by substituting the 31 N-terminal amino acid residues of the Thermomonospora fusca xylanase A (TfxA) for the corresponding region of 22 amino acid residues of the Bacillus subtilis xylanase A (BsxA). The btx gene was expressed in Escherichia coli BL21. The halo size produced by xylanase Btx on a Remanzol brilliant blue R (RBB) xylan plate at 60°C and pH 6.0 was larger than those of BsxA and TfxA. The molecular weight of Btx was 22 kDa. Temperature and pH optima for Btx were at 50–60°C and 6.0, respectively. Btx showed activity over 80% over a pH range of 5.0–9.0, which was wider than that of BsxA, and was also more acid-resistant than TfxA. Btx exhibited significant thermostability compared with BsxA. The results show the importance of the N-terminal sequence of TfxA in thermostability.
Current Microbiology – Springer Journals
Published: Aug 2, 2005
Read and print from thousands of top scholarly journals.
Already have an account? Log in
Bookmark this article. You can see your Bookmarks on your DeepDyve Library.
To save an article, log in first, or sign up for a DeepDyve account if you don’t already have one.
Copy and paste the desired citation format or use the link below to download a file formatted for EndNote
Access the full text.
Sign up today, get DeepDyve free for 14 days.
All DeepDyve websites use cookies to improve your online experience. They were placed on your computer when you launched this website. You can change your cookie settings through your browser.