Production of highly thermostable xylanase by a wild strain of thermophilic fungus Thermoascus aurantiacus and partial characterization of the enzyme

1994 ◽  
Vol 37 (1) ◽  
pp. 11-22 ◽  
Author(s):  
D.J. Gomes ◽  
J. Gomes ◽  
W. Steiner
1987 ◽  
Vol 33 (8) ◽  
pp. 689-692 ◽  
Author(s):  
Larry U. L. Tan ◽  
Paul Mayers ◽  
John N. Saddler

A thermostable endo-β-D-xylanase (1,4-β-D-xylan xylanohydrolase, EC 3.2.1.8) was purified from the culture filtrate of a thermophilic fungus Thermoascus aurantiacus C436, using a single chromatographic step on SP-Sephadex C50. The purified preparation was homogeneous based on denaturing polyacrylamide and isoelectric focusing gels. The xylanase had a subunit molecular mass of 32 000 daltons, isoelectric point at pH 7.1, apparent Km and Vmax of 0.17% (w/v) xylan and 61.3IU/mg protein, respectively, at 50 °C. The pH and temperature optima for xylan hydrolysis were pH 5.1 and 80 °C, respectively. The xylanase retained full activity following incubation at 60 °C for 97 h or 70 °C for 24 h. At 80 °C, the half-life of the enzyme was 54 min. The xylanase was not affected by copper sulfate, zinc sulfate, calcium chloride, cobalt chloride, barium chloride, magnesium sulfate, and EDTA at concentrations of 2 mM. Mercury chloride at 2 mM concentration abolished all xylanase activity, while lead acetate at the same concentration reduced xylanase activity by approximately 25%. From the initial hydrolysis products of xylan, the xylanase was deduced to hydrolyse xylan through an endo-acting mechanism.


2007 ◽  
Vol 131 (2) ◽  
pp. S232 ◽  
Author(s):  
Ana Flávia Azevedo Carvalho ◽  
Rodrigo Simões Ribeiro Leite ◽  
Eduardo Martins ◽  
Natália Martin ◽  
Roberto Silva ◽  
...  

1987 ◽  
Vol 9 (1) ◽  
pp. 16-24 ◽  
Author(s):  
Ernest K.C. Yu ◽  
Larry U.L. Tan ◽  
Maria K.-H. Chan ◽  
Lise Deschatelets ◽  
John N. Saddler

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