Purification and characterization of intracellular and extracellular, thermostable and alkali-tolerant alcohol oxidases produced by a thermophilic fungus, Thermoascus aurantiacus NBRC 31693

2005 ◽  
Vol 99 (4) ◽  
pp. 348-353 ◽  
Author(s):  
Hee-Sun Ko ◽  
Yuichi Yokoyama ◽  
Nobuko Ohno ◽  
Miho Okadome ◽  
Seigo Amachi ◽  
...  
Keyword(s):  
Thermophilic Fungus ◽  
Thermoascus Aurantiacus ◽  
Purification And Characterization

Purification and characterization of a thermostable xylanase from a thermophilic fungus Thermoascus aurantiacus

1987 ◽  
Vol 33 (8) ◽  
pp. 689-692 ◽  
Author(s):  
Larry U. L. Tan ◽  
Paul Mayers ◽  
John N. Saddler
Keyword(s):  
Xylanase Activity ◽  
Barium Chloride ◽  
Thermophilic Fungus ◽  
Mercury Chloride ◽  
Thermoascus Aurantiacus ◽  
Purification And Characterization ◽  
Acting Mechanism ◽  
A Subunit ◽  
Temperature Optima

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.

Purification and characterization of the α-glucosidase produced by thermophilic fungus Thermoascus aurantiacus CBMAI 756

2010 ◽  
Vol 48 (4) ◽  
pp. 452-459 ◽  
Author(s):  
Ana Flávia Azevedo Carvalho ◽  
Maurício Boscolo ◽  
Roberto da Silva ◽  
Henrique Ferreira ◽  
Eleni Gomes
Keyword(s):  
Thermophilic Fungus ◽  
Thermoascus Aurantiacus ◽  
Purification And Characterization

Purification and characterization of low molecular weight extreme alkaline xylanase from the thermophilic fungus Myceliophthora thermophila BF1-7

Mycoscience ◽  
2016 ◽  
Vol 57 (6) ◽  
pp. 408-416 ◽  
Author(s):  
Santhaya Boonrung ◽  
Somporn Katekaew ◽  
Wiyada Mongkolthanaruk ◽  
Tadanori Aimi ◽  
Sophon Boonlue
Keyword(s):  
Molecular Weight ◽  
Thermophilic Fungus ◽  
Low Molecular Weight ◽  
Myceliophthora Thermophila ◽  
Purification And Characterization
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