Purification and characterization of a thermostable intracellular β-xylosidase from the thermophilic fungus Sporotrichum thermophile

2006 ◽  
Vol 41 (12) ◽  
pp. 2402-2409 ◽  
Author(s):  
Petros Katapodis ◽  
Wim Nerinckx ◽  
Marc Claeyssens ◽  
Paul Christakopoulos
Keyword(s):  
Thermophilic Fungus ◽  
Purification And Characterization ◽  
Sporotrichum Thermophile

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

scholarly journals Purification and characterization of a new alkaline serine protease from the thermophilic fungus Myceliophthora sp.

2011 ◽  
Vol 46 (11) ◽  
pp. 2137-2143 ◽  
Author(s):  
L.M. Zanphorlin ◽  
H. Cabral ◽  
E. Arantes ◽  
D. Assis ◽  
L. Juliano ◽  
...  
Keyword(s):  
Serine Protease ◽  
Thermophilic Fungus ◽  
Purification And Characterization ◽  
Alkaline Serine Protease

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 an extracellular glucoamylase from the thermophilic fungus Humicola grisea var. thermoidea

1993 ◽  
Vol 39 (9) ◽  
pp. 846-852 ◽  
Author(s):  
Luis Ricardo Orsini Tosi ◽  
Héctor Francisco Terenzi ◽  
Joāo Atílio Jorge
Keyword(s):  
Molecular Mass ◽  
Half Life ◽  
Carbohydrate Content ◽  
Thermophilic Fungus ◽  
Apparent Molecular Mass ◽  
Purification And Characterization ◽  
Sds Page ◽  
Humicola Grisea ◽  
Temperature Optima

Humicola grisea var. thermoidea mycelium grown on maltose as the main source of carbon produced at least two amylases. The major amylolytic component was purified to homogeneity and classified as a glucoamylase. The apparent molecular mass of the purified enzyme was estimated to be 63 000 Da by SDS-PAGE and 65 000 Da by Bio-Gel P-100 filtration. The purified enzyme was a glycoprotein with 1.8% carbohydrate content and pH and temperature optima of 5.0 and 55 °C, respectively. The purified glucoamylase was thermostable at 60 °C with a half-life of 16 min at 65 °C. In the presence of starch the purified enzyme retained 75% of its thermostability at 65 °C, while the addition of maltose failed to protect the activity. The purified enzyme hydrolyzed branched substrates more efficiently than linear substrates. Starch and amylopectin were the best substrates utilized and amylose was hydrolyzed faster than maltopentaose, maltotetraose, and maltotriose. Kinetic experiments suggested that maltose and starch were hydrolyzed at the same catalytic site.Key words: glucoamylase, amylase, Humicola grisea.

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