scholarly journals Purification and characterization of a thermostable glucoamylase from the thermophilic fungus Thermomyces lanuginosus

1981 ◽  
Vol 193 (2) ◽  
pp. 379-387 ◽  
Author(s):  
V Basaveswara Rao ◽  
N V S Sastri ◽  
P V Subba Rao
Keyword(s):  
Molecular Weight ◽  
Thermal Denaturation ◽  
Average Molecular Weight ◽  
Thermophilic Fungus ◽  
Thermomyces Lanuginosus ◽  
Chain Mechanism ◽  
Purification And Characterization ◽  
Substrate Molecule ◽  
Starch Molecule

Glucoamylase (1,4-alpha-D-glucan glucohydrolase, EC 3.2.1.3) was purified from the culture filtrates of the thermophilic fungus Thermomyces lanuginosus and was established to be homogeneous by a number of criteria. The enzyme was a glycoprotein with an average molecular weight of about 57 000 and a carbohydrate content of 10-12%. The enzyme hydrolysed successive glucose residues from the non-reducing ends of the starch molecule. It did not exhibit any glucosyltransferase activity. The enzyme appeared to hydrolyse maltotriose by the multi-chain mechanism. The enzyme was unable to hydrolyse 1,6-alpha-D-glucosidic linkages of isomaltose and dextran. It was optimally active at 70 degrees C. The enzyme exhibited increase in the Vmax. and decreased in Km values with increasing chain length of the substrate molecule. The enzyme was inhibited by the substrate analogue D-glucono-delta-lactone in a non-competitive manner. The enzyme inhibited remarkable resistance towards chemical and thermal denaturation.

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

Prothrombin Metz : Purification and Characterization of a Variant of Human Prothrombin

1979 ◽  
Author(s):  
M Ribieto ◽  
J Elion ◽  
D Labie ◽  
F Josso
Keyword(s):  
Molecular Weight ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Factor Xa ◽  
Polyacrylamide Gel ◽  
Cleavage Pattern ◽  
Purification And Characterization ◽  
Double Immunodiffusion ◽  
The Family

For the purification of the abnormal prothrombin (Pt Metz), advantage has been taken of the existence in the family of three siblings who, being double heterozygotes for Pt Metz and a hypoprothrombinemia, have no normal Pt. Purification procedures included barium citrate adsorption and chromatography on DEAE Sephadex as for normal Pt. As opposed to some other variants (Pt Barcelona and Madrid), Pt Metz elutes as a single symetrical peak. By SDS polyacrylamide gel electrophoresis, this material is homogeneous and appears to have the same molecular weight as normal Pt. Comigration of normal and abnormal Pt in the absence of SDS, shows a double band suggesting an abnormal charge for the variant. Pt Metz exhibits an identity reaction with the control by double immunodiffusion. Upon activation by factor Xa, Pt Metz can generate amydolytic activity on Bz-Phe-Val-Arg-pNa (S2160), but only a very low clotting activity. Clear abnormalities are observed in the cleavage pattern of Pt Metz when monitored by SDS gel electrophoresis. The main feature are the accumulation of prethrombin l (Pl) and the appearance of abnormal intermediates migrating faster than Pl.

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