Purification and Properties of Malate Dehydrogenase from the Extreme Thermophile Bacillus Caldolyticus

1980 ◽  
pp. 47-54
Author(s):  
Hordur Kristjansson ◽  
Cyril Ponnamperuma
Keyword(s):  
Malate Dehydrogenase ◽  
Extreme Thermophile ◽  
Purification And Properties

scholarly journals Purification and properties of an aryl β-xylosidase from a cellulolytic extreme thermophile expressed in Escherichia coli

1991 ◽  
Vol 273 (3) ◽  
pp. 645-650 ◽  
Author(s):  
R C Hudson ◽  
L R Schofield ◽  
T Coolbear ◽  
R M Daniel ◽  
H W Morgan
Keyword(s):  
Escherichia Coli ◽  
Thermal Inactivation ◽  
Competitive Inhibitor ◽  
Coli Strain ◽  
Extreme Thermophile ◽  
First Order ◽  
Optimal Activity ◽  
First Order Kinetics ◽  
Purification And Properties ◽  
Optimum Ph

An aryl beta-xylosidase was purified to homogeneity from an Escherichia coli strain containing a recombinant plasmid carrying a beta-xylosidase (EC 3.2.1.37) gene from the extremely thermophilic anaerobic bacterium isolate Tp8T6.3.3.1 (‘Caldocellum saccharolyticum’). It has a pI of 4.3 and shows optimal activity at pH 5.7. The enzyme is highly specific, acting on o- and p-nitrophenyl beta-D-xylopyranosides and minimally on p-nitrophenyl alpha-L-arabinopyranoside. It does not act on xylobiose. The Km for p-nitrophenyl beta-D-xylopyranoside at the optimum pH for activity is 10 mM, and at pH 7.0 is 6.7 mM. Xylose is a competitive inhibitor with Ki 40 mM. Thermal inactivation follows first-order kinetics at 65 and 70 degrees C with t1/2 values of 4.85 h and 40 min respectively. The t1/2 at 70 degrees C is increased 3-fold and 4-fold by the addition of 0.5 mg of BSA/ml and 2 mM-dithiothreitol respectively.

Purification and Properties of Novel Malate Dehydrogenase Isolated from Pseudomonas aeruginosa

2011 ◽  
Vol 3 (5) ◽  
pp. 478-485 ◽  
Author(s):  
Ponnuswamy Vijayaragh ◽  
Surgen A. Bright ◽  
Anuj Nishanth L ◽  
S.G. Prakash Vincent
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Malate Dehydrogenase ◽  
Purification And Properties
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