Molecular and biochemical characterization of a new thermostable bacterial laccase from Meiothermus ruber DSM 1279

RSC Advances ◽  
2016 ◽  
Vol 6 (5) ◽  
pp. 3910-3918 ◽  
Author(s):  
D. C. Kalyani ◽  
L. Munk ◽  
J. D. Mikkelsen ◽  
A. S. Meyer
Keyword(s):  
Escherichia Coli ◽  
Biochemical Characterization ◽  
Soluble Form ◽  
Laccase Gene ◽  
Bacterial Laccase ◽  
Meiothermus Ruber ◽  
Chaperone Protein

A new bacterial laccase gene (mrlac) fromMeiothermus ruberDSM 1279 was successfully overexpressed to produce a laccase (Mrlac) in soluble form inEscherichia coliduring simultaneous overexpression of a chaperone protein (GroEL/ES).

Purification and biochemical characterization of a recombinant Anopheles gambiae tryptophan 2,3-dioxygenase expressed in Escherichia coli

2008 ◽  
Vol 38 (9) ◽  
pp. 871-876 ◽  
Author(s):  
Alessandra Paglino ◽  
Fabrizio Lombardo ◽  
Bruno Arcà ◽  
Menico Rizzi ◽  
Franca Rossi
Keyword(s):  
Escherichia Coli ◽  
Anopheles Gambiae ◽  
Biochemical Characterization

scholarly journals Molecular and Biochemical Characterization of the xlnD-Encoded 3-Hydroxybenzoate 6-Hydroxylase Involved in the Degradation of 2,5-Xylenol via the Gentisate Pathway in Pseudomonas alcaligenes NCIMB 9867

2005 ◽  
Vol 187 (22) ◽  
pp. 7696-7702 ◽  
Author(s):  
Xiaoli Gao ◽  
Chew Ling Tan ◽  
Chew Chieng Yeo ◽  
Chit Laa Poh
Keyword(s):  
Escherichia Coli ◽  
Fusion Protein ◽  
Molecular Mass ◽  
Electron Donor ◽  
Biochemical Characterization ◽  
Aromatic Substrates ◽  
Gentisate Pathway ◽  
A Subunit ◽  
Pseudomonas Alcaligenes

ABSTRACT The xlnD gene from Pseudomonas alcaligenes NCIMB 9867 (strain P25X) was shown to encode 3-hydroxybenzoate 6-hydroxylase I, the enzyme that catalyzes the NADH-dependent conversion of 3-hydroxybenzoate to gentisate. Active recombinant XlnD was purified as a hexahistidine fusion protein from Escherichia coli, had an estimated molecular mass of 130 kDa, and is probably a trimeric protein with a subunit mass of 43 kDa. This is in contrast to the monomeric nature of the few 3-hydroxybenzoate 6-hydroxylases that have been characterized thus far. Like other 3-hydroxybenzoate 6-hydroxylases, XlnD could utilize either NADH or NADPH as the electron donor. P25X harbors a second 3-hydroxybenzoate 6-hydroxylase II that was strictly inducible by specific aromatic substrates. However, the degradation of 2,5-xylenol and 3,5-xylenol in strain P25X was found to be dependent on the xlnD-encoded 6-hydroxylase I and not the second, strictly inducible 6-hydroxylase II.

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