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Título

Hyperthermophilic aldolases as biocatalyst for C–C bond formation: rhamnulose 1-phosphate aldolase from Thermotoga maritima

Autor Oroz-Guinea, Isabel ; Sánchez-Moreno, Israel ; Mena, Montaña; García-Junceda, Eduardo
Palabras clave Aldolases
Biocatalysis
Enzyme catalysis
Hyperthermophilic enzymes
Thermozyme
Thermostability
Fecha de publicación 2015
EditorSpringer
Citación Applied Microbiology and Biotechnology 99 : 3057–3068 (2015)
ResumenThe TM1072 gene from Thermotoga maritima codifies for a putative form of a rhamnulose-1-phosphate aldolase (Rha-1PATm). To investigate this enzyme further, its gene was cloned and expressed in Escherichia coli. The purified enzyme was activated by Co2+ as a divalentmetal ion cofactor, instead of Zn2+ as its E. coli homologue, and exhibited a maximum of activity at 95 °C. Furthermore, the enzyme displayed a high stability against extreme reaction conditions, retaining 90 % of its activity in the presence of 40 % of acetonitrile and showing a half-life greater than 3 h at 115 °C. The kinetic parameters at room temperature (R/T) were also studied; the KM was calculated to be 3.6±0.33 mM, while kcat/KM was found to be 0.7× 103 s−1 M−1. Given these characteristics, Rha-1PA Tm is an attractive enzyme for use as a biocatalyst for industrial applications, offering intriguing possibilities for practical biocatalysis.
Versión del editorhttp://dx.doi.org/10.1007/s00253-014-6123-7
URI http://hdl.handle.net/10261/113297
DOI10.1007/s00253-014-6123-7
ISSN0175-7598
E-ISSN1432-0614
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