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Background   Benzaldehyde dehydrogenase (BZDH) is encoded by the  xylC  that catalyzes the conversion of benzaldehyde into benzoate in many pathways such as toluene degradation.Objectives   In this study, the  xylC  gene from  Rhodococcus ruber  UKMP-5M was expressed in  Escherichia coli , purified, and characterized.Materials and Methods   The  xylC  was amplified and cloned in  E. coli . The recombinant plasmid  pGEMT-xylC  was digested by NdeI and HindIII to construct plasmid  pET28b-xylC  and transformed in  E. coli  BL21 (DE3). Expression of the recombinant protein was induced by 1 mM isopropyl β-D-thiogalactoside (IPTG) at 37°C. The BZDH was purified by ion exchange chromatography, in which the product was an NAD-dependent enzyme using benzaldehyde as a substrate for enzyme characterization. The end metabolite was identified via gas chromatography mass spectrometry (GC-MS).Results   The recombinant BZDH is 27 kDa, purified by ion exchange chromatography. The activity of BZDH was 9.4 U.μL -1  The optimum pH and temperature were 8.5 and 25ºC, respectively. The Michaelis constant (K m ) and maximum velocity (V max ) were 4.2 mM and 19.7 U.mL -1 , respectively. The metabolite of BZDH was benzene carboxylic acid as determined by GC-MS analysis.Conclusions   BZDH has the ability to degrade benzaldehyde to less toxic compounds. The BZDH is a critical enzyme for the degradation of aromatic hydrocarbons in  Rhodococcus  sp. The BZDH from R. ruber UKMP-5M is showed similar function with other aldehyde dehydrogenases.

Partial Purifi cation and Characterization of the Recombinant Benzaldehyde Dehydrogenase from Rhodococcus ruber UKMP-5M