Biochemical characterization of a novel azo reductase named BVU5 from the bacterial flora DDMZ1: application for decolorization of azo dyes
Junhao Cong, Xuehui Xie, Yanbiao Liu, Qin Yan, Jiao Fan, Yingrong Fang, Na Liu, Qingyun Zhang, Xinshan Song, Wolfgang Sand
Abstract
-hexane. However, the enzyme BVU5 has a low tolerance to high concentrations of denaturants. In particular, it is sensitive to the denaturants guanidine hydrochloride (GdmCl) (2 M) and urea (2 M). Analysis of the dye substrate specificity shows that enzyme BVU5 decolorizes most azo dyes, which is indicating that the enzyme is not strictly substrate specific, it is a functional enzyme for breaking the azo structure. Liquid chromatography/time-of-flight/mass spectrometry (LC-TOF-MS) revealed after the action of enzyme BVU5 that some intermediate products with relatively large molecular weights were produced; this illustrates a symmetric or an asymmetric rapid cleavage of the azo bonds by this enzyme. The potential degradation pathways and the enzyme-catalyzed degradation mechanism are deduced in the end of this paper. The results give insight into the potential of a rapid bio-pretreatment by enzyme BVU5 for processing azo dye wastewater.