Molecular cloning and characterization of vanillin dehydrogenase from Streptomyces sp. NL15-2K.

ABSTRACT:

Background

Streptomyces sp. NL15-2K, previously isolated from the forest soil, features an extensive catabolic network for lignin-derived aromatic compounds, including pathways transforming ferulic acid to vanillin, vanillic acid, and protocatechuic acid. To successfully use Streptomyces sp. NL15-2K as a biocatalyst for vanillin production, it is necessary to characterize the vanillin dehydrogenase (VDH) that degrades the produced vanillin to vanillic acid, as well as the gene encoding this enzyme. Here, we cloned the VDH-encoding gene (vdh) from strain NL15-2K and comprehensively characterized its gene product.

Results

The vdh open reading frame contains 1488 bp and encodes a 496-amino-acid protein with a calculated molecular mass of 51,705 Da. Whereas the apparent native m

SUBMITTER: Nishimura M 

PROVIDER: S-EPMC6201588 | biostudies-literature | 2018 Oct

REPOSITORIES: biostudies-literature