Abstract
The enzyme 2,3‐Butanediol dehydrogenase (BDH) plays important roles in reduction of acetoin to 2,3‐butanediol which is an important platform chemical with many industrial applications. Here, a TcBDH cDNA (1348 bp) encoding a putative BDH was cloned from Taiwanofungus camphorata. The deduced amino acid sequence is similar to the BDHs from other species. A 3‐D structural model of TcBDH has been constructed based on the known structure of Pseudomonas putida formaldehyde dehydrogenase (PpFdh, PDB code 1KOL). To characterize the TcBDH protein, the coding region was subcloned into an expression vector pYEX‐S1 and transformed into Saccharomyces cerevisiae. The recombinant His6‐tagged TcBDH was expressed and purified by Ni2+‐nitrilotriacetic acid Sepharose. The purified enzyme showed a single band of ~50 kD on 12% sodium dodecyl sulfate‐polyacrylamide gel electrophoresis. The Michaelis constant (KM) value of the recombinant enzyme for acetoin was 8.46 mM. The enzyme’s optimal pH was 6.Grant Funding Source: National Science Council of the Republic of China, Taiwan under grant NSC 100‐2313‐B‐019‐003‐MY3
Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
