3 years ago

Bacillus amyloliquefaciens CotA degradation of the lignin model compound guaiacylglycerol‐β‐guaiacyl ether

H. Li, Z.Z. Li, H.Y. Li, J. Yang, M.Y. Gao, M. Li


The cotA gene from Bacillus amyloliquefaciens MN‐13 was cloned and expressed in Escherichia coli Transetta (DE3). Nucleotide sequence analysis showed an open reading frame of 1542 bp encoding a polypeptide comprised of 513 amino acids. The degradation of lignin model compounds by recombinant CotA was investigated by HPLC‐MS with guaiacylglycerol‐β‐guaiacyl ether as the substrate. The compounds including guaiacol, 3‐(4‐hydro‐3‐methoxyphenyl)‐3‐oxo‐propanol and 4‐hydro‐3‐methoxy acetophenone detected by HPLC‐MS verified the rupture of β‐O‐4 bond and oxidation Cα bond of guaiacylglycerol‐β‐guaiacyl ether by CotA. 4‐vinylguaiacol and 1‐(4‐hydroxy‐3‐methoxyl phenyl)‐1‐(2‐methoxyl) phenoxyl ethylene were first time found in the degradation products of guaiacylglycerol‐β‐guaiacyl ether. The appearance of 4‐vinylguaiacol and 4‐hydro‐3‐methoxy acetophenone confirmed the cleavage of Cβ‐Cγ bond. 1‐(4‐hydroxy‐3‐methoxyl phenyl)‐2‐(2‐methoxyl) phenoxyl ethylene was coupled by the radical reaction of 4‐vinylguaiacol with guaiacol. Otherwise, no corresponding degradation product was found to give a proof of cleavage of Cα‐Cβ bond in guaiacylglycerol‐β‐guaiacyl ether by CotA.

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