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Updated: Aug 30, 2026
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Published on: February 24, 2026
A thermostable laccase from Streptomyces lavendulae REN-7: purification, characterization, nucleotide sequence, and
Takashi Suzuki1, Kohki Endo, Masaaki Ito
1Central Laboratory, Rengo Co., Ltd., Ohhiraki, Osaka, Japan.
Abstract:
We found a polyphenoloxidase (PPO) in the cell extract of Streptomyces lavendulae REN-7. About 0.8 mg of purified PPO was obtained from 200 g of the mycelia with a yield of 9.0%. REN-7-PPO showed broad substrate specificity toward various aromatic compounds. Moreover, this enzyme was capable of oxidation of syringaldazine, which is a specific substrate for laccase. Interestingly, REN-7-PPO retained its original activity after 20 min of incubation at even 70 degrees C. The gene encoding the PPO was cloned. Four copper-binding sites characteristics of laccases were contained in the deduced amino acid sequence. We constructed a high-level expression system of this gene in Escherichia coli. The properties of the recombinant enzyme were identical that of wild-type. In conclusion, this PPO is a thermostable laccase.
