Characterization of a New Laccase from Vibrio sp. with pH-stability, Salt-tolerance, and Decolorization Ability

Laccases have been widely used for fruit juice clarification, food modification, and paper pulp delignification. In addition, laccases exhibit remarkable performance in the degradation of toxic substances, including pesticides, organic synthetic dyes, antibiotics, and organic pollutants. Thus, the screening and development of robust laccases has attracted significant attention. In this study, Vibrio sp. LA is a strain capable of producing cold-adapted laccases. The laccase coding gene L01 was cloned from this strain and expressed in Yarrowia lipolytica, a host with good secretion ability. The secreted L01 (approximate MW of 56,000 Da) had the activity and specific activity of 18.6 U/mL and 98.6 U/mg toward ABTS, respectively. The highest activity occurred at 35 ?. At 20 ?, L01 activity was over 70% of the maximum activity in pH conditions ranging from 4.5-10.0. Several synthetic dyes were efficiently degraded by L01. Owing to its robustness, salt tolerance, and pH stability, L01 is a promising catalytic tool for potential industrial applications.

Automated summary

In this study, the laccase coding gene L01 was successfully cloned from a cold-adapted Vibrio sp. LA strain and expressed in the high secretion host Yarrowia lipolytica. The secreted L01 showed high activity and specific activity towards ABTS with the highest activity observed at 35 ℃ and pH conditions ranging from 4.5-10.0. L01 efficiently degraded several synthetic dyes and exhibited robustness, salt tolerance, and pH stability, making it a promising catalytic tool for potential industrial applications.