Abstract
Three-phase partitioning (TPP) is a simple, fast, cost-effective, and highly efficient process that can be used in the purification of laccases. In this study, microorganisms with laccase activity were isolated from water samples collected from the Agri-Diyadin hot spring. The isolate with the highest laccase activity was found to be the A2 strain. As a result of molecular (16S rRNA sequence) and conventional (morphological, biochemical, and physiological) analyses, it was determined that the A2 isolate was 99% similar to Enterococcus faecium (Genbank number: MH424896). The laccase was purified to 4.9-fold with 110% recovery using the TPP. The molecular mass of the enzyme was found by SDS-PAGE to be 50.11kDa. Optimum pH 6.0 and optimum temperature for laccase were determined as 80°C. The laccase exhibited pH stability over a wide range (pH 3.0-9.0) and a high thermostability, retaining over 90% of its activity after 1h of incubation at 20-90°C. The laccase exhibited high thermostability, with a heat inactivation half-life of approximately 24h at 80°C. The enzyme remained highly stable in the presence of surfactants and increased its activity in the presence of organic solvents, Cr2+, Cu2+, and Ag+ metal ions. The Km, Vmax, kcat, and kcat/Km values of laccase for 2,2'-azino-bis (3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) substrate were 0.68mM, 5.29μmolmL-1min-1, 110.2s-1, and 162.1s-1mM-1, respectively.
Sign-in/Register to access full text options 
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 callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
