AI Article Synopsis
- The small laccase (SLAC) enzyme from *Streptomyces coelicolor* A3(2) was successfully expressed and secreted in *Pichia pastoris*, achieving a high production level of 500 U/l.
- Pre-incubation at 80°C for 30 minutes further increased the enzyme's production by seven times, and the SLAC showed optimal activity at 80°C with varying pH levels depending on the substrate.
- The enzyme demonstrated effective dye decolorization, achieving over 90% removal of certain dyes in just 6 hours, showcasing its potential for industrial applications.
Article Abstract
This work reports for the first time the secretory expression of the small laccase (SLAC) from Streptomyces coelicolor A3(2) in Pichia pastoris. Using an AOX1 promoter and α factor as a secretion signal, the recombinant P. pastoris harbouring the laccase gene (rSLAC) produced high titres of extracellular laccase (500 ± 10 U/l), which were further increased seven fold by pre-incubation at 80 °C for 30 min. The enzyme (∼38 kDa) had an optimum activity at 80 °C, but optimum pH varied with substrate used. K values for ABTS, SGZ and 2,6-DMP were 142.85 μM, 10 μM and 54.55 μM and the corresponding k values were 60.6 s, 25.36 s and 27.84 s, respectively. The t values of the rSLAC at 60 °C, 70 °C, 80 °C were 60 h, 32 h and 10 h, respectively. The enzyme deactivation energy (E) was 117.275 kJ/mol while ΔG, ΔH and ΔS for thermal inactivation of the rSLAC were all positive. The rSLAC decolourised more than 90% of Brilliant Blue G and Trypan Blue dye in 6 h without the addition of a mediator. High titres of SLAC expressed in P. pastoris enhance its potential for various industrial applications.
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| http://dx.doi.org/10.1016/j.ijbiomac.2017.11.169 | DOI Listing |
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