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Turkey Tail, Yun Zhi · 2014 · Research Support, Non U.S. Gov'T

Low relevance

Immobilized laccase on activated poly(vinyl alcohol) microspheres for enzyme thermistor application.

Trametes versicolor

OncologyImmune support
SpeciesTurkey Tail, Yun Zhi
JournalApplied biochemistry and biotechnology
Year2014

Key points

  • Poly(vinyl alcohol) (PVA) microspheres were prepared by inverse suspension crosslinked method, with glutaraldehyde as a crosslinking agent
  • PVA microspheres activated with aldehyde groups were employed for Trametes versicolor laccase immobilization
  • Fourier transform infrared spectroscopy and X-ray photoelectron spectroscopy were used to characterize the activated PVA microspheres and PVA microspheres with immobilized laccase (Lac/PVA microspheres), which show that laccase was successfully immobilized on the PVA microspheres
  • The optimum pH and temperature coupling conditions for the immobilized laccase were determined to be 3.3 and 30 °C, respectively
  • Residual activity was also investigated by soaking the immobilized laccase in organic solvents at different concentrations, proving it chemically stable
  • Immobilized laccase exhibited good storage stability at 4 °C. The enzyme biosensor showed good performance in 2,2-azinobis(3-ethylthiazoline-6-sulfonate) and bisphenol A, with concentration ranges of 2 to 8 mM and 0.05 to 0.25 mM, respectively

Metadata-grounded summary

Citation abstract

Poly(vinyl alcohol) (PVA) microspheres were prepared by inverse suspension crosslinked method, with glutaraldehyde as a crosslinking agent. PVA microspheres activated with aldehyde groups were employed for Trametes versicolor laccase immobilization. Fourier transform infrared spectroscopy and X-ray photoelectron spectroscopy were used to characterize the activated PVA microspheres and PVA microspheres with immobilized laccase (Lac/PVA microspheres), which show that laccase was successfully immobilized on the PVA microspheres. The optimum pH and temperature coupling conditions for the immobilized laccase were determined to be 3.3 and 30 °C, respectively. Residual activity was also investigated by soaking the immobilized laccase in organic solvents at different concentrations, proving it chemically stable. Immobilized laccase exhibited good storage stability at 4 °C. The enzyme biosensor showed good performance in 2,2-azinobis(3-ethylthiazoline-6-sulfonate) and bisphenol A, with concentration ranges of 2 to 8 mM and 0.05 to 0.25 mM, respectively. Therefore, PVA microspheres may have high potential as support for enzyme thermistor applications.

Citation

Bai X, Gu H, Chen W, Shi H, Yang B, Huang X, et al. (2014). Immobilized laccase on activated poly(vinyl alcohol) microspheres for enzyme thermistor application. Applied biochemistry and biotechnology https://doi.org/10.1007/s12010-014-0913-3 PMID: 24760609

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