TY - JOUR
T1 - The response surface methodology for optimization of tyrosinase immobilization onto electrospun polycaprolactone-chitosan fibers for use in bisphenol A removal
AU - Zdarta, Jakub
AU - Staszak, Maciej
AU - Jankowska, Katarzyna
AU - Kaźmierczak, Karolina
AU - Degórska, Oliwia
AU - Nguyen, Luong N
AU - Kijeńska-Gawrońska, Ewa
AU - Pinelo, Manuel
AU - Jesionowski, Teofil
PY - 2020
Y1 - 2020
N2 - Composite polycaprolactone-chitosan material was produced by an electrospinning method and used as a support for immobilization of tyrosinase by mixed ionic interactions and hydrogen bonds formation. The morphology of the fibers and enzyme deposition were confirmed by SEM images. Further, multivariate polynomial regression was used to model the experimental data and to determine optimal conditions for immobilization process, which were found to be pH 7, temperature 25 °C and 16 h process duration. Under these conditions, novel type of biocatalytic system was produced with immobilization yield of 93% and expressed activity of 95%. Furthermore, as prepared system was applied in batch experiments related to biodegradation of bisphenol A under various remediation conditions. It was found that over 80% of the pollutant was removed after 120 min of the process, in the temperature range 15-45 °C and pH 6-9, using solutions at concentration up to 3 mg/L., Experimental data collected proved that the stability and reusability of the tyrosinase were significantly improved upon immobilization: the immobilized biomolecule retained around 90% of its initial activity after 30 days of storage, and was still capable to remove over 80% of bisphenol A even after 10 repeated uses. By contrast, free enzyme was able to remove over 80% of bisphenol A at pH 7-8 and temperature range 15-35 °C, and retained less than 60% of its initial activity after 30 days of storage.
AB - Composite polycaprolactone-chitosan material was produced by an electrospinning method and used as a support for immobilization of tyrosinase by mixed ionic interactions and hydrogen bonds formation. The morphology of the fibers and enzyme deposition were confirmed by SEM images. Further, multivariate polynomial regression was used to model the experimental data and to determine optimal conditions for immobilization process, which were found to be pH 7, temperature 25 °C and 16 h process duration. Under these conditions, novel type of biocatalytic system was produced with immobilization yield of 93% and expressed activity of 95%. Furthermore, as prepared system was applied in batch experiments related to biodegradation of bisphenol A under various remediation conditions. It was found that over 80% of the pollutant was removed after 120 min of the process, in the temperature range 15-45 °C and pH 6-9, using solutions at concentration up to 3 mg/L., Experimental data collected proved that the stability and reusability of the tyrosinase were significantly improved upon immobilization: the immobilized biomolecule retained around 90% of its initial activity after 30 days of storage, and was still capable to remove over 80% of bisphenol A even after 10 repeated uses. By contrast, free enzyme was able to remove over 80% of bisphenol A at pH 7-8 and temperature range 15-35 °C, and retained less than 60% of its initial activity after 30 days of storage.
KW - Enzyme immobilization
KW - Biocatalysts
KW - Immobilization optimization
KW - Bisphenol A removal
U2 - 10.1016/j.ijbiomac.2020.10.081
DO - 10.1016/j.ijbiomac.2020.10.081
M3 - Journal article
C2 - 33086111
SN - 0141-8130
VL - 165
SP - 2049
EP - 2059
JO - International Journal of Biological Macromolecules
JF - International Journal of Biological Macromolecules
ER -