Biodegradation of bisphenol A by the immobilized laccase on some synthesized and modified forms of zeolite Y.

Bisphenol A (BPA) is an environmental pollutant with adverse effects on different ecosystems. In this study, immobilized laccase enzymes onto inorganic supports were used to remove BPA. Laccase was successfully immobilized on sodium zeolite Y (NaY) and its modified desilicated (DSY) and dealuminated (DAY) forms. NaY-based supports were instrumentally characterized. The immobilized laccase on NaY (laccase@NaY), desilicated (laccase@DSY), and dealuminated (laccase@DAY) forms showed significant improvement on immobilization yield (IY%) and efficiency (IE%). Laccase@DSY and laccase@NaY showed IY% = 73.18 ± 3.33 % and 46.23 ± 1.81 % and IE% = 94.50 ± 1.86 %, and 74.39 ± 1.41 %, respectively, whereas IY% and IE% for laccase@DAY were achieved as 81.12 ± 1.32 % and 98.56 ± 2.93 %, respectively. The supports also increased the enzyme characteristics such as pH-temperature range, catalytic stability, and reusability. K values were 0.73 ± 0.05, 0.26 ± 0.09, 0.31 ± 0.5, and 1.01 ± 0.03 mM for laccase@NaY, laccase@DAY, laccase@DSY, and the free enzyme, respectively. The enzyme demonstrated higher biodegradation ability of bisphenol A upon immobilization on the supports compared to that of the soluble enzyme. A bio-removal yield of 86.7 % was obtained considering three parameters including amount of laccase@DAY (8 U mg), concentration of BPA (0.5 mM), and treatment time (1 h) based on response surface methodology (RSM). Biodegradation metabolites (49 ± 5.8 %) and unconverted BPA (14 ± 5.2 %) were analyzed by gas chromatography-mass spectrometry.