PHENOL DEGRADATION CATALYZED BY MAGNETICALLY IMMOBILIZED TYROSINASE
The magnetically immobilized tyrosinase (MIT) was prepared by using sodium alginate crosslinked with glutaraldehyde in the presence of magnetic powder. The immobilized tyrosinase was magnetized (M-MIT) and used for catalyzing phenol oxidation. Compared with the conventional immobilized tyrosinase (IT) without magnetic particles, higher enzyme activities were found for MIT and M-MIT. The MIT and M-MIT are also of better pH stability and thermal-stability. The Michaelis constants of IT, MIT and M-MIT were determined to be 0.953 mrnol·L-1, 0.838 mmol·L-1 and 0.773 mmol·L-1 respectively. The phenol degradation rates catalyzed by MIT and M-MIT were obviously higher than that of IT. Tyrisinase immobilized on the magnetic beads with or without magnetization maintained 55% and 51% of the phenol oxidation activity respectively after 6 cycles of reuse. For free tyrosinase, it was not possible to isolate the enzyme after each treatment.
degradation immobilized tyrosinase magnetic powder magnetization
An Yan Cheng Jiang Wen Xiufang Pi Pihui Yang Zhuoru
School of Chemical and Energy Engineering, South China University of Technology, Guangzhou, 510640, School of Chemical and Energy Engineering, South China University of Technology, Guangzhou, 510640,
国际会议
广州
英文
707-710
2006-11-08（万方平台首次上网日期，不代表论文的发表时间）