Improvement of chloroperoxidase stability by covalent immobilization on chitosan membranes.
Chloroperoxidase (CPO) from Caldariomyces fumago was optimally covalently immobilized on chitosan membranes pretreated with 0.8 M glutaraldehyde at pH 3.5 to give 3.18 mg CPO g(-1) support. Using monochlorodimedone (MCD) as assay substrate, the immobilized-CPO retained 40% activity at 50 degrees C after 40 min whereas free CPO retained only 0.02%. The residual activity for immobilized-CPO was 99 and 58% compared with 68 and 43% for free CPO in the presence of 1.5 M urea and 300 microM H(2)O(2), respectively, after 20 h.
Zhang
Li-Hua
LH
School of Chemistry and Materials Science, Shaanxi Normal University, Chang'an South Road, 199, Xi'an, Shaanxi, 710062, People's Republic of China.
Bai
Chao-Hong
CH
Wang
Ying-Song
YS
Jiang
Yu-Cheng
YC
Hu
Man-Cheng
MC
Li
Shu-Ni
SN
Zhai
Quan-Guo
QG
D001203:Ascomycota / Q000201:enzymology*; D048271:Chitosan / Q000378:metabolism*; D002711:Chloride Peroxidase / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D003512:Cyclohexanones / Q000378:metabolism; D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000737:chemistry / Q000378:metabolism*; D006358:Hot Temperature; D008566:Membranes / Q000201:enzymology*; D013997:Time Factors
D003512:Cyclohexanones; D004800:Enzymes, Immobilized; C006991:chlorodimedone; D048271:Chitosan; D002711:Chloride Peroxidase