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Oriented covalent immobilization of esterase BioH on hydrophilic‐modified Fe 3 O 4 nanoparticles
Author(s) -
Li Rongrong,
Jiang Ling,
Ye Lidan,
Lu Jie,
Yu Hongwei
Publication year - 2014
Publication title -
biotechnology and applied biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 70
eISSN - 1470-8744
pISSN - 0885-4513
DOI - 10.1002/bab.1211
Subject(s) - esterase , covalent bond , chemistry , immobilized enzyme , azide , surface modification , chemical modification , enzyme , combinatorial chemistry , organic chemistry , polymer chemistry
The esterase BioH from Escherichia coli was covalently immobilized onto the surface of the functional magnetic nanosupport in an oriented manner. The surface of the Fe 3 O 4 nanosupport was modified with acyl azide groups or both acyl azide groups and hydroxyl groups. The protein loading of the support was increased from 55 to 99 mg/g by an improvement in hydrophilicity, and the activity retention of the immobilized esterase on the nanosupport was improved by 40% after hydrophilic modification (30% and 70% of the free BioH , respectively). For the BioH immobilized on the hydrophilic‐modified nanosupport, the recovery activity remained 80% of the original activity after 10 times of recycling. The catalytic kinetics and thermo‐/pH‐stability of the immobilized esterase BioH were also determined and compared with those of the free enzyme. The comparatively high activity retention, improved thermo‐/ pH ‐stability, and good reusability of the immobilized enzyme indicate that oriented covalent immobilization is an efficient method for immobilizing esterase BioH .