Improved immobilization of laccase on a glassy carbon electrode by oriented covalent attachment | Zendy

Xin Liu | Zendy; Liu Ke-wu | Zendy

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Improved immobilization of laccase on a glassy carbon electrode by oriented covalent attachment

Author(s) -

Xin Liu,

Liu Ke-wu

Publication year - 2014

Publication title -

archives of biological sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.217

H-Index - 25

eISSN - 1821-4339

pISSN - 0354-4664

DOI - 10.2298/abs1403975l

Subject(s) - laccase , thermus thermophilus , biosensor , electrode , immobilized enzyme , covalent bond , glassy carbon , chemistry , cyclic voltammetry , materials science , nuclear chemistry , chemical engineering , electrochemistry , enzyme , organic chemistry , biochemistry , escherichia coli , engineering , gene

A laccase from Thermus thermophilus HB27 was reported to be potentially useful in the design of a temperature controlled biofuel cell. For enhancing its application in different thermal conditions, we engineered a laccase-oriented immobilized electrode. A site-directed mutant N323C of the laccase was constructed. A photometric assay was employed in order to compare the catalytic properties of wild-type laccase and mutant. The mutant was attached to a glass carbon electrode by covalent cross-linking. The electrochemical properties of the immobilized laccase were investigated by cyclic voltammetry. This immobilization allowed the active electrode to function at temperatures up to 95°C. The thermal and pH dependence profiles were similar to those of the soluble enzyme investigated by spectrophotometry

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