Premium
Composite Magnetic Particles as Carriers for Laccase from Trametes versicolor
Author(s) -
Pich Andrij,
Bhattacharya Sanchita,
Adler HansJuergen P.,
Wage Tobias,
Taubenberger Anna,
Li Zheng,
van Pee KarlHeinz,
Böhmer Ulrike,
Bley Thomas
Publication year - 2006
Publication title -
macromolecular bioscience
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.924
H-Index - 105
eISSN - 1616-5195
pISSN - 1616-5187
DOI - 10.1002/mabi.200500192
Subject(s) - laccase , maghemite , chemistry , trametes versicolor , polystyrene , chemical engineering , immobilized enzyme , particle (ecology) , composite number , colloid , particle size , magnetic nanoparticles , chromatography , enzyme , nanoparticle , organic chemistry , polymer , materials science , mineralogy , composite material , hematite , oceanography , engineering , geology
Summary: In this paper we report a study of laccase immobilisation on different kinds of carrier particles. The immobilisation of enzyme on the particle surface with respect to the immobilisation efficiency and the properties of the immobilised enzymes is discussed. The immobilisation of laccase on polystyrene particles bearing reactive β ‐diketone groups is characterised by high efficiency, but grafting of the enzyme increases the stability of the colloidal system, which makes the separation/purification procedure difficult. Additionally, the extreme colloidal stability of the immobilisates hinders the application of such particles with immobilised enzymes in some applications where the recycling of the enzyme should be performed. It has been found that hybrid PS‐AAEM particles equipped with maghemite show similar immobilisation efficiency to that of their analogues without maghemite and can additionally be manipulated in magnetic fields. The activity of the immobilised laccase is much higher in the pH region 5–7 and the temperature range 50–70 °C as compared with that of the free enzyme. Immobilised enzymes also exhibit much better storage stability.SEM images of PS‐AAEM particles before (a) and after (b) laccase immobilisation.