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Immobilization of aPleurotus ostreatusLaccase Mixture on Perlite and Its Application to Dye Decolourisation
Author(s) -
Cinzia Pezzella,
Maria Elena Russo,
Antonio Marzocchella,
Piero Salatino,
Giovanni Sannia
Publication year - 2014
Publication title -
biomed research international
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 126
eISSN - 2314-6141
pISSN - 2314-6133
DOI - 10.1155/2014/308613
Subject(s) - pleurotus ostreatus , laccase , perlite , chemistry , adsorption , chromatography , immobilized enzyme , nuclear chemistry , chemical engineering , materials science , organic chemistry , enzyme , food science , mushroom , composite material , engineering
In the present study, a crude laccase preparation from Pleurotus ostreatus was successfully immobilized on perlite, a cheap porous silica material, and tested for Remazol Brilliant Blue R (RBBR) decolourisation in a fluidized bed recycle reactor. Results showed that RBBR decolourisation is mainly due to enzyme action despite the occurrence of dye adsorption-related enzyme inhibition. Fine tuning of immobilization conditions allowed balancing the immobilization yield and the resulting rate of decolourisation, with the adsorption capacity of the solid biocatalyst. In the continuous lab scale reactor, a maximum conversion degree of 56.1% was achieved at reactor space-time of 4.2 h. Stability and catalytic parameters of the immobilized laccases were also assessed in comparison with the soluble counterparts, revealing an increase in stability, despite a reduction of the catalytic performances. Both effects are most likely ascribable to the occurrence of multipoint attachment phenomena.

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