Covalent immobilization of laccase in green coconut fiber and use in clarification of apple juice

• Published in: Process biochemistry (1991) Vol. 50; no. 3; pp. 417 - 423
• Main Authors: Bezerra, Thaís Milena de Souza, Bassan, Juliana Cristina, Santos, Victor Tabosa de Oliveira, Ferraz, André, Monti, Rubens
• Format: Journal Article
• Language: English
• Published: Elsevier Ltd 01.03.2015
• Subjects: Apple juice; Coconut fiber; Enzyme immobilization; Laccase; Trametes versicolor; Coconut fiber; Enzyme immobilization; Apple juice; Trametes versicolor; Laccase
• ISSN: 1359-5113; 1873-3298
• DOI: 10.1016/j.procbio.2014.12.009

•A process for apple juice clarification is proposed using an immobilized laccase.•A low-cost support “coconut fiber” was used with success in the laccase immobilization.•The derivative showed better stability in relation to the free enzyme with possibility of reuse.•This immobilized enzyme can be used to remove phenol compounds from apple juice.•The enzyme can be removed from the final product because it is bound in a solid matrix. Waste materials from agroindustry constituted from lignocellulose have been used in the immobilization process of technological interest enzymes to reduce costs, increasing the value of such products. In the present study, green coconut husk was used to obtain fibers (CF) that were treated through thermal decompression in combination with either acid or alkaline medium. A solid support for enzyme immobilization was prepared using the pretreated CF activated with glyoxyl or glutaraldehyde and was used to immobilize the laccase enzyme (EC 1.10.3.2) produced by Trametes versicolor. Immobilized enzyme retained up to 59±1% of the initial activity and showed maximum immobilization profile of 98±1%. The thermal stability was higher when laccase was immobilized on alkaline pretreated support with increments of 6.8-fold (laccase-glutaraldehyde-FC) up to 16.5-fold (laccase-glyoxyl-FC) of the soluble enzyme. The laccase-glutaraldehyde-CF achieved excellent results in the clarification of apple juice, reducing 61±1% of the original juice color and 29±1% of its turbidity, retaining up to 100% of the initial activity after a 10-times reuse assay. This study is pioneer in the utilization of low-cost support for laccase immobilization with application in the juice fruits clarification.