Recent developments and applications of immobilized laccase.
Identifieur interne : 000442 ( Main/Exploration ); précédent : 000441; suivant : 000443Recent developments and applications of immobilized laccase.
Auteurs : RBID : pubmed:22398306Abstract
Laccase is a promising biocatalyst with many possible applications, including bioremediation, chemical synthesis, biobleaching of paper pulp, biosensing, textile finishing and wine stabilization. The immobilization of enzymes offers several improvements for enzyme applications because the storage and operational stabilities are frequently enhanced. Moreover, the reusability of immobilized enzymes represents a great advantage compared with free enzymes. In this work, we discuss the different methodologies of enzyme immobilization that have been reported for laccases, such as adsorption, entrapment, encapsulation, covalent binding and self-immobilization. The applications of laccase immobilized by the aforementioned methodologies are presented, paying special attention to recent approaches regarding environmental applications and electrobiochemistry.
DOI: 10.1016/j.biotechadv.2012.02.013
PubMed: 22398306
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The immobilization of enzymes offers several improvements for enzyme applications because the storage and operational stabilities are frequently enhanced. Moreover, the reusability of immobilized enzymes represents a great advantage compared with free enzymes. In this work, we discuss the different methodologies of enzyme immobilization that have been reported for laccases, such as adsorption, entrapment, encapsulation, covalent binding and self-immobilization. The applications of laccase immobilized by the aforementioned methodologies are presented, paying special attention to recent approaches regarding environmental applications and electrobiochemistry.</div></front></TEI><pubmed><MedlineCitation Owner="NLM" Status="In-Process"><PMID Version="1">22398306</PMID><DateCreated><Year>2013</Year><Month>11</Month><Day>25</Day></DateCreated><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1873-1899</ISSN><JournalIssue CitedMedium="Internet"><Volume>31</Volume><Issue>8</Issue><PubDate><Year>2013</Year><Month>Dec</Month></PubDate></JournalIssue><Title>Biotechnology advances</Title><ISOAbbreviation>Biotechnol. Adv.</ISOAbbreviation></Journal><ArticleTitle>Recent developments and applications of immobilized laccase.</ArticleTitle><Pagination><MedlinePgn>1808-25</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.biotechadv.2012.02.013</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S0734-9750(12)00064-X</ELocationID><Abstract><AbstractText>Laccase is a promising biocatalyst with many possible applications, including bioremediation, chemical synthesis, biobleaching of paper pulp, biosensing, textile finishing and wine stabilization. The immobilization of enzymes offers several improvements for enzyme applications because the storage and operational stabilities are frequently enhanced. Moreover, the reusability of immobilized enzymes represents a great advantage compared with free enzymes. In this work, we discuss the different methodologies of enzyme immobilization that have been reported for laccases, such as adsorption, entrapment, encapsulation, covalent binding and self-immobilization. The applications of laccase immobilized by the aforementioned methodologies are presented, paying special attention to recent approaches regarding environmental applications and electrobiochemistry.</AbstractText><CopyrightInformation>Copyright © 2012 Elsevier Inc. 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