Laccase enzymes: purification, structure to catalysis and tailoring

Laccases belong to the multicopper binding protein family that catalysis the reduction of oxygen molecule to produce water. These enzymes are glycosylated proteins and have been isolated and purified from fungi, bacteria, plant, insects and lichens. The variety of commercial and industrial applicati...

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Main Authors:	Moin, Syed Faraz, Omar, Muhammad Nor
Format:	Article
Language:	English English
Published:	Bentham Science Publishers 2014
Subjects:	Q Science (General)
Online Access:	http://irep.iium.edu.my/37445/ http://irep.iium.edu.my/37445/ http://irep.iium.edu.my/37445/ http://irep.iium.edu.my/37445/1/Moin_%26_Omar_PPL.pdf http://irep.iium.edu.my/37445/4/37445_Laccase%20enzymes_WoS.pdf

id	iium-37445
recordtype	eprints
spelling	iium-374452017-09-07T01:27:26Z http://irep.iium.edu.my/37445/ Laccase enzymes: purification, structure to catalysis and tailoring Moin, Syed Faraz Omar, Muhammad Nor Q Science (General) Laccases belong to the multicopper binding protein family that catalysis the reduction of oxygen molecule to produce water. These enzymes are glycosylated proteins and have been isolated and purified from fungi, bacteria, plant, insects and lichens. The variety of commercial and industrial application of laccases has attracted much attention towards the research addressing different aspects of the protein characterization, production and fit for purpose molecule. Here we briefly discuss the purification, catalytic mechanism in light of available understanding of structure-function relationship and the tailoring side of the protein, which has been the subject of recent research. Purification strategy of laccases is a method of choice and is facilitated by increased production of the enzyme. The structure-function relationship has given insights to unfold the catalytic mechanism. Site directed mutagenesis and other modification at C-terminal end or surrounding environment of copper centres have shown promising results to fit for purpose aspect, with a lot remains to be explored in glycosylation status and its alteration. Bentham Science Publishers 2014 Article PeerReviewed application/pdf en http://irep.iium.edu.my/37445/1/Moin_%26_Omar_PPL.pdf application/pdf en http://irep.iium.edu.my/37445/4/37445_Laccase%20enzymes_WoS.pdf Moin, Syed Faraz and Omar, Muhammad Nor (2014) Laccase enzymes: purification, structure to catalysis and tailoring. Protein and Peptide Letters, 21. pp. 707-713. ISSN 1875-5305 (O), 0929-8665 (P) http://www.eurekaselect.com/112767/article 10.2174/09298665113209990058
repository_type	Digital Repository
institution_category	Local University
institution	International Islamic University Malaysia
building	IIUM Repository
collection	Online Access
language	English English
topic	Q Science (General)
spellingShingle	Q Science (General) Moin, Syed Faraz Omar, Muhammad Nor Laccase enzymes: purification, structure to catalysis and tailoring
description	Laccases belong to the multicopper binding protein family that catalysis the reduction of oxygen molecule to produce water. These enzymes are glycosylated proteins and have been isolated and purified from fungi, bacteria, plant, insects and lichens. The variety of commercial and industrial application of laccases has attracted much attention towards the research addressing different aspects of the protein characterization, production and fit for purpose molecule. Here we briefly discuss the purification, catalytic mechanism in light of available understanding of structure-function relationship and the tailoring side of the protein, which has been the subject of recent research. Purification strategy of laccases is a method of choice and is facilitated by increased production of the enzyme. The structure-function relationship has given insights to unfold the catalytic mechanism. Site directed mutagenesis and other modification at C-terminal end or surrounding environment of copper centres have shown promising results to fit for purpose aspect, with a lot remains to be explored in glycosylation status and its alteration.
format	Article
author	Moin, Syed Faraz Omar, Muhammad Nor
author_facet	Moin, Syed Faraz Omar, Muhammad Nor
author_sort	Moin, Syed Faraz
title	Laccase enzymes: purification, structure to catalysis and tailoring
title_short	Laccase enzymes: purification, structure to catalysis and tailoring
title_full	Laccase enzymes: purification, structure to catalysis and tailoring
title_fullStr	Laccase enzymes: purification, structure to catalysis and tailoring
title_full_unstemmed	Laccase enzymes: purification, structure to catalysis and tailoring
title_sort	laccase enzymes: purification, structure to catalysis and tailoring
publisher	Bentham Science Publishers
publishDate	2014
url	http://irep.iium.edu.my/37445/ http://irep.iium.edu.my/37445/ http://irep.iium.edu.my/37445/ http://irep.iium.edu.my/37445/1/Moin_%26_Omar_PPL.pdf http://irep.iium.edu.my/37445/4/37445_Laccase%20enzymes_WoS.pdf
first_indexed	2023-09-18T20:53:43Z
last_indexed	2023-09-18T20:53:43Z
_version_	1777410164914126848

Laccase enzymes: purification, structure to catalysis and tailoring

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