Facile, high efficiency immobilization of lipase enzyme on magnetic iron oxide nanoparticles via a biomimetic coating

<p>Abstract</p> <p>Background</p> <p>Immobilization of lipase on appropriate solid supports is one way to improve their stability and activity, and can be reused for large scale applications. A sample, cost- effective and high loading capacity method is still challengin...

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Main Authors: He Lihong, Rivera Jose G, Ren Yuhong, Kulkarni Harsha, Lee Dong-Keun, Messersmith Phillip B
Format: Article
Language:English
Published: BMC 2011-06-01
Series:BMC Biotechnology
Online Access:http://www.biomedcentral.com/1472-6750/11/63
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spelling doaj-92ea21ab4aa9479ab71286f7c349513e2020-11-25T03:41:51ZengBMCBMC Biotechnology1472-67502011-06-011116310.1186/1472-6750-11-63Facile, high efficiency immobilization of lipase enzyme on magnetic iron oxide nanoparticles via a biomimetic coatingHe LihongRivera Jose GRen YuhongKulkarni HarshaLee Dong-KeunMessersmith Phillip B<p>Abstract</p> <p>Background</p> <p>Immobilization of lipase on appropriate solid supports is one way to improve their stability and activity, and can be reused for large scale applications. A sample, cost- effective and high loading capacity method is still challenging.</p> <p>Results</p> <p>A facile method of lipase immobilization was developed in this study, by the use of polydopamine coated magnetic nanoparticles (PD-MNPs). Under optimal conditions, 73.9% of the available lipase was immobilized on PD-MNPs, yielding a lipase loading capacity as high as 429 mg/g. Enzyme assays revealed that lipase immobilized on PD-MNPs displayed enhanced pH and thermal stability compared to free lipase. Furthermore, lipase immobilized on PD-MNPs was easily isolated from the reaction medium by magnetic separation and retained more than 70% of initial activity after 21 repeated cycles of enzyme reaction followed by magnetic separation.</p> <p>Conclusions</p> <p>Immobilization of enzyme onto magnetic iron oxide nanoparticles via poly-dopamine film is economical, facile and efficient.</p> http://www.biomedcentral.com/1472-6750/11/63
collection DOAJ
language English
format Article
sources DOAJ
author He Lihong
Rivera Jose G
Ren Yuhong
Kulkarni Harsha
Lee Dong-Keun
Messersmith Phillip B
spellingShingle He Lihong
Rivera Jose G
Ren Yuhong
Kulkarni Harsha
Lee Dong-Keun
Messersmith Phillip B
Facile, high efficiency immobilization of lipase enzyme on magnetic iron oxide nanoparticles via a biomimetic coating
BMC Biotechnology
author_facet He Lihong
Rivera Jose G
Ren Yuhong
Kulkarni Harsha
Lee Dong-Keun
Messersmith Phillip B
author_sort He Lihong
title Facile, high efficiency immobilization of lipase enzyme on magnetic iron oxide nanoparticles via a biomimetic coating
title_short Facile, high efficiency immobilization of lipase enzyme on magnetic iron oxide nanoparticles via a biomimetic coating
title_full Facile, high efficiency immobilization of lipase enzyme on magnetic iron oxide nanoparticles via a biomimetic coating
title_fullStr Facile, high efficiency immobilization of lipase enzyme on magnetic iron oxide nanoparticles via a biomimetic coating
title_full_unstemmed Facile, high efficiency immobilization of lipase enzyme on magnetic iron oxide nanoparticles via a biomimetic coating
title_sort facile, high efficiency immobilization of lipase enzyme on magnetic iron oxide nanoparticles via a biomimetic coating
publisher BMC
series BMC Biotechnology
issn 1472-6750
publishDate 2011-06-01
description <p>Abstract</p> <p>Background</p> <p>Immobilization of lipase on appropriate solid supports is one way to improve their stability and activity, and can be reused for large scale applications. A sample, cost- effective and high loading capacity method is still challenging.</p> <p>Results</p> <p>A facile method of lipase immobilization was developed in this study, by the use of polydopamine coated magnetic nanoparticles (PD-MNPs). Under optimal conditions, 73.9% of the available lipase was immobilized on PD-MNPs, yielding a lipase loading capacity as high as 429 mg/g. Enzyme assays revealed that lipase immobilized on PD-MNPs displayed enhanced pH and thermal stability compared to free lipase. Furthermore, lipase immobilized on PD-MNPs was easily isolated from the reaction medium by magnetic separation and retained more than 70% of initial activity after 21 repeated cycles of enzyme reaction followed by magnetic separation.</p> <p>Conclusions</p> <p>Immobilization of enzyme onto magnetic iron oxide nanoparticles via poly-dopamine film is economical, facile and efficient.</p>
url http://www.biomedcentral.com/1472-6750/11/63
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