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Immobilization of α-Amylase onto Luffa operculata Fibers

A commercial amylase (amy) was immobilized by adsorption onto Luffa operculata fibers (LOFs). The derivative LOF-amy presented capacity to hydrolyze starch continuously and repeatedly for over three weeks, preserving more than 80% of the initial activity. This system hydrolyzed more than 97% of star...

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Autores principales: Morais, Ricardo R., Pascoal, Aline M., Caramori, Samantha S., Lopes, Flavio M., Fernandes, Kátia F.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Hindawi Publishing Corporation 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3626310/
https://www.ncbi.nlm.nih.gov/pubmed/23606948
http://dx.doi.org/10.1155/2013/803415
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author Morais, Ricardo R.
Pascoal, Aline M.
Caramori, Samantha S.
Lopes, Flavio M.
Fernandes, Kátia F.
author_facet Morais, Ricardo R.
Pascoal, Aline M.
Caramori, Samantha S.
Lopes, Flavio M.
Fernandes, Kátia F.
author_sort Morais, Ricardo R.
collection PubMed
description A commercial amylase (amy) was immobilized by adsorption onto Luffa operculata fibers (LOFs). The derivative LOF-amy presented capacity to hydrolyze starch continuously and repeatedly for over three weeks, preserving more than 80% of the initial activity. This system hydrolyzed more than 97% of starch during 5 min, at room temperature. LOF-amy was capable to hydrolyze starch from different sources, such as maize (93.96%), wheat (85.24%), and cassava (79.03%). A semi-industrial scale reactor containing LOF-amy was prepared and showed the same yield of the laboratory-scale system. After five cycles of reuse, the LOF-amy reactor preserved over 80% of the initial amylase activity. Additionally, the LOF-amy was capable to operate as a kitchen grease trap component in a real situation during 30 days, preserving 30% of their initial amylase activity.
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spelling pubmed-36263102013-04-19 Immobilization of α-Amylase onto Luffa operculata Fibers Morais, Ricardo R. Pascoal, Aline M. Caramori, Samantha S. Lopes, Flavio M. Fernandes, Kátia F. Enzyme Res Research Article A commercial amylase (amy) was immobilized by adsorption onto Luffa operculata fibers (LOFs). The derivative LOF-amy presented capacity to hydrolyze starch continuously and repeatedly for over three weeks, preserving more than 80% of the initial activity. This system hydrolyzed more than 97% of starch during 5 min, at room temperature. LOF-amy was capable to hydrolyze starch from different sources, such as maize (93.96%), wheat (85.24%), and cassava (79.03%). A semi-industrial scale reactor containing LOF-amy was prepared and showed the same yield of the laboratory-scale system. After five cycles of reuse, the LOF-amy reactor preserved over 80% of the initial amylase activity. Additionally, the LOF-amy was capable to operate as a kitchen grease trap component in a real situation during 30 days, preserving 30% of their initial amylase activity. Hindawi Publishing Corporation 2013 2013-03-31 /pmc/articles/PMC3626310/ /pubmed/23606948 http://dx.doi.org/10.1155/2013/803415 Text en Copyright © 2013 Ricardo R. Morais et al. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Morais, Ricardo R.
Pascoal, Aline M.
Caramori, Samantha S.
Lopes, Flavio M.
Fernandes, Kátia F.
Immobilization of α-Amylase onto Luffa operculata Fibers
title Immobilization of α-Amylase onto Luffa operculata Fibers
title_full Immobilization of α-Amylase onto Luffa operculata Fibers
title_fullStr Immobilization of α-Amylase onto Luffa operculata Fibers
title_full_unstemmed Immobilization of α-Amylase onto Luffa operculata Fibers
title_short Immobilization of α-Amylase onto Luffa operculata Fibers
title_sort immobilization of α-amylase onto luffa operculata fibers
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3626310/
https://www.ncbi.nlm.nih.gov/pubmed/23606948
http://dx.doi.org/10.1155/2013/803415
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