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Agarase: Review of Major Sources, Categories, Purification Method, Enzyme Characteristics and Applications
Agarases are the enzymes which catalyze the hydrolysis of agar. They are classified into α-agarase (E.C. 3.2.1.158) and β-agarase (E.C. 3.2.1.81) according to the cleavage pattern. Several agarases have been isolated from different genera of bacteria found in seawater and marine sediments, as well a...
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Formato: | Texto |
Lenguaje: | English |
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Molecular Diversity Preservation International
2010
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2817930/ https://www.ncbi.nlm.nih.gov/pubmed/20161978 http://dx.doi.org/10.3390/md8010200 |
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author | Fu, Xiao Ting Kim, Sang Moo |
author_facet | Fu, Xiao Ting Kim, Sang Moo |
author_sort | Fu, Xiao Ting |
collection | PubMed |
description | Agarases are the enzymes which catalyze the hydrolysis of agar. They are classified into α-agarase (E.C. 3.2.1.158) and β-agarase (E.C. 3.2.1.81) according to the cleavage pattern. Several agarases have been isolated from different genera of bacteria found in seawater and marine sediments, as well as engineered microorganisms. Agarases have wide applications in food industry, cosmetics, and medical fields because they produce oligosaccharides with remarkable activities. They are also used as a tool enzyme for biological, physiological, and cytological studies. The paper reviews the category, source, purification method, major characteristics, and application fields of these native and gene cloned agarases in the past, present, and future. |
format | Text |
id | pubmed-2817930 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | Molecular Diversity Preservation International |
record_format | MEDLINE/PubMed |
spelling | pubmed-28179302010-02-16 Agarase: Review of Major Sources, Categories, Purification Method, Enzyme Characteristics and Applications Fu, Xiao Ting Kim, Sang Moo Mar Drugs Review Agarases are the enzymes which catalyze the hydrolysis of agar. They are classified into α-agarase (E.C. 3.2.1.158) and β-agarase (E.C. 3.2.1.81) according to the cleavage pattern. Several agarases have been isolated from different genera of bacteria found in seawater and marine sediments, as well as engineered microorganisms. Agarases have wide applications in food industry, cosmetics, and medical fields because they produce oligosaccharides with remarkable activities. They are also used as a tool enzyme for biological, physiological, and cytological studies. The paper reviews the category, source, purification method, major characteristics, and application fields of these native and gene cloned agarases in the past, present, and future. Molecular Diversity Preservation International 2010-01-26 /pmc/articles/PMC2817930/ /pubmed/20161978 http://dx.doi.org/10.3390/md8010200 Text en © 2010 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland http://creativecommons.org/licenses/by/3.0 This article is an open-access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/). |
spellingShingle | Review Fu, Xiao Ting Kim, Sang Moo Agarase: Review of Major Sources, Categories, Purification Method, Enzyme Characteristics and Applications |
title | Agarase: Review of Major Sources, Categories, Purification Method, Enzyme Characteristics and Applications |
title_full | Agarase: Review of Major Sources, Categories, Purification Method, Enzyme Characteristics and Applications |
title_fullStr | Agarase: Review of Major Sources, Categories, Purification Method, Enzyme Characteristics and Applications |
title_full_unstemmed | Agarase: Review of Major Sources, Categories, Purification Method, Enzyme Characteristics and Applications |
title_short | Agarase: Review of Major Sources, Categories, Purification Method, Enzyme Characteristics and Applications |
title_sort | agarase: review of major sources, categories, purification method, enzyme characteristics and applications |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2817930/ https://www.ncbi.nlm.nih.gov/pubmed/20161978 http://dx.doi.org/10.3390/md8010200 |
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