dc.creator | Moreno Amador, María de Lourdes | es |
dc.creator | Pérez Gómez, Dolores | es |
dc.creator | García Gutiérrez, María Teresa | es |
dc.creator | Mellado Durán, María Encarnación | es |
dc.date.accessioned | 2016-10-04T12:55:17Z | |
dc.date.available | 2016-10-04T12:55:17Z | |
dc.date.issued | 2013 | |
dc.identifier.citation | Moreno, L., Pérez, D., García Gutiérrez, M.T. y Mellado Durán, M.E. (2013). Halophilic Bacteria as a source of novel hydrolytic enzymes. Life, 3, 38-51. | |
dc.identifier.issn | 075-1729 | es |
dc.identifier.uri | http://hdl.handle.net/11441/46925 | |
dc.description.abstract | Hydrolases constitute a class of enzymes widely distributed in nature from
bacteria to higher eukaryotes. The halotolerance of many enzymes derived from halophilic
bacteria can be exploited wherever enzymatic transformations are required to function
under physical and chemical conditions, such as in the presence of organic solvents and
extremes in temperature and salt content. In recent years, different screening programs
have been performed in saline habitats in order to isolate and characterize novel enzymatic
activities with different properties to those of conventional enzymes. Several halophilic
hydrolases have been described, including amylases, lipases and proteases, and then used
for biotechnological applications. Moreover, the discovery of biopolymer-degrading
enzymes offers a new solution for the treatment of oilfield waste, where high temperature
and salinity are typically found, while providing valuable information about heterotrophic
processes in saline environments. In this work, we describe the results obtained in different
screening programs specially focused on the diversity of halophiles showing hydrolytic
activities in saline and hypersaline habitats, including the description of enzymes with
special biochemical properties. The intracellular lipolytic enzyme LipBL, produced by the
moderately halophilic bacterium Marinobacter lipolyticus, showed advantages over other
lipases, being an enzyme active over a wide range of pH values and temperatures. The
immobilized LipBL derivatives obtained and tested in regio- and enantioselective
reactions, showed an excellent behavior in the production of free polyunsaturated fatty
acids (PUFAs). On the other hand, the extremely halophilic bacterium, Salicola marasensis sp.
IC10 showing lipase and protease activities, was studied for its ability to produce
promising enzymes in terms of its resistance to temperature and salinity | es |
dc.format | application/pdf | es |
dc.language.iso | eng | es |
dc.publisher | MDPI | es |
dc.relation.ispartof | Life, 3, 38-51. | |
dc.rights | Attribution-NonCommercial-NoDerivatives 4.0 Internacional | * |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/4.0/ | * |
dc.subject | Halophiles | es |
dc.subject | Extremophiles | es |
dc.subject | Hydrolases | es |
dc.subject | Saline environments | es |
dc.title | Halophilic Bacteria as a source of novel hydrolytic enzymes | es |
dc.type | info:eu-repo/semantics/article | es |
dcterms.identifier | https://ror.org/03yxnpp24 | |
dc.type.version | info:eu-repo/semantics/publishedVersion | es |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | es |
dc.contributor.affiliation | Universidad de Sevilla. Departamento de Microbiología y Parasitología | es |
dc.relation.publisherversion | 10.3390/life3010038 | es |
dc.identifier.doi | 10.3390/life3010038 | es |
idus.format.extent | 14 p. | es |
dc.journaltitle | Life | es |
dc.publication.volumen | 3 | es |
dc.publication.initialPage | 38 | es |
dc.publication.endPage | 51 | es |
dc.identifier.idus | https://idus.us.es/xmlui/handle/11441/46925 | |