Mostrar el registro sencillo del ítem
dc.contributor.author
Aguirre, Andres
dc.contributor.author
Eberhardt, Maria Florencia
dc.contributor.author
Hails, Guillermo
dc.contributor.author
Cerminati, Sebastián
dc.contributor.author
Castelli, Maria Eugenia
dc.contributor.author
Rasia, Rodolfo Maximiliano
dc.contributor.author
Paoletti, Luciana Elisa
dc.contributor.author
Menzella, Hugo Gabriel
dc.contributor.author
Peirú, Salvador
dc.date.available
2019-11-25T13:23:59Z
dc.date.issued
2018-03
dc.identifier.citation
Aguirre, Andres; Eberhardt, Maria Florencia; Hails, Guillermo; Cerminati, Sebastián; Castelli, Maria Eugenia; et al.; The production, properties, and applications of thermostable steryl glucosidases; Springer; World Journal of Microbiology; 34; 3; 3-2018; 39-45
dc.identifier.issn
0959-3993
dc.identifier.uri
http://hdl.handle.net/11336/89644
dc.description.abstract
Extremophilic microorganisms are a rich source of enzymes, the enzymes which can serve as industrial catalysts that can withstand harsh processing conditions. An example is thermostable β-glucosidases that are addressing a challenging problem in the biodiesel industry: removing steryl glucosides (SGs) from biodiesel. Steryl glucosidases (SGases) must be tolerant to heat and solvents in order to function efficiently in biodiesel. The amphipathic nature of SGs also requires enzymes with an affinity for water/solvent interfaces in order to achieve efficient hydrolysis. Additionally, the development of an enzymatic process involving a commodity such as soybean biodiesel must be cost-effective, necessitating an efficient manufacturing process for SGases. This review summarizes the identification of microbial SGases and their applications, discusses biodiesel refining processes and the development of analytical methods for identifying and quantifying SGs in foods and biodiesel, and considers technologies for strain engineering and process optimization for the heterologous production of a SGase from Thermococcus litoralis. All of these technologies might be used for the production of other thermostable enzymes. Structural features of SGases and the feasibility of protein engineering for novel applications are explored.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Springer
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
BIOFUELS
dc.subject
EXTREMOZYMES
dc.subject
STERYL GLUCOSIDASES
dc.subject.classification
Otros Tópicos Biológicos
dc.subject.classification
Ciencias Biológicas
dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
dc.title
The production, properties, and applications of thermostable steryl glucosidases
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2019-10-15T17:28:20Z
dc.journal.volume
34
dc.journal.number
3
dc.journal.pagination
39-45
dc.journal.pais
Alemania
dc.description.fil
Fil: Aguirre, Andres. Keclon S.a. Tucuman 7180; Argentina. Universidad Nacional de Rosario; Argentina
dc.description.fil
Fil: Eberhardt, Maria Florencia. Universidad Nacional de Rosario; Argentina
dc.description.fil
Fil: Hails, Guillermo. Universidad Nacional de Rosario; Argentina
dc.description.fil
Fil: Cerminati, Sebastián. Universidad Nacional de Rosario; Argentina
dc.description.fil
Fil: Castelli, Maria Eugenia. Universidad Nacional de Rosario; Argentina
dc.description.fil
Fil: Rasia, Rodolfo Maximiliano. Universidad Nacional de Rosario; Argentina
dc.description.fil
Fil: Paoletti, Luciana Elisa. Universidad Nacional de Rosario; Argentina
dc.description.fil
Fil: Menzella, Hugo Gabriel. Universidad Nacional de Rosario; Argentina. Keclon S.a. Tucuman 7180; Argentina
dc.description.fil
Fil: Peirú, Salvador. Keclon S.a. Tucuman 7180; Argentina. Universidad Nacional de Rosario; Argentina
dc.journal.title
World Journal of Microbiology
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://link.springer.com/10.1007/s11274-018-2423-x
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1007/s11274-018-2423-x
Archivos asociados