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dc.contributor.author
Piñuel, Maria Lucrecia
dc.contributor.author
Mazzaferro, Laura
dc.contributor.author
Breccia, Javier Dario
dc.date.available
2023-03-17T10:18:17Z
dc.date.issued
2011-09
dc.identifier.citation
Piñuel, Maria Lucrecia; Mazzaferro, Laura; Breccia, Javier Dario; Operational stabilization of fungal α-rhamnosyl-β-glucosidase by immobilization on chitosan composites; Elsevier; Process Biochemistry; 46; 12; 9-2011; 2330-2335
dc.identifier.issn
1359-5113
dc.identifier.uri
http://hdl.handle.net/11336/190843
dc.description.abstract
The diglycosidase α-rhamnosyl-β-glucosidase from Acremonium sp. DSM24697 was immobilized by adsorption and cross-linking. The supports screened included beads of chitosan composites (gelatin, arabic gum, silica gel), epoxy-activated agarose and chitosan, and macroporous polyvinyl-alcohol cryogel. The chitosan-silica gel beads were selected because of the highest immobilization efficiency obtained and their morphological properties (diameter 1.67 ± 0.99 mm, circularity 0.81 ± 0.05). The optimization of the immobilization - coating with polyethyleneimine, changes in the enzyme load - improved the immobilization efficiency up to 18%. The practical use of the enzyme deals with low water solubility substrates. The higher KM for the immobilized enzyme - 8 mM vs. 1.8 mM hesperidin for the free enzyme - indicated that substrate diffusion limits the enzymatic reaction. The solvent dimethylsulfoxide (50%, v/v) was added in order to increase the substrate solubility, and 80% activity was retained (1 h, 60 °C) in contrast with the complete inactivation of the free form. The stability of the immobilized catalyst was extended to metal catalyzed oxidation where the enzyme was fully preserved in harsh conditions such as 1 mM CuSO4 at 60 °C during 1 h.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Elsevier
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
DIMETHYLSULFOXIDE
dc.subject
GLYCOSIDE HYDROLASE
dc.subject
HESPERIDIN
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HESPERIDIN METHYLCHALCONE
dc.subject
METAL CATALYZED OXIDATION
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POLYETHYLENEIMINE
dc.subject
RUTINOSE
dc.subject.classification
Bioprocesamiento Tecnológico, Biocatálisis, Fermentación
dc.subject.classification
Biotecnología Industrial
dc.subject.classification
INGENIERÍAS Y TECNOLOGÍAS
dc.title
Operational stabilization of fungal α-rhamnosyl-β-glucosidase by immobilization on chitosan composites
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2023-03-05T15:33:52Z
dc.journal.volume
46
dc.journal.number
12
dc.journal.pagination
2330-2335
dc.journal.pais
Países Bajos
dc.journal.ciudad
Amsterdam
dc.description.fil
Fil: Piñuel, Maria Lucrecia. Universidad Nacional de La Pampa; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Ciencias de la Tierra y Ambientales de La Pampa. Universidad Nacional de La Pampa. Facultad de Ciencias Exactas y Naturales. Instituto de Ciencias de la Tierra y Ambientales de La Pampa; Argentina
dc.description.fil
Fil: Mazzaferro, Laura. Universidad Nacional de La Pampa; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Ciencias de la Tierra y Ambientales de La Pampa. Universidad Nacional de La Pampa. Facultad de Ciencias Exactas y Naturales. Instituto de Ciencias de la Tierra y Ambientales de La Pampa; Argentina
dc.description.fil
Fil: Breccia, Javier Dario. Universidad Nacional de La Pampa; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Ciencias de la Tierra y Ambientales de La Pampa. Universidad Nacional de La Pampa. Facultad de Ciencias Exactas y Naturales. Instituto de Ciencias de la Tierra y Ambientales de La Pampa; Argentina
dc.journal.title
Process Biochemistry
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.procbio.2011.09.014
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/abs/pii/S1359511311003242
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