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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  
dc.subject
HESPERIDIN METHYLCHALCONE  
dc.subject
METAL CATALYZED OXIDATION  
dc.subject
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