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dc.contributor.author
Esparza Flores, Elí Emanuel
dc.contributor.author
Cardoso, Fernanda Dias
dc.contributor.author
Siquiera, Larisa Bertoldo
dc.contributor.author
Santagapita, Patricio Roman
dc.contributor.author
Hertz, Plinho F.
dc.contributor.author
Rodrigues, Rafael C.
dc.date.available
2024-02-27T15:35:26Z
dc.date.issued
2023-10
dc.identifier.citation
Esparza Flores, Elí Emanuel; Cardoso, Fernanda Dias; Siquiera, Larisa Bertoldo; Santagapita, Patricio Roman; Hertz, Plinho F.; et al.; Genipin crosslinked porous chitosan beads as robust supports for β-galactosidase immobilization: Characterization, stability, and bioprocessing potential; Elsevier Science; International Journal of Biological Macromolecules; 250; 126234; 10-2023; 1-12
dc.identifier.issn
0141-8130
dc.identifier.uri
http://hdl.handle.net/11336/228646
dc.description.abstract
This study aimed to modify the porosity of chitosan beads using Na2CO3 as a porogen agent and to crosslink them with genipin for the immobilization of β-galactosidase from Aspergillus oryzae. Immobilization was performed under four different pH conditions (4.5, 6.0, 7.5, and 9.0), resulting in biocatalysts named B4, B6, B7, and B9, respectively. The immobilized enzymes were characterized for immobilization parameters and stability, including thermal, pH, storage, and operational stability. The optimal conditions for the support were determined as 50 mM Na2CO3. The biocatalyst exhibited nearly 100 % retention of initial activity after 5 h of incubation at different pH conditions and showed improved thermal stability compared to the free enzyme across all pH conditions. After 50 cycles of lactose hydrolysis, all biocatalysts retained at least 71 % of their initial activity, with B6 retaining nearly 100 %. Scanning electron microscopy revealed structural modifications, particularly in B4, leading to weakened support structure after reuse. Continuous lactose hydrolysis showed increased productivity from 41.3 to 48.1 g L−1 h−1 for B6, with 78.1 % retention of initial capacity. All biocatalysts retained >95 % activity when stored at 4 °C for 20 weeks, highlighting their suitability for enzyme immobilization in continuous and discontinuous bioprocesses.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Elsevier Science
dc.rights
info:eu-repo/semantics/restrictedAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.subject
BATCH REACTOR
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CHITOSAN
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COLUMN REACTOR
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ENZYME IMMOBILIZATION
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GENIPIN
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Β-GALACTOSIDASE
dc.subject.classification
Físico-Química, Ciencia de los Polímeros, Electroquímica
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Ciencias Químicas
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CIENCIAS NATURALES Y EXACTAS
dc.title
Genipin crosslinked porous chitosan beads as robust supports for β-galactosidase immobilization: Characterization, stability, and bioprocessing potential
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2024-02-22T11:12:00Z
dc.journal.volume
250
dc.journal.number
126234
dc.journal.pagination
1-12
dc.journal.pais
Países Bajos
dc.journal.ciudad
Amsterdam
dc.description.fil
Fil: Esparza Flores, Elí Emanuel. Universidade Federal do Rio Grande do Sul; Brasil
dc.description.fil
Fil: Cardoso, Fernanda Dias. Universidade Federal do Rio Grande do Sul; Brasil
dc.description.fil
Fil: Siquiera, Larisa Bertoldo. Universidade Federal do Rio Grande do Sul; Brasil
dc.description.fil
Fil: Santagapita, Patricio Roman. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Orgánica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Centro de Investigaciones en Hidratos de Carbono. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Centro de Investigaciones en Hidratos de Carbono; Argentina
dc.description.fil
Fil: Hertz, Plinho F.. Universidade Federal do Rio Grande do Sul; Brasil
dc.description.fil
Fil: Rodrigues, Rafael C.. Universidade Federal do Rio Grande do Sul; Brasil
dc.journal.title
International Journal of Biological Macromolecules
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/abs/pii/S0141813023031306
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.ijbiomac.2023.126234
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