Please use this identifier to cite or link to this item: http://www.alice.cnptia.embrapa.br/alice/handle/doc/1187279
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dc.contributor.authorBERGMANN, J. C.
dc.contributor.authorLACERDA, V. A. M.
dc.contributor.authorALENCAR, K. L. C.
dc.contributor.authorFAVARO, L. C. de L.
dc.contributor.authorRODRIGUES, D. de S.
dc.contributor.authorMARINS, L. F.
dc.contributor.authorQUIRINO, B. F.
dc.date.accessioned2026-06-01T15:48:38Z-
dc.date.available2026-06-01T15:48:38Z-
dc.date.created2026-06-01
dc.date.issued2026
dc.identifier.citationACS Agricultural Science & Technology, 2026.
dc.identifier.urihttp://www.alice.cnptia.embrapa.br/alice/handle/doc/1187279-
dc.descriptionAbstract: β-Glucosidases catalyze the hydrolysis of β-glycosidic bonds and play key roles in biomass conversion and glycoside processing. We report the identification and characterization of Cr_B1, a GH3 β-glucosidase from Chryseobacterium sp. containing a predicted signal peptide. Cr_B1 hydrolyzed pNPG, cellobiose, salicin, and daidzin, showing optimal activity at pH 5.0−5.5 and 45−55 °C. The enzyme retained over 90% activity after 190 days at 4°C and 25 °C and above 80% activity after 24 h at 50 °C, indicating remarkable long-term and thermal stability. Cr_B1 exhibited high glucose tolerance (IC50: 1.5−1.8 M) and substrate-dependent kinetics. In synergy with Celluclast, it increased glucose release from CMC by 69%, demonstrating its potential to enhance enzymatic saccharification. These properties highlight Cr_B1 as a promising biocatalyst for improving saccharification, enhancing isoflavone bioavailability, and reducing bitterness in food and feed applications.
dc.language.isoeng
dc.rightsopenAccess
dc.titleA new GH3 B-Glucosidase from Chryseobacterium sp. with applications in cellulosic ethanol production and agri-biotechnological processes.
dc.typeArtigo de periódico
dc.subject.thesagroEnzima
dc.subject.thesagroHidrolise
dc.subject.thesagroGlicose
dc.subject.thesagroBiomassa
dc.subject.thesagroSacarificação
dc.subject.nalthesaurusBeta-glucosidase
dc.subject.nalthesaurusEnzyme kinetics
dc.subject.nalthesaurusHydrolysis
dc.subject.nalthesaurusGlucose tolerance
dc.subject.nalthesaurusBiomass
dc.subject.nalthesaurusSaccharification
dc.description.notesOn-line first.
riaa.ainfo.id1187279
riaa.ainfo.lastupdate2026-06-01
dc.identifier.doihttps://doi.org/10.1021/acsagscitech.5c01090
dc.contributor.institutionJESSICA CARVALHO BERGMANN; VALQUIRIA ALICE MICHALCZECHEN LACERDA; KAMILA LOURRANE CARVALHO ALENCAR; LEIA CECILIA DE LIMA FAVARO, CNPAE; DASCIANA DE SOUSA RODRIGUES, CNPAE; LUIS FERNANDO MARINS, UNIVERSIDADE FEDERAL DO RIO GRANDE; BETANIA FERRAZ QUIRINO, CNPAE.
Appears in Collections:Artigo em periódico indexado (CNPAE)

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