Title:	A new GH3 B-Glucosidase from Chryseobacterium sp. with applications in cellulosic ethanol production and agri-biotechnological processes.
Authors:	BERGMANN, J. C. LACERDA, V. A. M. ALENCAR, K. L. C. FAVARO, L. C. de L. RODRIGUES, D. de S. MARINS, L. F. QUIRINO, B. F.
Affiliation:	JESSICA 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.
Date Issued:	2026
Citation:	ACS Agricultural Science & Technology, 2026.
Description:	Abstract: 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.
Thesagro:	Enzima Hidrolise Glicose Biomassa Sacarificação
NAL Thesaurus:	Beta-glucosidase Enzyme kinetics Hydrolysis Glucose tolerance Biomass Saccharification
DOI:	https://doi.org/10.1021/acsagscitech.5c01090
Notes:	On-line first.
Type of Material:	Artigo de periódico
Access:	openAccess
Appears in Collections:	Artigo em periódico indexado (CNPAE)