Results 61 to 70 of about 1,854 (190)

Thermostability of β‐xylosidase from Aspergillus sydowii MG49 [PDF]

FEBS Letters, 1993
Heating of Aspergillus β‐xylosidase at 85°C ± 1°C and pH 5.5–6.0 (optimum for activity), causes irreversible, covalent thermoinactivation of the enzyme, involving oxidation of the thiol groups that are required for catalysis. Exogenous addition of cysteine, DTT, GSH and mercaptoethanol stabilizes the enzyme by extending its half‐life.
Ghosh, Mousumi, Nanda, Geeta
openaire   +2 more sources

Family 39 a-L-iduronidases and b-D-xylosidases react through similar glycosyl-enzyme intermediates: Identification of the human iduronidase nucleophile

, 2003
The inclusion of both beta-D-xylosidases and alpha-L-iduronidases within the same sequence-related family (family 39), despite the considerable difference in substrate structures and poor sequence conservation around the putative nucleophile, raises ...
Clarke, L., Hopwood, J., Withers, S., Nieman, C., Wong, A., He, S.   +5 more
core   +1 more source

Beta-xylosidase activity of a GH3 glucosidase/xylosidase from yak rumen metagenome promotes the enzymatic degradation of hemicellulosic xylans [PDF]

Letters in Applied Microbiology, 2011
  To characterize the duel activities of a glycosyl hydrolase family 3 β-glucosidase/xylosidase from rumen bacterial metagenome and to investigate the capabilities of its β-d-xylosidase activities for saccharification of hemicellulosic xylans.  A β-glucosidase/xylosidase gene RuBGX1 was cloned from yak (Bos grunniens) rumen using the metagenomic ...
J. Zhou, L. Bao, L. Chang, Z. Liu, C. You, H. Lu   +5 more
openaire   +2 more sources

Temporal Expression Dynamics of Plant Biomass-Degrading Enzymes by a Synthetic Bacterial Consortium Growing on Sugarcane Bagasse

Frontiers in Microbiology, 2018
Plant biomass (PB) is an important source of sugars useful for biofuel production, whose degradation efficiency depends on synergistic and dynamic interactions of different enzymes.
Diego Javier Jiménez, Diego Javier Jiménez, Maryam Chaib De Mares, Joana Falcão Salles   +3 more
doaj   +1 more source

Transcriptomic analysis reveals the hepatic response mechanisms of the Chinese spiny frog (Quasipaa spinosa) to Citrobacter freundii infection

Journal of the World Aquaculture Society, Volume 57, Issue 3, June 2026.
Abstract To elucidate the pathogen and host response mechanisms underlying mass mortality in Quasipaa spinosa, dominant bacteria were isolated from diseased individuals and identified as Citrobacter freundii by morphological, physiological, and biochemical characterization, 16S rRNA sequencing, and phylogenetic analysis.
Yanhong Li, Baohong Zhou, Yiran Lu, Yi Zang, Minghao Hu, Qiaochen Jin, Wenbin Fang, Shanjian Zheng   +7 more
wiley   +1 more source

Guardians or Gateways? The Intricate Relationship Between Plant Cell Walls and Pathogenic Xanthomonas

Molecular Plant Pathology, Volume 27, Issue 6, June 2026.
An overview of the intricate interactions between Xanthomonas and the plant cell wall during the infection process. ABSTRACT Plants have evolved a complex cell wall (CW) providing support and protection against environmental constraints, including constant attacks from pests and pathogens.
Charlotte Gaudin, Marie‐Agnès Jacques, Nicolas W. G. Chen   +2 more
wiley   +1 more source

Thermostable ?-xylosidase from Thermomonospora curvata

Journal of Industrial Microbiology and Biotechnology, 1998
produced a thermostable β-xylosidase during growth on birch xylan. The enzyme, extracted by sonication of early stationary phase mycelia, was purified by isoelectric focusing and size exclusion HPLC. The isoelectric point was pH 4.8. The molecular weight was estimated to be 102 000 by size exclusion HPLC and 112 000 by SDS-PAGE.
F Stutzenberger, A B Bodine
openaire   +1 more source

Cloning and Molecular Characterization of an Alpha-Glucosidase (MalH) from the Halophilic Archaeon Haloquadratum walsbyi

Life, 2017
We report the heterologous expression and molecular characterization of the first extremely halophilic alpha-glucosidase (EC 3.2.1.20) from the archaeon Haloquadratum walsbyi. A 2349 bp region (Hqrw_2071) from the Hqr.
Mara F. Cuebas-Irizarry, Ricardo A. Irizarry-Caro, Carol López-Morales, Keyla M. Badillo-Rivera, Carlos M. Rodríguez-Minguela, Rafael Montalvo-Rodríguez   +5 more
doaj   +1 more source

Safety evaluation of the food enzyme β‐glucosidase from the genetically modified Trichoderma reesei strain DP‐Nyk114

EFSA Journal, Volume 24, Issue 6, June 2026.
Abstract The food enzyme β‐glucosidase (β‐d‐glucoside glucohydrolase; EC 3.2.1.21) is produced with the genetically modified Trichoderma reesei strain DP‐Nyk114 by Genencor International B.V. The genetic modifications do not give rise to safety concerns. The food enzyme was considered free from viable cells of the production organism and its DNA. It is
EFSA Panel on Food Enzymes (FEZ), Holger Zorn, José Manuel Barat Baviera, Claudia Bolognesi, Francesco Catania, Gabriele Gadermaier, Ralf Greiner, Baltasar Mayo, Alicja Mortensen, Yrjö Henrik Roos, Marize L. M. Solano, Henk Van Loveren, Laurence Vernis, Ana Gomes, Magdalena Andryszkiewicz, Daniele Cavanna, Natália Kovalkovičová, Yi Liu   +17 more
wiley   +1 more source

Safety evaluation of the food enzyme containing endo‐1,3(4)‐β‐glucanase, endo‐1,4‐β‐xylanase and cellulase activities from the non‐genetically modified Rasamsonia emersonii strain FGB

EFSA Journal, Volume 24, Issue 6, June 2026.
Abstract The food enzyme containing endo‐1,3(4)‐β‐glucanase (3‐(1,3;1,4)‐β‐d‐glucan 3(4)‐glucanohydrolase; EC 3.2.1.6), endo‐1,4‐β‐xylanase (4‐β‐d‐xylan xylanohydrolase; EC 3.2.1.8) and cellulase (4‐(1,3;1,4)‐β‐d‐glucan‐4‐glucanohydrolase EC 3.2.1.4) is produced with the non‐genetically modified Rasamsonia emersonii strain FGB by DSM Food Specialties B.
EFSA Panel on Food Enzymes (FEZ), Holger Zorn, José Manuel Barat Baviera, Claudia Bolognesi, Francesco Catania, Gabriele Gadermaier, Ralf Greiner, Baltasar Mayo, Alicja Mortensen, Yrjö Henrik Roos, Marize L. M. Solano, Henk Van Loveren, Laurence Vernis, Cristina Andreoli, Andrea Terron, Simone Lunardi, Magdalena Andryzskiewicz, Ana Criado, Yi Liu   +18 more
wiley   +1 more source