نتایج جستجو برای: cellobiose dehydrogenase

تعداد نتایج: 72344  

2011
Mathieu Bey Jean-Guy Berrin Laetitia Poidevin Jean-Claude Sigoillot

BACKGROUND Cellobiose dehydrogenase (CDH) is an extracellular hemoflavoenzyme produced by lignocellulose-degrading fungi including Pycnoporus cinnabarinus. We investigated the cellulolytic system of P. cinnabarinus, focusing on the involvement of CDH in the deconstruction of lignocellulosic biomass. RESULTS First, P. cinnabarinus growth conditions were optimized for CDH production. Following ...

2015
Jin Seop Bak

Plant biomass can be utilized by a lignocellulose-degrading fungus, Phanerochaete chrysosporium, but the metabolic and regulatory mechanisms involved are not well understood. A polyomics-based analysis (metabolomics, proteomics, and transcriptomics) of P. chrysosporium has been carried out using statistically optimized conditions for lignocellulolytic reaction. Thirty-nine metabolites and 123 g...

Journal: :The Biochemical journal 1997
G Henriksson A Salumets C Divne G Pettersson

The binding isotherm to cellulose of cellobiose dehydrogenase (CDH) from Phanerochaete chrysosporium has been compared with that of cellobiohydrolase 1 (CBH 1) from Trichoderma reesei. CDH binds more strongly but more sparsely to cellulose than does CBH 1. In a classical Scatchard analysis, a better fit to a one-site binding model was obtained for CDH than for CBH 1. The binding of both enzymes...

Journal: :Monatshefte f�r Chemie 1901

2015
Tetiana Chudina Andrii Labyntsev Kyrylo Manoilov Denys Kolybo Serhiy Komisarenko

AIM To evaluate the dose-dependent immunogenic properties of poly(lactide-co-glycolide) (PLGA) particles coated with cellobiose as antigen carriers for oral immunization. METHODS Two types of PLGA-cellobiose particles (PLGA-cellobiose-1, ~ 0.8 μm and PLGA-cellobiose-2, ~ 1.2 μm) containing non-toxic recombinant subunit B (SbB) of diphtheria toxin fused with enhanced green fluorescent protein ...

Journal: :Biotechnology for Biofuels 2021

Abstract Background The cellulolytic thermophile Clostridium thermocellum is an important biocatalyst due to its ability solubilize lignocellulosic feedstocks without the need for pretreatment or exogenous enzyme addition. At low concentrations of substrate, C. can corn fiber > 95% in 5 days, but solubilization declines markedly at substrate higher than 20 g/L. This differs model cellulose l...

Journal: :Applied and environmental microbiology 2008
Dawn M Adin Karen L Visick Eric V Stabb

Cellobiose utilization is a variable trait that is often used to differentiate members of the family Vibrionaceae. We investigated how Vibrio fischeri ES114 utilizes cellobiose and found a cluster of genes required for growth on this beta-1,4-linked glucose disaccharide. This cluster includes genes annotated as a phosphotransferase system II (celA, celB, and celC), a glucokinase (celK), and a g...

Journal: :Journal of bacteriology 1961
J K ALEXANDER

The phosphorolysis of cellobiose was first demonstrated by Sih and McBee (1955a, b). These workers found that cellobiose phosphorylase was present in cell-free extracts of Clostridium thermocellum. Recently cellobiose phosphorylase has been reported from two other bacteria, Ruminococcus flavefaciens (Ayers, 1958, 1959), and Cellvibrio gilvus (Hulcher and King, 1958). This enzyme also catalyzes ...

Journal: :Acta crystallographica. Section F, Structural biology communications 2015
Li Chu Tsai Imamaddin Amiraslanov Hung Ren Chen Yun Wen Chen Hsiao Lin Lee Po Huang Liang Yen Chywan Liaw

Exoglucanase/cellobiohydrolase (EC 3.2.1.176) hydrolyzes a β-1,4-glycosidic bond from the reducing end of cellulose and releases cellobiose as the major product. Three complex crystal structures of the glycosyl hydrolase 48 (GH48) cellobiohydrolase S (ExgS) from Clostridium cellulovorans with cellobiose, cellotetraose and triethylene glycol molecules were solved. The product cellobiose occupies...

Journal: :Journal of bacteriology 1977
L K Nakamura D D Tyler

D-Aldohexopyranoside:cytochrome c oxidoreductase (ACO) was strongly induced by cellobiose, alpha-methylglucoside, beta-methylglucoside, kojibiose, and sophorose. Induction was rapid, and ACO was readily detectable within 10 min after addition of cellobiose as inducer. Although not measurable for 30 to 40 min after addition of inducer, once started, the rate of induction with alpha-methylglucosi...

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