Nomenclature Abstract for Cellvibrio japonicus Humphry et al. 2003.

2003 ◽  
Author(s):  
Charles Thomas Parker ◽  
George M Garrity
Keyword(s):  
Cellvibrio Japonicus

scholarly journals The modular architecture of Cellvibrio japonicus mannanases in glycoside hydrolase families 5 and 26 points to differences in their role in mannan degradation

2003 ◽  
Vol 371 (3) ◽  
pp. 1027-1043 ◽  
Author(s):  
Deborah HOGG ◽  
Gavin PELL ◽  
Paul DUPREE ◽  
Florence GOUBET ◽  
Susana M. MARTÍN-ORÚE ◽  
...  
Keyword(s):  
Glycoside Hydrolase ◽  
Plant Cell Wall ◽  
Catalytic Domain ◽  
Glycoside Hydrolases ◽  
Crystalline Cellulose ◽  
Carbohydrate Binding ◽  
Molecular Architecture ◽  
Catalytic Domains ◽  
Carbohydrate Binding Modules ◽  
Cellvibrio Japonicus

β-1,4-Mannanases (mannanases), which hydrolyse mannans and glucomannans, are located in glycoside hydrolase families (GHs) 5 and 26. To investigate whether there are fundamental differences in the molecular architecture and biochemical properties of GH5 and GH26 mannanases, four genes encoding these enzymes were isolated from Cellvibrio japonicus and the encoded glycoside hydrolases were characterized. The four genes, man5A, man5B, man5C and man26B, encode the mannanases Man5A, Man5B, Man5C and Man26B, respectively. Man26B consists of an N-terminal signal peptide linked via an extended serine-rich region to a GH26 catalytic domain. Man5A, Man5B and Man5C contain GH5 catalytic domains and non-catalytic carbohydrate-binding modules (CBMs) belonging to families 2a, 5 and 10; Man5C in addition contains a module defined as X4 of unknown function. The family 10 and 2a CBMs bound to crystalline cellulose and ivory nut crystalline mannan, displaying very similar properties to the corresponding family 10 and 2a CBMs from Cellvibrio cellulases and xylanases. CBM5 bound weakly to these crystalline polysaccharides. The catalytic domains of Man5A, Man5B and Man26B hydrolysed galactomannan and glucomannan, but displayed no activity against crystalline mannan or cellulosic substrates. Although Man5C was less active against glucomannan and galactomannan than the other mannanases, it did attack crystalline ivory nut mannan. All the enzymes exhibited classic endo-activity producing a mixture of oligosaccharides during the initial phase of the reaction, although their mode of action against manno-oligosaccharides and glucomannan indicated differences in the topology of the respective substrate-binding sites. This report points to a different role for GH5 and GH26 mannanases from C. japonicus. We propose that as the GH5 enzymes contain CBMs that bind crystalline polysaccharides, these enzymes are likely to target mannans that are integral to the plant cell wall, while GH26 mannanases, which lack CBMs and rapidly release mannose from polysaccharides and oligosaccharides, target the storage polysaccharide galactomannan and manno-oligosaccharides.

scholarly journals Complete Genome Sequences of Cellvibrio japonicus Strains with Improved Growth When Using α-Diglucosides

2019 ◽  
Vol 8 (44) ◽  
Author(s):  
Cecelia A. Garcia ◽  
Jackson A. Narrett ◽  
Jeffrey G. Gardner
Keyword(s):  
Complete Genome ◽  
Growth Characteristics ◽  
Metabolic Flexibility ◽  
Genome Sequences ◽  
Additional Insight ◽  
Content Type ◽  
Carbohydrate Degradation ◽  
Cellvibrio Japonicus ◽  
Insight Into

Cellvibrio japonicus is a saprophytic bacterium that has been studied for its substantial carbohydrate degradation capability. We announce the genome sequences of three strains with improved growth characteristics when utilizing α-diglucosides. These data provide additional insight into the metabolic flexibility of a biotechnologically relevant bacterium.

scholarly journals Enzyme-Catalyzed Production of Potato Galactan-Oligosaccharides and Its Optimization by Response Surface Methodology

Materials ◽  
2019 ◽  
Vol 12 (9) ◽  
pp. 1465 ◽  
Author(s):  
Mirian Angelene González-Ayón ◽  
Ángel Licea-Claveríe ◽  
José Benigno Valdez-Torres ◽  
Lorenzo A. Picos-Corrales ◽  
Rosabel Vélez-de la Rocha ◽  
...  
Keyword(s):  
Response Surface Methodology ◽  
Response Surface ◽  
Degree Of Polymerization ◽  
Enzyme Substrate ◽  
Low Degree ◽  
Ft Ir ◽  
Cellvibrio Japonicus ◽  
Substrate Ratio ◽  
Optimized Conditions ◽  
Hydrolysis Of

This work shows an optimized enzymatic hydrolysis of high molecular weight potato galactan yielding pectic galactan-oligosaccharides (PGOs), where endo-β-1,4-galactanase (galactanase) from Cellvibrio japonicus and Clostridium thermocellum was used. For this, response surface methodology (RSM) by central composite design (CCD) was applied. The parameters varied were temperature (°C), pH, incubation time (min), and enzyme/substrate ratio (U/mg). The optimized conditions for the production of low degree of polymerization (DP) PGOs were obtained for each enzyme by spectrophotometric assay and confirmed by chromatography. The optimal conditions predicted for the use of C. japonicus galactanase to obtain PGOs of DP = 2 were T = 51.8 °C, pH 5, E/S = 0.508 U/mg, and t = 77.5 min. For DP = 3, they were T = 21 °C, pH 9, E/S = 0.484 U/mg, and t = 12.5 min; and for DP = 4, they were T = 21 °C, pH 5, E/S = 0.462 U/mg, and t = 12.5 min. The efficiency results were 51.3% for substrate hydrolysis. C. thermocellum galactanase had a lower yield (35.7%) and optimized conditions predicted for PGOs of DP = 2 were T = 60 °C, pH 5, E/S = 0.525 U/mg, and time = 148 min; DP = 3 were T = 59.7 °C, pH 5, E/S = 0.506 U/mg, and time = 12.5 min; and DP = 4, were T = 34.5 °C, pH 11, E/S = 0.525 U/mg, and time = 222.5 min. Fourier transformed infrared (FT-IR) and nuclear magnetic resonance (NMR) characterizations of PGOs are presented.

scholarly journals Requirement of the Type II Secretion System for Utilization of Cellulosic Substrates by Cellvibrio japonicus

2010 ◽  
Vol 76 (15) ◽  
pp. 5079-5087 ◽  
Author(s):  
Jeffrey G. Gardner ◽  
David H. Keating
Keyword(s):  
Secretion System ◽  
Biofuel Production ◽  
Growth Defect ◽  
Cellulolytic Bacterium ◽  
Type Ii Secretion ◽  
Type Ii ◽  
Wild Type ◽  
Gram Negative ◽  
Type Ii Secretion System ◽  
Cellvibrio Japonicus

ABSTRACT Cellulosic biofuels represent a powerful alternative to petroleum but are currently limited by the inefficiencies of the conversion process. While Gram-positive and fungal organisms have been widely explored as sources of cellulases and hemicellulases for biomass degradation, Gram-negative organisms have received less experimental attention. We investigated the ability of Cellvibrio japonicus, a recently sequenced Gram-negative cellulolytic bacterium, to degrade bioenergy-related feedstocks. Using a newly developed biomass medium, we showed that C. japonicus is able to utilize corn stover and switchgrass as sole sources of carbon and energy for growth. We also developed tools for directed gene disruptions in C. japonicus and used this system to construct a mutant in the gspD gene, which is predicted to encode a component of the type II secretion system. The gspD::pJGG1 mutant displayed a greater-than-2-fold decrease in endoglucanase secretion compared to wild- type C. japonicus. In addition, the mutant strain showed a pronounced growth defect in medium with biomass as a carbon source, yielding 100-fold fewer viable cells than the wild type. To test the potential of C. japonicus to undergo metabolic engineering, we constructed a strain able to produce small amounts of ethanol from biomass. Collectively, these data suggest that C. japonicus is a useful platform for biomass conversion and biofuel production.

scholarly journals C-type cytochrome-initiated reduction of bacterial lytic polysaccharide monooxygenases.

2021 ◽  
Author(s):  
Jessie Branch ◽  
Badri S Rajagopal ◽  
Alessandro Paradisi ◽  
Nick Yates ◽  
Peter J Lindley ◽  
...  
Keyword(s):  
Cellulose Degradation ◽  
H2o2 Production ◽  
Electron Sources ◽  
Lytic Polysaccharide Monooxygenases ◽  
Energy Needs ◽  
Polysaccharide Monooxygenases ◽  
Cellvibrio Japonicus ◽  
New Research ◽  
The Impact ◽  
Insight Into

The release of glucose from lignocellulosic waste for subsequent fermentation into biofuels holds promise for securing humankind's future energy needs. The discovery of a set of copper dependent enzymes known as lytic polysaccharide monooxygenases (LPMOs) has galvanized new research in this area. LPMOs act by oxidatively introducing chain breaks into cellulose and other polysaccharides, boosting the ability of cellulases to act on the substrate. Although several proteins have been implicated as electron sources in fungal LPMO biochemistry, no equivalent bacterial LPMO electron donors have been previously identified, although the proteins Cbp2D and E from Cellvibrio japonicus have been implicated as potential candidates. Here we analyze a small c-type cytochrome (CjX183) present in Cellvibrio japonicus Cbp2D, and show that it can initiate bacterial CuII/I LPMO reduction and also activate LPMO-catalyzed cellulose-degradation. In the absence of cellulose, CjX183-driven reduction of the LPMO results in less H2O2 production from O2, and correspondingly less oxidative damage to the enzyme than when ascorbate is used as the reducing agent. Significantly, using CjX183 as the activator maintained similar cellulase boosting levels relative to the use of an equivalent amount of ascorbate. Our results therefore add further evidence to the impact that the choice of electron source can have on LPMO action. Furthermore, the study of Cbp2D and other similar proteins may yet reveal new insight into the redox processes governing polysaccharide degradation in bacteria.

scholarly journals Insights into Plant Cell Wall Degradation from the Genome Sequence of the Soil Bacterium Cellvibrio japonicus

2008 ◽  
Vol 190 (15) ◽  
pp. 5455-5463 ◽  
Author(s):  
Robert T. DeBoy ◽  
Emmanuel F. Mongodin ◽  
Derrick E. Fouts ◽  
Louise E. Tailford ◽  
Hoda Khouri ◽  
...  
Keyword(s):  
Cell Wall ◽  
Plant Cell ◽  
Plant Cell Wall ◽  
Hydrolytic Enzymes ◽  
Soil Bacterium ◽  
Glycoside Hydrolases ◽  
Carbohydrate Binding ◽  
Carbohydrate Binding Modules ◽  
Cellvibrio Japonicus ◽  
And Storage

ABSTRACT The plant cell wall, which consists of a highly complex array of interconnecting polysaccharides, is the most abundant source of organic carbon in the biosphere. Microorganisms that degrade the plant cell wall synthesize an extensive portfolio of hydrolytic enzymes that display highly complex molecular architectures. To unravel the intricate repertoire of plant cell wall-degrading enzymes synthesized by the saprophytic soil bacterium Cellvibrio japonicus, we sequenced and analyzed its genome, which predicts that the bacterium contains the complete repertoire of enzymes required to degrade plant cell wall and storage polysaccharides. Approximately one-third of these putative proteins (57) are predicted to contain carbohydrate binding modules derived from 13 of the 49 known families. Sequence analysis reveals approximately 130 predicted glycoside hydrolases that target the major structural and storage plant polysaccharides. In common with that of the colonic prokaryote Bacteroides thetaiotaomicron, the genome of C. japonicus is predicted to encode a large number of GH43 enzymes, suggesting that the extensive arabinose decorations appended to pectins and xylans may represent a major nutrient source, not just for intestinal bacteria but also for microorganisms that occupy terrestrial ecosystems. The results presented here predict that C. japonicus possesses an extensive range of glycoside hydrolases, lyases, and esterases. Most importantly, the genome of C. japonicus is remarkably similar to that of the gram-negative marine bacterium, Saccharophagus degradans 2-40T. Approximately 50% of the predicted C. japonicus plant-degradative apparatus appears to be shared with S. degradans, consistent with the utilization of plant-derived complex carbohydrates as a major substrate by both organisms.

Cellvibrio japonicus α-L-arabinanase 43A has a novel five-blade β-propeller fold

2002 ◽  
Vol 9 (9) ◽  
pp. 665-668 ◽  
Author(s):  
Didier Nurizzo ◽  
Johan P. Turkenburg ◽  
Simon J. Charnock ◽  
Shirley M. Roberts ◽  
Eleanor J. Dodson ◽  
...  
Keyword(s):  
Cellvibrio Japonicus
Sign in / Sign up

Export Citation Format

Share Document