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molecular cloning and characterization of a multidomain endoglucanase from paenibacillus sp bp-23: evaluation of its performance in pulp refining.the gene celb encoding an endoglucanase from paenibacillus sp. bp-23 was cloned and expressed in escherichia coli. the nucleotide sequence of a 4161 bp dna fragment containing the celb gene was determined, revealing an open reading frame of 2991 nucleotides that encodes a protein of 106,927 da. comparison of the deduced amino acid sequence of endoglucanase b with known beta-glycanase sequences showed that the encoded enzyme is a modular protein and exhibits high homology to enzymes belonging to ...200111234960
paenibacillus barcinonensis sp. nov., a xylanase-producing bacterium isolated from a rice field in the ebro river delta.a gram-positive, endospore-forming, xylanase-producing bacterium isolated from a rice field was studied taxonomically. the strain grows at 10-40 degrees c and in the presence of lysozyme or 5 % (w/v) nacl. chemotaxonomic analysis revealed that mk-7 was the predominant menaquinone of the isolated strain, while the major fatty acid was anteiso-c(15 : 0). comparison of 16s rrna gene sequences showed that strain bp-23(t) fell within the radiation of the cluster comprising paenibacillus species. the ...200515774688
pectate lyase c from bacillus subtilis: a novel endo-cleaving enzyme with activity on highly methylated pectin.the gene yvpa from bacillus subtilis was cloned and expressed in escherichia coli. it encoded a pectate lyase of 221 amino acids that was denominated pelc. the heterologously expressed enzyme was purified by his-tag affinity chromatography and characterized. pelc depolymerized polygalacturonate and pectins of methyl esterification degree from 22 % to 89 %, exhibiting maximum activity on 22 % esterified citrus pectin. it showed an absolute ca2+ requirement and the optimum temperature and ph were ...200616514142
paenibacillus provencensis sp. nov., isolated from human cerebrospinal fluid, and paenibacillus urinalis sp. nov., isolated from human urine.gram-negative, spore-forming rods were isolated from a human urine sample (strain 5402403(t)) and a human cerebrospinal fluid sample (strain 4401170(t)). based on genotypic characteristics, these strains belonged to the genus paenibacillus and were closely related. phylogenetic analysis based on 16s rrna gene sequence comparison showed that they clustered with paenibacillus massiliensis 2301065(t) (95.9 and 94.3 % 16s rrna gene sequence similarity, respectively, for strains 5402403(t) and 440117 ...200818319478
paenibacillus taichungensis sp. nov., from soil in taiwan.among a large collection of taiwanese soil isolates, a novel gram-variable, rod-shaped, motile, endospore-forming bacterial strain, strain v10537(t), was subjected to a polyphasic study including 16s rrna and gyrb gene sequence analysis, dna-dna hybridization experiments, cell wall peptidoglycan type, cellular fatty acid composition analysis and comparative phenotypic characterization. 16s rrna gene sequence analysis indicated that the organism belonged to the genus paenibacillus. strain v10537( ...200818984707
use of cellulases and recombinant cellulose binding domains for refining tcf kraft pulp.the modular endoglucanase cel9b from paenibacillus barcinonensis is a highly efficient biocatalyst, which expedites pulp refining and reduces the associated energy costs as a result. in this work, we set out to identify the specific structural domain or domains responsible for the action of this enzyme on cellulose fibre surfaces with a view to facilitating the development of new cellulases for optimum biorefining. using the recombinant enzymes gh9-cbd3c, fn3-cbd3b, and cbd3b, which are truncate ...201020730755
recombinant expression of an alkali stable gh10 xylanase from paenibacillus barcinonensis.xylanase a from paenibacillus barcinonensis, a new species isolated from a rice field, has been cloned and expressed in escherichia coli. purified recombinant xylanase showed high activity on xylans from hardwoods and cereals, and exhibited k(m) and v(max) of 2.93 mg/ml and 50.67 u/mg on birchwood xylan. xylanase a was highly active at 60 degrees c in alkaline ph values up to 9.5 and remained stable for at least 3 h in alkaline conditions. the amino acid sequence deduced from xyna revealed that ...201020218604
engineering a family 9 processive endoglucanase from paenibacillus barcinonensis displaying a novel architecture.cel9b from paenibacillus barcinonensis is a modular endoglucanase with a novel molecular architecture among family 9 enzymes that comprises a catalytic domain (gh9), a family 3c cellulose-binding domain (cbm3c), a fibronectin iii-like domain repeat (fn3(1,2)), and a c-terminal family 3b cellulose-binding domain (cbm3b). a series of truncated derivatives of endoglucanase cel9b have been constructed and characterized. deletion of cbm3c produced a notable reduction in hydrolytic activity, while it ...201019957081
structural insights into the specificity of xyn10b from paenibacillus barcinonensis and its improved stability by forced protein evolution.paenibacillus barcinonensis is a soil bacterium bearing a complex set of enzymes for xylan degradation, including several secreted enzymes and xyn10b, one of the few intracellular xylanases reported to date. the crystal structure of xyn10b has been determined by x-ray analysis. the enzyme folds into the typical (beta/alpha)(8) barrel of family 10 glycosyl hydrolases (gh10), with additional secondary structure elements within the beta/alpha motifs. one of these loops -l7- located at the beta7 c t ...201019940147
efficient expression of a paenibacillus barcinonensis endoglucanase in saccharomyces cerevisiae.the endoglucanase coded by cela (genbank access no. y12512) from paenibacillus barcinonensis, an enzyme with good characteristics for application on paper manufacture from agricultural fibers, was expressed in saccharomyces cerevisiae by using different domains of the cell wall protein pir4 as translational fusion partners, to achieve either secretion or cell wall retention of the recombinant enzyme. given the presence of five potential n-glycosylation sites in the amino acid sequence coded by c ...201121701899
modular glucuronoxylan-specific xylanase with a family cbm35 carbohydrate-binding module.xyn30d from the xylanolytic strain paenibacillus barcinonensis has been identified and characterized. the enzyme shows a modular structure comprising a catalytic module family 30 (gh30) and a carbohydrate-binding module family 35 (cbm35). like gh30 xylanases, recombinant xyn30d efficiently hydrolyzed glucuronoxylans and methyl-glucuronic acid branched xylooligosaccharides but showed no catalytic activity on arabinose-substituted xylans. kinetic parameters of xyn30d were determined on beechwood x ...201222447606
purification and characterization of a thermophilic cellulase from a novel cellulolytic strain, paenibacillus barcinonensis.a novel bacterial strain, mg7, with high cellulase activity was isolated and identified by morphological characteristics and molecular phylogeny analysis as paenibacillus barcinonensis. maximum production of cellulase by mg7 was observed at ph 7.0 and 35°c. the enzyme was purified with a specific activity of 16.88 u/mg, the cellulase activity was observed in a zymogram, and its molecular mass (58.6 kda) was confirmed by sds-page. the purified enzyme showed maximum activity at ph 6.0 and 65°c and ...201223124341
paenibacillus oceanisediminis sp. nov. isolated from marine sediment.a gram-stain-negative, non-motile, aerobic, endospore forming and rod-shaped bacterium, designated strain l10(t), was isolated from marine sediment collected from the south korean coast. the organism grew optimally under conditions of 30 °c, 1 % (w/v) nacl and ph 6.0. it was oxidase-negative and catalase-positive. phylogenetic analysis based on 16s rrna gene sequences indicated that strain l10(t) was associated with the genus paenibacillus and most closely related to paenibacillus barcinonensis ...201322467156
the influence of supramolecular structure of cellulose allomorphs on the interactions with cellulose-binding domain, cbd3b from paenibacillus barcinonensis.the interaction of recombinant cellulose-binding domains (cbds) of endoglucanase cel9b from paenibacillus barcinonensis with different cotton cellulose allomorphs (i, ii and iii) has been investigated, in order to bring new insights regarding the cbd adsorption and desorption processes. the highest cbd adsorption capacity was recorded for cellulose i, confirming the affinity of proteins to the most crystalline substrate. the weakening and splitting of the hydrogen bonds within cellulose structur ...201424525243
crystallization and preliminary x-ray diffraction analysis of xyn30d from paenibacillus barcinonensis.xyn30d, a new member of a recently identified group of xylanases, has been purified and crystallized. xyn30d is a bimodular enzyme composed of an n-terminal catalytic domain belonging to glycoside hydrolase family 30 (gh30) and a c-terminal family 35 carbohydrate-binding domain (cbm35) able to bind xylans and glucuronic acid. xyn30d shares the characteristic endo mode of action described for gh30 xylanases, with the hydrolysis of the β-(1,4) bonds of xylan being directed by α-1,2-linked glucuron ...201425005099
xyn11e from paenibacillus barcinonensis bp-23: a lppx-chaperone-dependent xylanase with potential for upgrading paper pulps.a new xylanase from paenibacillus barcinonensis bp-23, xyn11e, has been identified and characterized. xyn11e has been cloned and heterologously expressed in escherichia coli. it is a single-domain xylanase belonging to the family 11 of glycosyl hydrolases (gh11) with a predicted molecular weight of 20.652 kda and an isoelectric point (pi) of 8.7. substrate specificity, kinetic properties, and mode of action of the purified xylanase were characterized. xyn11e exhibited high activity toward branch ...201424549767
unusual carboxylesterase bearing a ggg(a)x-type oxyanion hole discovered in paenibacillus barcinonensis bp-23.strain paenibacillus barcinonensis bp-23, previously isolated from ebro's river delta (spain), bears a complex hydrolytic system showing the presence of at least two enzymes with activity on lipidic substrates. esta, a cell-bound b-type carboxylesterase from the strain was previously isolated and characterized. the gene coding for a second putative lipase, located upstream cellulase cel5a, was obtained using a genome walking strategy and cloned in escherichia coli for further characterization. t ...201424929101
isolation and characterization of a novel thermostable β-glucosidase from bacillus subtilis su40.a new bacterial strain su40 with ability to produce thermostable β-glucosidase was isolated from soil located at puducherry (india) and identified as bacillus subtilis. the conditions like temperature, ph, carbon and nitrogen sources were optimized conditions for the maximum production of β-glucosidase. the enzyme was purified using ammonium sulphate precipitation and biosep and hplc chromatography. purified enzyme was found to be a monomeric protein with an apparent molecular mass of 38.3 kda. ...201525842900
crystallization and preliminary x-ray diffraction analysis of the n-terminal domain of paenibacillus barcinonensis xylanase 10c containing the cbm22-1-cbm22-2 tandem.a construct containing the cbm22-1-cbm22-2 tandem forming the n-terminal domain of paenibacillus barcinonensis xylanase 10c (xyn10c) has been purified and crystallized. a xylan-binding function and an affinity for mixed β-1,3/β-1,4 glucans have previously been demonstrated for some members of the cbm22 family. the sequence of the tandem is homologous to the n-terminal domains found in several thermophilic enzymes. crystals of this tandem were grown by the streak-seeding method after a long optim ...201525664784
exploring multimodularity in plant cell wall deconstruction: structural and functional analysis of xyn10c containing the cbm22-1-cbm22-2 tandem.elucidating the molecular mechanisms regulating multimodularity is a challenging task. paenibacillus barcinonensis xyn10c is a 120-kda modular enzyme that presents the cbm22/gh10/cbm9 architecture found in a subset of large xylanases. we report here the three-dimensional structure of the xyn10c n-terminal region, containing the xylan-binding cbm22-1-cbm22-2 tandem (xyn10c-xbd), which represents the first solved crystal structure of two contiguous cbm22 modules. xyn10c-xbd is folded into two sepa ...201526001782
paenibacillus puernese sp. nov., a β-glucosidase-producing bacterium isolated from pu'er tea.a gram-staining-positive, endospore-forming, aerobic, rod-shaped bacterium, designated as dcy97(t), was isolated from ripened pu'er tea and was identified by using a polyphasic approach. 16s rrna gene sequence analysis showed that strain dcy97(t) was closely related to paenibacillus dongdonensis kudc0114(t) (98.0 %), paenibacillus oceanisediminis l10(t) (97.7 %), and paenibacillus barcinonensis bp-23(t) (97.2 %). the phenotypic and chemotaxonomic characteristics of strain dcy97(t) matched with t ...201626721586
the glycoside hydrolase family 8 reducing-end xylose-releasing exo-oligoxylanase rex8a from paenibacillus barcinonensis bp-23 is active on branched xylooligosaccharides.a gh8 family enzyme involved in xylan depolymerization has been characterized. the enzyme, rex8a, is a reducing-end xylose-releasing exo-oligoxylanase (rex) that efficiently hydrolyzes xylooligosaccharides and shows minor activity on polymeric xylan. rex8a hydrolyzes xylooligomers of 3 to 6 xylose units to xylose and xylobiose in long-term incubations. kinetic constants of rex8a were determined on xylotriose, showing a km of 1.64 ± 0.03 mm and a kcat value of 118.8 s(-1) besides linear xylooligo ...201627316951
new gh16 β-glucanase from paenibacillus barcinonensis bp-23 releases a complex pattern of mixed-linkage oligomers from barley glucan.the gene coding for a lichenase from paenibacillus barcinonensis bp-23, a powerful carbohydrate-degrading strain, was obtained using a genome walking strategy and expressed in escherichia coli for further characterization. the amino acid sequence deduced from lic16a revealed that the lichenase is a single-domain enzyme belonging to the gh16 family. purified recombinant lic16a showed exclusive activity on β-1,3-1,4-glucans, showing a km of 16.88 mg/ml and a vmax of 266.09 u/mg using lichenan as a ...201625603884
a newly discovered arabinoxylan-specific arabinofuranohydrolase. synergistic action with xylanases from different glycosyl hydrolase families.arabinofuranosidase abf43a from bacillussp. bp-7 i s a newly discovered arabinoxylan arabinofuranohydrolase (axh). it is a modular enzyme comprised of a gh43 catalytic domain and a carbohydrate-binding module of family cbm6. recombinant abf43a showed high activity on arabinoxylans, being rye arabinoxylan the preferred substrate on which the purified enzyme exhibited a km of 10.6 ± 3.3 mg/ml and a vmax of 29.2 ± 3.4 u/mg. thin-layer chromatography analysis of hydrolysis products showed arabinose ...201626481625
paenibacillus silvae sp. nov., isolated from tropical rainforest soil.two gram-stain-positive, facultatively aerobic, endospore-forming and rod-shaped bacteria, designated db13031t and db13311, were isolated from soil of jiaxi nature reserve in hainan, china. 16s rrna gene analysis of the strains db13031t and db13311 showed that they were within the paenibacillus cluster, with the highest similarities of paenibacillus cucumis ap-115t (98.4 % and 98.3 %, respectively), paenibacillus barcinonensis bp-23t (98.3 % and 98.2 %, respectively) and paenibacillus oceanisedi ...201627902310
paenibacillus cucumis sp. nov. isolated from a cucumber plant.a gram-positive staining, aerobic, endospore-forming bacterial strain, isolated from a stem of a cucumber plant was studied in detail for its taxonomic position. based on 16s rrna gene sequence similarity comparisons, strain ap-115t was grouped into the genus paenibacillus, most closely related to paenibacillus amylolyticus (98.8%), paenibacillus tundrae and paenibacillus barcinonensis (both 98.4%). the 16s rrna gene sequence similarity to other paenibacillus species was ≤ 98.3%. chemotaxonomic ...201627089462
a bacterial gh6 cellobiohydrolase with a novel modular structure.cel6d from paenibacillus barcinonensis is a modular cellobiohydrolase with a novel molecular architecture among glycosyl hydrolases of family 6. it contains an n-terminal catalytic domain (family 6 of glycosyl hydrolases (gh6)), followed by a fibronectin iii-like domain repeat (fn31,2) and a c-terminal family 3b cellulose-binding domain (cbm3b). the enzyme has been identified and purified showing catalytic activity on cellulosic substrates and cellodextrins, with a marked preference for phosphor ...201728120014
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