title: Recombinant endo-beta-1,4-xylanase from Penicillium canescens.
abstract: Recombinant endo-beta-1,4-xylanase (Xyl-31rec, 31 kD, pI 8.2-9.3, the tenth family of glycosyl hydrolases) was isolated from the culture liquid of Penicillium canescens (strain with the amplified homologous xylanase gene) by chromatofocusing on Mono P and hydrophobic chromatography on phenyl-Superose. It is shown that the biochemical and kinetic parameters, substrate specificity, stability, and other properties of the recombinant and native enzymes are almost the same. It was found that Xyl-31rec can be used for biobleaching of cellulose, the recombinant P. canescens strains providing a high yield of extracellular Xyl-31rec (up to 800-900 U/ml of culture liquid) and not secreting cellulases.
authors.affiliation: Faculty of Chemistry, Lomonosov Moscow State University, Moscow 199899, Russia. oasinitsyna@enzyme.chem.msu.ru
authors.forename: O A
authors.initials: OA
authors.lastname: Sinitsyna
authors.forename: A V
authors.initials: AV
authors.lastname: Gusakov
authors.forename: O N
authors.initials: ON
authors.lastname: Okunev
authors.forename: V A
authors.initials: VA
authors.lastname: Serebryany
authors.forename: E A
authors.initials: EA
authors.lastname: Vavilova
authors.forename: Yu P
authors.initials: YP
authors.lastname: Vinetsky
authors.forename: A P
authors.initials: AP
authors.lastname: Sinitsyn
mesh_terms: D000042:Absorption; D002482:Cellulose / Q000378:metabolism; D002845:Chromatography; D043364:Endo-1,4-beta Xylanases / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism*; D004795:Enzyme Stability; D006863:Hydrogen-Ion Concentration; D010407:Penicillium / Q000201:enzymology* / Q000235:genetics; D011994:Recombinant Proteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D013379:Substrate Specificity; D013696:Temperature
chemical_list: D011994:Recombinant Proteins; D002482:Cellulose; D043364:Endo-1,4-beta Xylanases