Recombinant endo-beta-1,4-xylanase from Penicillium canescens

• Published in: Biochemistry (Moscow) Vol. 68; no. 12; pp. 1313 - 1319
• Main Authors: Sinitsyna, O A, Gusakov, A V, Okunev, O N, Serebryany, V A, Vavilova, E A, Vinetsky, Yu P, Sinitsyn, A P
• Format: Journal Article
• Language: English
• Published: United States 01.12.2003
• Subjects: Absorption; Cellulose - metabolism; Chromatography; Endo-1,4-beta Xylanases - genetics; Endo-1,4-beta Xylanases - isolation & purification; Endo-1,4-beta Xylanases - metabolism; Enzyme Stability; Hydrogen-Ion Concentration; Penicillium - enzymology; Penicillium - genetics; Recombinant Proteins - genetics; Recombinant Proteins - isolation & purification; Recombinant Proteins - metabolism; Substrate Specificity; Temperature
• ISSN: 0006-2979; 1608-3040
• DOI: 10.1023/B:BIRY.0000011652.52741.d6

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.