title: Purification and characterization of a family G/11 beta-xylanase from Streptomyces olivaceoviridis E-86.
abstract: A beta-xylanase (GXYN) was purified from the culture filtrate of Streptomyces olivaceoviridis E-86 by successive chromatography on DE-52, CM-Sepharose and Superose 12. The molecular mass of the xylanase was estimated to be 23 kDa, indicating that the enzyme consists of a catalytic domain only. The enzyme displayed an optimum pH of 6, a temperature optimum of 60 degrees C, a pH stability range from 2 to 11 and thermal stability up to 40 degrees C. The N-terminal amino acid sequence of GXYN was A-T-V-I-T-T-N-Q-T-G-T-N-N-G-I-Y-Y-S-F-W-, and sharing a high degree of similarity with the N-terminal sequence of xylanases B and C from Streptomyces lividans, indicating GXYN belongs to family G/11 of glycoside hydrolases. GXYN was inferior to xylanase B from Streptomyces lividans in the hydrolysis of insoluble xylan because of its lack of a xylan binding domain.
authors.affiliation: National Food Research Institute, Ministry of Agriculture, Forestry, and Fisheries, Ibaraki, Japan. sakaneko@nfri.affrc.go.jp
authors.forename: S
authors.initials: S
authors.lastname: Kaneko
authors.forename: A
authors.initials: A
authors.lastname: Kuno
authors.forename: M
authors.initials: M
authors.lastname: Muramatsu
authors.forename: S
authors.initials: S
authors.lastname: Iwamatsu
authors.forename: I
authors.initials: I
authors.lastname: Kusakabe
authors.forename: K
authors.initials: K
authors.lastname: Hayashi
mesh_terms: D000595:Amino Acid Sequence; D001483:Base Sequence; D002853:Chromatography, Liquid; D004269:DNA, Bacterial; D004591:Electrophoresis, Polyacrylamide Gel; D008969:Molecular Sequence Data; D017386:Sequence Homology, Amino Acid; D013302:Streptomyces / Q000201:enzymology*; D043325:Xylan Endo-1,3-beta-Xylosidase; D014995:Xylosidases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism
chemical_list: D004269:DNA, Bacterial; D014995:Xylosidases; D043325:Xylan Endo-1,3-beta-Xylosidase