Purification and characterization of a family G/11 beta-xylanase from Streptomyces olivaceoviridis E-86.
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.
Kaneko
S
S
National Food Research Institute, Ministry of Agriculture, Forestry, and Fisheries, Ibaraki, Japan. sakaneko@nfri.affrc.go.jp
Kuno
A
A
Muramatsu
M
M
Iwamatsu
S
S
Kusakabe
I
I
Hayashi
K
K
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
D004269:DNA, Bacterial; D014995:Xylosidases; D043325:Xylan Endo-1,3-beta-Xylosidase