A thermo stable xylanase was purified from Streptomyces thermocyaneoviolaceus M049 for the production of xylooligosaccharides from xylan. The enzyme showed thermostability by maintaining 65% of remaining enzyme activity after 1 h heat treatment at $70^{circ}C$. The molecular weight of the purified protein was 35 kDa in SDS-PAGE, and the optimal pH and temperature for the enzymatic activity were pH 5.0 and $60^{circ}C$, respectively. N-terminal amino acid sequences of the purified xylanase, DTITSNQTGTHNGYF, were similar to StxII from S. thermoviolaceus and XlnB from S. lividans. Using those two genes, XlnB as probe DNA, a gene encoding xylanase, XlnB, was cloned from genomic library of S. thermocyaneoviolaceus M049. The open reading frame of the XlnB was composed of 1008 nucleotide sequences. Compared to N-terminal sequences from purified enzyme, it was proposed that the XynB contained a 40 amino acid long signal peptide to the N-terminus. For easy production and purification, a XynB overproduction strain was constructed using pET21a(+) and strain E. coli BLR(DE3). Consequently, the recombinant enzyme was tested for the production of xylooligosaccharides through TLC and HPLC analyses.