The extracellular GH11 β-1,4-xylanase (XylY) gene (633-bp) of Paenibacillus sp. strain KYJ-16 was molecularly cloned by repeated DNA walking and nested PCR method. The xylY gene was predicted to encode an extracellular protein consisting of 611 amino acids with a nesuced molecular mass of 23 kDa and a calculated pI of 9.55. Protein blast search revealed that the enzyme consisted of a putative catalytic domain, which is homologous to a catalytic GH11 domain. The highest sequence identity (92%) was obtained as the catalytic GH11 domain of XylY was compared to that of Paenibacillus sp. strain HGF5 (GenBank accession number: EGG35584) that has not yet been characterized. Enzymatic properties of the recombinant His-tagged enzyme (rXylY) overexpressed in E. coli BL21 harboring pET-28a(+)/xylY will be also presented.

• Yi-Joon Kim(Insect Biotech Co. Ltd.)
• Do Young Kim(Industrial Bio-materials Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB))
• Han-Young Cho(Industrial Bio-materials Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB))
• Dong-Ha Shin(Insect Biotech Co. Ltd.)
• Kwang-Hee Son(Industrial Bio-materials Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB))
• Ho-Yong Park(Industrial Bio-materials Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB))