The 1,4-β-D-glucan glucohydrolase gene (Ggh) which was isolated from Paenibacillus sp. strain HPL-001 (KCTC11365BP) has been cloned and expressed in Escherichia coli, and efficiently purified using affinity column chromatography. Recombinant 1,4-β-Dglucan glucohydrolase (719aa, NCBI accession number KJ573391) was highly active at 40°C in pH 6.0 without significant changes to most salts tested, and exhibited K m 0.893 mg/mL V max 33.33 U/mg on pNPG, respectively. All soluble cellooligomers

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... cellobiose, cellotriose, cellotetraose, cellopentaose, and cellohexaose) had been virtually hydrolyzed to glucose by this enzyme. When compared with the commercialized-enzymes, the hydrolytic pattern to all substrates was almost same to the Celluclast 1.5L with about 1/3 strength, however hydrolytic pattern of Glucosidase and Almonds was significantly decreased with substrates increasing number of glucose polymer from cellotriose to cellohexaose. About 90% of the initial enzyme activity was maintained even after 10 consecutive recycle by the 11-carbon bridge and aldehyde-functionalized MCF-immobilization. 3-D structure of this enzyme has the ligand of cellobiose and cellulose binding in the center of niche according to the sequence information. Keywords: 1,4-β-D-glucan glucohydrolase; Cellooligomer; Immobilization; Saccharification we immobilized this enzyme on aldehyde-, amine-, SH-, epoxyfunctionalized meso-structured cellular foam silica (MCF) for practical applications.