원문정보
초록
영어
A new β-1,4-D-glucosidase gene which was isolated from Paenibacillus sp. strain HPL-001 (KCTC11365BP) has been cloned and expressed in Escherichia coli. The molecular weight was 79 kDa upon SDS-PAGE analysis and consisted of 2,160 nucleotides, encoding a polypeptide of 719 amino acid residues. This gene exhibited 68% identity (DNA) to the previously reported glycoside hydrolase family 3 domain protein (GB: ZP_07902992.1), belonging to the glyco-hydro-3 superfamily, glyco-hydro-3-C superfamily and BglX multi-domain. Hydrolysis of the substrate, cellobiose to glucose by this enzyme was confirmed by HPLC analysis. The enzyme was then immobilized on aldehyde-, amine-, SH-, epoxy- functionalized meso-structured cellular foam silica (MCF). MCF silica has a pore diameter of 20-50nm and surface area of 500-1,000m2/g. Among them, about 90% of the initial enzyme activity was maintained even after 10 consecutive recycle by aldehydefunctionalized MCF-immobilized enzyme, in particular, when introduced by a flexible 11-carbon spacer.