title: Characterization and preparation of highly stable aggregates of a novel type of hydrolase (BL28) from Bacillus licheniformis.
abstract: A novel type of hydrolase (BL28) from Bacillus licheniformis was identified, expressed in Escherichia coli, characterized, and immobilized for industrial applications. Biochemical characteristics of BL28 were investigated by performing SDS-PAGE, mass spectrometry, enzyme assays, CD spectroscopy, intrinsic fluorescence, and in silico analysis. Furthermore, cross-linked enzyme aggregates (CLEAs) of BL28 were prepared. These CLEA-BL28 aggregates exhibited improved catalytic efficiencies and stabilities compared to free BL28 against harsh conditions of thermal or chemical stress as well as high reusability. The characteristics of the CLEA-BL28 aggregates highlight their great potentials in pharmaceutical and chemical industries.
authors.affiliation: Department of Molecular Science and Technology, Graduate School of Interdisciplinary Programs, Ajou University, Suwon 443-749, South Korea.
authors.forename: Hansol
authors.initials: H
authors.lastname: Ju
authors.forename: Eunjin
authors.initials: E
authors.lastname: Jang
authors.forename: Bum Han
authors.initials: BH
authors.lastname: Ryu
authors.forename: T Doohun
authors.initials: TD
authors.lastname: Kim
mesh_terms: D000595:Amino Acid Sequence; D001407:Bacillus / Q000201:enzymology*; D004789:Enzyme Activation; D004795:Enzyme Stability; D006867:Hydrolases / Q000737:chemistry* / Q000302:isolation & purification*; D008969:Molecular Sequence Data; D013379:Substrate Specificity
chemical_list: D006867:Hydrolases