title: Identification, characterization, immobilization of a novel type hydrolase (LmH) from Listeria monocytogenes.
abstract: A novel type of hydrolase (LmH) from Listeria monocytogenes was identified, characterized, and immobilized for biotechnological applications. Primary sequence analysis indicated that LmH had a catalytic triad (Ser(91)-Asp(192)-His(222)) with a molecular weight of 27.8 kDa. Homologs of this enzyme are produced by many Gram-positive bacteria including Bacillus, Staphylococcus, and Enterococcus. Biochemical properties of LmH were investigated by performing mass spectrometry, dynamic light scattering (DLS), enzyme assays, enantioselective analysis, circular dichroism (CD) spectroscopy, fluorescence analysis, and macroscopic hydrogel formations. Interestingly, cross-linked enzyme aggregates (CLEAs) of LmH exhibited enhanced stability and good recycling abilities compared to free LmH. These molecular characteristics of LmH highlight its great potential for the pharmaceutical, biotechnological, and chemical industries.
authors.affiliation: Department of Applied Chemistry and Biological Engineering, College of Engineering, Ajou University, Suwon 443-749, South Korea.
authors.forename: Hansol
authors.initials: H
authors.lastname: Ju
authors.affiliation: Department of Applied Chemistry and Biological Engineering, College of Engineering, Ajou University, Suwon 443-749, South Korea.
authors.forename: Bum Han
authors.initials: BH
authors.lastname: Ryu
authors.affiliation: Department of Applied Chemistry and Biological Engineering, College of Engineering, Ajou University, Suwon 443-749, South Korea. Electronic address: doohunkim@ajou.ac.kr.
authors.forename: T
authors.initials: T
authors.lastname: Doohun Kim
mesh_terms: D000595:Amino Acid Sequence; D019295:Computational Biology; D003198:Computer Simulation; D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000378:metabolism*; D006867:Hydrolases / Q000737:chemistry / Q000378:metabolism*; D008089:Listeria monocytogenes / Q000201:enzymology*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010802:Phylogeny; D066329:Protein Aggregates; D016415:Sequence Alignment
chemical_list: D004800:Enzymes, Immobilized; D066329:Protein Aggregates; D006867:Hydrolases
keywords: CLEA; Hydrogel; LmH