title: Halophiles and their enzymes: negativity put to good use.
abstract: Halophilic microorganisms possess stable enzymes that function in very high salinity, an extreme condition that leads to denaturation, aggregation, and precipitation of most other proteins. Genomic and structural analyses have established that the enzymes of halophilic Archaea and many halophilic Bacteria are negatively charged due to an excess of acidic over basic residues, and altered hydrophobicity, which enhance solubility and promote function in low water activity conditions. Here, we provide an update on recent bioinformatic analysis of predicted halophilic proteomes as well as experimental molecular studies on individual halophilic enzymes. Recent efforts on discovery and utilization of halophiles and their enzymes for biotechnology, including biofuel applications are also considered.
authors.affiliation: Institute of Marine and Environmental Technology, Department of Microbiology and Immunology, University of Maryland School of Medicine, 701 East Pratt Street, Columbus Center, Baltimore, MD 21202, USA. Electronic address: sdassarma@som.umaryland.edu.
authors.forename: Shiladitya
authors.initials: S
authors.lastname: DasSarma
authors.affiliation: Institute of Marine and Environmental Technology, Department of Microbiology and Immunology, University of Maryland School of Medicine, 701 East Pratt Street, Columbus Center, Baltimore, MD 21202, USA.
authors.forename: Priya
authors.initials: P
authors.lastname: DasSarma
mesh_terms: D001105:Archaea / Q000201:enzymology* / Q000378:metabolism; D056804:Biofuels; D001709:Biotechnology; D019295:Computational Biology; D004795:Enzyme Stability; D004798:Enzymes / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D016680:Genome, Bacterial; D020543:Proteome; D054712:Salinity; D055049:Salt Tolerance
chemical_list: D056804:Biofuels; D004798:Enzymes; D020543:Proteome