Properties of extremely thermostable proteases from anaerobic hyperthermophilic bacteria

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dc.contributor.author Hashwa, Fuad
dc.contributor.author Klingeberg, Micheal
dc.contributor.author Antranikian, Garabed
dc.date.accessioned 2017-01-30T09:39:49Z
dc.date.available 2017-01-30T09:39:49Z
dc.date.copyright 1991 en_US
dc.date.issued 2017-01-30
dc.identifier.issn 0175-7598 en_US
dc.identifier.uri http://hdl.handle.net/10725/5105
dc.description.abstract Hyperthermostable proteases were characterized from five archaeobacterial species (Thermococcus celer, T. stetteri, Thermococcus strain AN 1, T. litoralis, Staphylothermus marinus) and the hyperthermophilic eubacterium Thermobacteroides proteolyticus. These proteases, which were found to be of the serine type, exhibited a preference for phenylalanine in the carboxylic side of the peptide. The enzymes from Thermococcus stetteri and T. litoralis hydrolysed most substrates (peptides) tested. All proteases were extremely thermostable and demonstrated optimal activities between 80 and 95°C. The pH optimum was either neutral (T. celer, Thermococcus strain AN 1) or alkaline. The protease of Thermobacteroides proteolyticus was optimally active at pH 9.5. Zymogram staining showed the presence of multiple protease bands for all strains investigated. en_US
dc.language.iso en en_US
dc.title Properties of extremely thermostable proteases from anaerobic hyperthermophilic bacteria en_US
dc.type Article en_US
dc.description.version Published en_US
dc.author.school SAS en_US
dc.author.idnumber 199390070 en_US
dc.author.department Natural Sciences en_US
dc.description.embargo N/A en_US
dc.relation.journal Applied Microbiology and Biotechnology en_US
dc.journal.volume 34 en_US
dc.journal.issue 6 en_US
dc.article.pages 715-719 en_US
dc.identifier.doi http://dx.doi.org/10.1007/BF00169339 en_US
dc.identifier.ctation Klingeberg, M., Hashwa, F., & Antranikian, G. (1991). Properties of extremely thermostable proteases from anaerobic hyperthermophilic bacteria. Applied microbiology and biotechnology, 34(6), 715-719. en_US
dc.author.email fhashwa@lau.edu.lb en_US
dc.identifier.tou http://libraries.lau.edu.lb/research/laur/terms-of-use/articles.php en_US
dc.identifier.url http://link.springer.com/article/10.1007%2FBF00169339?LI=true en_US
dc.author.affiliation Lebanese American University en_US

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