Mise en évidence d'enzymes thermostables chez des micro-organismes thermophiles d'origine hydrothermale

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Éditeur(s) John Libbey Eurotext Ltd
Identifiant documentaire 9-29008
Identifiant OAI oai:archimer.ifremer.fr:29008
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Auteur(s): Ladrat, Christine,Cornec, Laurence,Alayse Danet, Anne-marie,Barbier, Georges
Mots clés alcool-déshydrogénase estérase ~-glucosidase protéase criblage thermostabilité ALCOHOL DEHYDROGENASE ESTERASE PROTEASE SCREENING BETA-GLUCOSIDASE THERMOSTABILITY
Date de publication 01/04/1995
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Source Comptes Rendus de l'Academie des Sciences Serie III-sciences De La Vie-life Sciences (0764-4469) (John Libbey Eurotext Ltd), 1995-04 , Vol. 318 , N. 4 , P. 423-429
Droits de réutilisation Académie des Sciences

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Description
During 3 cruises in the Pacific ocean, hydrothermal samples have been collected and some thermophilic bacteria and archaea have been purified. Four enzymatic activities have been screened on 77 chemo-organoheterotrophic thermophilic microorganisms. Forty-two isolates exhibited intracellular beta-glucosidase activity whereas only 7 (including only one archaeon) showed alcohol dehydrogenase one. Protease activity was not detected on only 6 isolates over 77. Twenty-seven isolates exhibited esterase activity and 3 different electrophoretic patterns have been revealed No isolate was found to exhibit the 4 activities. Preliminary characterization of these activities showed high thermophily and thermostability, properties which could be used in potential biotechnological applications.

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