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Coccolithophores: functional biodiversity, enzymes and bioprospecting.
Reid, Emma L; Worthy, Charlotte A; Probert, Ian; Ali, Sohail T; Love, John; Napier, Johnathan; Littlechild, Jenny A; Somerfield, Paul J; Allen, Michael J.
Afiliación
  • Reid EL; Plymouth Marine Laboratory, Prospect Place, The Hoe, Plymouth, PL1 3DH, UK.
  • Worthy CA; College of Life and Environmental Science, Biosciences, University of Exeter, Exeter, EX4 4QD, UK.
  • Probert I; Plymouth Marine Laboratory, Prospect Place, The Hoe, Plymouth, PL1 3DH, UK.
  • Ali ST; Department of Biological Chemistry, Rothamsted Research, Harpenden, Herts AL5 2JQ, UK.
  • Love J; CNRS-UPMC Station Biologique de Roscoff, Place Georges Teissier, 29682 Roscoff Cedex, France.
  • Napier J; Plymouth Marine Laboratory, Prospect Place, The Hoe, Plymouth, PL1 3DH, UK.
  • Littlechild JA; College of Life and Environmental Science, Biosciences, University of Exeter, Exeter, EX4 4QD, UK.
  • Somerfield PJ; Department of Biological Chemistry, Rothamsted Research, Harpenden, Herts AL5 2JQ, UK.
  • Allen MJ; College of Life and Environmental Science, Biosciences, University of Exeter, Exeter, EX4 4QD, UK.
Mar Drugs ; 9(4): 586-602, 2011.
Article en En | MEDLINE | ID: mdl-21731551
ABSTRACT
Emiliania huxleyi is a single celled, marine phytoplankton with global distribution. As a key species for global biogeochemical cycling, a variety of strains have been amassed in various culture collections. Using a library consisting of 52 strains of E. huxleyi and an 'in house' enzyme screening program, we have assessed the functional biodiversity within this species of fundamental importance to global biogeochemical cycling, whilst at the same time determining their potential for exploitation in biocatalytic applications. Here, we describe the screening of E. huxleyi strains, as well as a coccolithovirus infected strain, for commercially relevant biocatalytic enzymes such as acid/alkali phosphodiesterase, acid/alkali phosphomonoesterase, EC1.1.1-type dehydrogenase, EC1.3.1-type dehydrogenase and carboxylesterase.
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Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Fitoplancton / Biodiversidad / Haptophyta Idioma: En Revista: Mar Drugs Asunto de la revista: BIOLOGIA / FARMACOLOGIA Año: 2011 Tipo del documento: Article País de afiliación: Reino Unido

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Fitoplancton / Biodiversidad / Haptophyta Idioma: En Revista: Mar Drugs Asunto de la revista: BIOLOGIA / FARMACOLOGIA Año: 2011 Tipo del documento: Article País de afiliación: Reino Unido