Molecular cloning and characterization of (+)-epi-a-bisabolol synthase, the entry point enzyme involved in the hernadulcin biosynthetic pathway in lippia dulcis
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2012
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Abstract
Hemandulcin, a C 15 sesquiterpene ketone, is a natural sweetener isolated from the leaves of Lippia dulcis, an indigenous plant to the Central America. Hernandulcin is a promising sugar substitute due to its safety and low caloric potential. However, its biosynthesis in L. dulcis remains unknown. The first biochemical step in hemandulcin biosynthetic pathway is the synthesis of (+)-epi-a-bisabolol from famesyl diphosphate, which is presumed to be catalyzed by a unique sesquiterpene synthase in L. dulcis. To identify(+)epi-a-bisabolol synthase gene in L. dulcis, deep transcript sequencings ( 454 and Illumina) were performed and five potential candidates were identified by bioinformatic analysis. One of these candidates was successfully identified as a-bisabolol synthase by in vivo functional characterization in metabolically engineered yeast. Deep structural analysis of the produced a-bisabolol confirmed its configuration to be ( + )-epi-a-bisabolol, the core skeleton of hemandulcin. Bisabolol yield from the engineered yeast was quantified and kinetic constants of the identified ( + )-epi-a-bisabolol synthase were determined.
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Bibliography: p. 81-97
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Attia, M. (2012). Molecular cloning and characterization of (+)-epi-a-bisabolol synthase, the entry point enzyme involved in the hernadulcin biosynthetic pathway in lippia dulcis (Master's thesis, University of Calgary, Calgary, Canada). Retrieved from https://prism.ucalgary.ca. doi:10.11575/PRISM/5002