Characterisation of the glycoside hydrolase domain of a novel bi-functional metagenomic clone for use in the biofuel production industry

dc.contributor.advisorPeters, Shaunen_ZA
dc.contributor.advisorLoedolff, Biankeen_ZA
dc.contributor.advisorKossmann, Jensen_ZA
dc.contributor.authorSwanepoel, Craig C.en_ZA
dc.contributor.otherStellenbosch University. Faculty of AgriSciences. Dept. of Genetics.en_ZA
dc.descriptionThesis (MSc)--Stellenbosch University, 2017.en_ZA
dc.description.abstractENGLISH ABSTRACT: The current practice of 1st generation biofuel production is marred by several hurdles, namely concerns over food security and the moral dilemma created by using edible feedstocks as a biofuel production source. Second generation biofuel production methods stand to take the forefront and address the world’s need for a renewable liquid fuel source without affecting food security and adding value to the abundant lignocellulosic biomass available worldwide. However, in order to achieve this, 2nd generation biofuel production methods need to become more efficient at liberating fermentable glucose from lignocellulosic biomass. Metagenomic sampling and novel enzyme discovery are the most promising sources of finding new, more efficient enzymes from unculturable microorganisms that can degrade lignocellulosic biomass into fermentable glucose more ably than current enzymes used in industry. Industrial enzymes within the biofuels scope are required to be thermotolerant, pH tolerant, resistant to product inhibition and resistant to denaturation by industrial solvents. A novel, bi-functional, ßglucosidase and ß-galactosidase enzyme, termed Clone 3L, was identified via a metagenomic sampling approach. This study outlines the characterization of clone 3L, including the kinetics of the enzyme and an assessment of the suitability of the enzyme within an industrial, 2nd generation biofuel production pipeline. Clone 3L was found to be a promising candidate for use in 2nd generation biofuel production schemes, with the enzyme exhibiting high activity and affinity for its cellobiose substrate and a high degree of tolerance to various solvents, glucose inhibition and a high activity across a wide pH range.en_ZA
dc.description.abstractAFRIKAANSE OPSOMMING: Geen opsomming beskikbaaraf_ZA
dc.format.extent43 pages : illustrationsen_ZA
dc.publisherStellenbosch : Stellenbosch Universityen_ZA
dc.subjectBiomass energyen_ZA
dc.subjectLignocellulose -- Biotechnologyen_ZA
dc.subjectNovel bi-functional metagenomic cloneen_ZA
dc.titleCharacterisation of the glycoside hydrolase domain of a novel bi-functional metagenomic clone for use in the biofuel production industryen_ZA
dc.rights.holderStellenbosch Universityen_ZA

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