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Title: Investigating the plant cell wall degrading enzyme systems of Humicola insolens
Author: Mozolowski, Guy
Awarding Body: University of Nottingham
Current Institution: University of Nottingham
Date of Award: 2008
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The thermophilic filamentous fungus H. insolens has been widely recognised for its ability to degrade plant cell wall matter. Hydrolytic preparations derived from H. insolens have existing applications in industry, primarily concerning reduction in viscosity ofagro-industrial effluents. In recent years the rea li sation that effluents containing high levels of flow value plant cell wall polysaccharide could represent a significant source of fermentable sugars for a rapidly emerging bic-fuel industry has lead to the investigation of catabolic enzyme systems of a number of saprophytic organisms. This thesis presents a study of the H insolens derived hydrolytic preparation DEPOL 740L. DEPOL 740L has been shown to contain plant cell wall polysaccharide degrading enzymes which exhibit a high degree of efficacy against a variety of substrates. This study provides insight into the hydrolytic properties of DE POL 740L and the reasons for its efficacy. Evidence is presented which suggest that organisation of the individual catalytic components of the system into complex, multi-subunit structures may be partially responsible for the observed hydrolytic efficiency. In addition two novel enzymes were purified from the preparation and subsequently characterised . A type 8 feruloyl esterase was shown to have physico-chemical properties typical of this group of fungal enzymes. It was also shown to exhibit unusual properties at extremes of pH, these observations were interpreted as a mechanism designed to protect the enzyme from hydrolysis under extreme conditions. Furthermore, a novel 8-1 ,4-xylosidase enzyme was shown to exhibit remarkable physico-chemical properties, displaying an affinity for extremely high tem peratures and kinetic properties which suggest that it is among the most active and catalytically efficient enzymes of this type isolated thus far.
Supervisor: Not available Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID:  DOI: Not available