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Showing 1 to 7 of 7 for “"Geobacillus pallidus"”.
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The crystal structure of an aliphatic amidase from Geobacillus pallidus RAPc8
… of acidic products. Aliphatic amidase from Geobacillus pallidus RAPcS (RAPcS amidase), which belongs to the nitrilase superfamily of enzymes, has recently been characterised biochemically. It shows both amide hydrolysis and acyl transfer activities, and also exhibits stereo selectivity for …
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Investigation of the determinants of thermal stability of the nitrile hydratase from Geobacillus pallidus RAPc8
… composite mutants generated from the wild type Geobacillus pallidus RAPc8 nitrile hydratase (NHase), namely: L103S+Y127N+F36L+D4G, M43K+T150A+S169R and D96E+D167V+M188V each labelled as 9E, 9C and 8C respectively. The composite mutants were previously developed using error-prone PCR of the wild …
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An investigation into the biocatalytic application of the thermostable nitrile hydratase from the thermophilic strain Geobacillus pallidus RAPc8
… A novel moderately thermophilic microorganism, Geobacillus pallidus RAPc8, was isolated by our collaborators (Pereira and co-workers, 1998). The strain has an optimal growth temperature of 65oC and constutitively expresses a thermostable nitrile hydratase. The gene cluster containing the nitrile …
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Synthesis of enantio-pure amides by reversal of the Geobacillus pallidus RAPc8 amidase hydrolysis reaction in non-aqueous media
… was previously isOlated from a thermophilic Geobacillus species, and the amidase was cloned and expressed in an Escherichia coli BL21 strain. Also in previous studies, it was shown that the enzyme exhibits both amide hydrolysis and acyl transfer activities. The highest activity of the G. …
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Process integration in the optimisation of amidase production from recombinant Escherichia coli
… a novel thermostable amidase (EC 3.5.1.4) from Geobacillus pallidus RAPc8 using recombinant E.coli BL21 (DE3). The choice of growth medium and induction strategy were optimised under bioreactor conditions to enhance amidase productivity. Further, expanded bed adsorption (EBA) was assessed as a …
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The structure, function and engineering of a thermostable nitrile hydratase
… this study belongs to the thermophilic bacteria Geobacillus pallidus. The G. pallidus RAPc8 NHase is a heterotetramer that has a 28 kDa α subunit and a 29 kDa β subunit, with a α2β2 configured functional unit. The G. pallidus RAPc8 NHase operon has been cloned, sequenced and expressed at high …
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The relationship between structure and thermostability of a nitrile hydratase from Goebacillus pallidus RAPc8
… used in the present study was isolated from Geobacillus pallidus RAPc8, a moderate thermophile. The primary aims of this study were to use random mutagenesis to engineer the G. pallidus RAPc8 NHase towards improved thermostability and then to use X-ray crystallography to investigate the …