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  • About
  • The Global ETD Search service is a free service for researchers to find electronic theses and dissertations. This service is provided by the Networked Digital Library of Theses and Dissertations.
    Our metadata is collected from universities around the world. If you manage a university/consortium/country archive and want to be added, details can be found on the NDLTD website.
1

The relationship between structure and thermostability of a nitrile hydratase from Goebacillus pallidus RAPc8.

Van Wyk, Jennifer Caroline. January 2008 (has links)
<p>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 molecular mechanism(s) involved in the enhanced thermostability.</p>
2

The relationship between structure and thermostability of a nitrile hydratase from Goebacillus pallidus RAPc8.

Van Wyk, Jennifer Caroline. January 2008 (has links)
<p>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 molecular mechanism(s) involved in the enhanced thermostability.</p>
3

The relationship between structure and thermostability of a nitrile hydratase from Goebacillus pallidus RAPc8

Van Wyk, Jennifer Caroline January 2008 (has links)
Philosophiae Doctor - PhD / Nitrile hydratases (NHases) are very important biocatalysts for the enzymatic conversion of nitriles to industrially important amides such as acrylamide and nicotinamide. An “ideal” NHase should fulfil several essential criteria including, high substrate conversion rates, being able to tolerate high substrate and product concentrations as well as being highly thermostable. The NHase 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 molecular mechanism(s) involved in the enhanced thermostability. Two randomly mutated libraries were constructed using MnCl2 mediated errorprone PCR. The PCR reaction was performed using 0.05 mM and 0.10 mM MnCl2 and a biased dNTP concentration. The hydroxamic acid assay was used to screen the randomly mutated libraries for NHase mutants with enhanced thermostability. Six mutants that exhibited thermostability-enhancing mutations were isolated from the randomly mutated libraries. The thermostabilised mutants contained between 3 and 7 nucleotide changes per NHase operon. The wild-type and four thermostabilised mutant NHases (7D, 8C, 9C, 9E) were over-expressed, purified, crystallised and subjected to X-ray crystallography. The resolution of the diffraction data for the all the mutant NHases were better than the 2.4Å previously obtained for the wild-type G. pallidus NHase. The best quality data was collected for mutant 9E, which diffracted to a resolution of 1.15Å. The high quality crystal structures allowed each thermostability-enhancing mutation to be viewed in detail. As most of the NHase mutants contained multiple mutations, the crystal structures were important in correlating the observed thermostabilisation with the structural effect of the mutations. Analysis of the X-ray crystal structures illustrated the importance of electrostatic interactions, particularly salt bridges and hydrogen bonds in enhancing the thermostability of the mutant NHases. The difference in the free energy of activation of thermal unfolding (DDG) was used to compare the wild-type and mutant NHases thermostability. The most improved NHase, mutant 9C, was stabilised by both a buried inter-subunit salt bridge between aR169 and bD218 and an inter-helical hydrogen bond between bK43 and bK50. The stabilisation provided by these electrostatic interactions was 7.62 kJ/mol. Mutant 8C was primarily stabilised by the introduction an electrostatic network consisting of a salt bridge between bE96 and aR28 and a hydrogen bond between bE96 and bE92. Also, an intra-helical salt bridge between aE192 and aK195 stabilised the helix consisting of a190-196 in mutant 8C by shielding the helix backbone from solvation and preventing co-operative unfolding of the a helix. However, mutant 8C was also destabilised by a mutation that disrupted a water-mediated hydrogen bond between bD167 and bK168 at the heterotetramer interface of the enzyme. Consequently, the net stabilisation energy provided as a result of stabilising and destabilising interactions was 6.16 kJ/mol. Mutant 7D was the only NHase mutant with only one possible thermostabilising mutation. This mutant was stabilised by 3.40 kJ/mol as the result of a water-mediated hydrogen bond between aS47 and bE33. Similarly, a water-mediated hydrogen bond between aS23 and bS103 provided a stabilisation energy of 4.27 kJ/mol to mutant 9E. This project has shown that moderate-frequency randomly mutated libraries can yield mutants with multiple thermostabilising interactions. Also, the importance of utilising X-ray crystallography to investigate structure-function relationships in proteins has been illustrated. / South Africa
4

Direct carbonylation of aromatic nitriles using dicabalt octacarbonyl

Gervay, Joseph Edmund January 1963 (has links)
A new method of synthesizing N-substituted phthalimidines is described. When benzonitrile was reacted with carbon monoxide containing about 0.04 volume percent of hydrogen and in the presence of dicobalt octacarbonyl and pyridine in benzene solution at 235° and 3400 p.s.i. pressure the following compounds were produced: N-benzyphthalimidine (8%), N-phenylphthalimidine (3.7%), and benzamide (3.9%). When 40 p.s.i. hydrogen was added under the same reaction conditions, the yield of N-benzylphthalimidine increased (16%). When benzonitrile was subjected to the same reaction conditions using 240 p.s.d. hydrogen and no pyridine, N-benzylphthalimidine (15%) and sym-dibenzylurea (8%) were produced. A study on the mechanism of the ring closure process using deuterium gas revealed, that the ortho- hydrogen of the aromatic ring is not transferred directly to the unsaturated carbon-nitrogen bond in the course of the reaction. When phenylacetonitrile was reacted with carbon monoxide and 350 p.s.i. hydrogen at 250° in the presence of dicobalt octacarbonyl the following compounds were isolated: phenacetyl- β-phenethylamine (30%), di-β-phenylethylamine (23%), di- β-phenylethylurea (3.1%) and phenylacetamide (3%). When m-tolunitrile was reacted under similar reaction conditions with 185 p.s.i. hydrogen at 240°, N-m-xylylurea (9.5%), N,N'-di-m-xylylurea (13.5%), and m-toluamide (11.5%) were produced. Organometallic complexes were also obtained in all the reactions described above. The infrared spectra of all the compounds obtained, and the n.m.r.. spectra of N-benzylphthalimidine and N phenylphthalimidine are described. / Science, Faculty of / Chemistry, Department of / Graduate
5

The preparation of lauronitrile and myristonitrile

Bogert, Virgil Vernon. January 1937 (has links)
Thesis (M.S.)--University of Wisconsin--Madison, 1937. / Typescript. eContent provider-neutral record in process. Description based on print version record. Includes bibliographical references (leaves 16-17).
6

Some reactions of sodium phenylacetonitrile and sodium [alpha]-phenylbutyronitrile ...

Aldrich, Helen Fiske, January 1935 (has links)
Part of Thesis (Ph. D.)--University of Chicago, 1933. / Lithoprinted. "Private edition, distributed by the University of Chicago Libraries, Chicago, Illinois."
7

The degradation of nitrile compounds by an acinetobacter SP. RFB.1

Toerien, Stefan 13 February 2014 (has links)
M.Sc. (Biochemistry) / An Acinetobacter sp. was isolated which had the ability to metabolise both organic nitriles and inorganic cyanide salts. The enzyme responsible for the degradation of the nitrile groups, was found to be an extra-cellular complex. This complex was partially purified and was shown to consist of not only a number of protein fractions, but also a definite lipid fraction which was identified as being fatty acids. The entire complex had a molecular weight of about 80 000 Da. The enzyme complex exhibited a high degree of stability in the crude form, but rapidly lost its activity on further purification. The complex had a Km of 0.154 ug/ml and a Vmax of 0.534 ug/ml/min for KCN as substrate. This Km value indicates that the complex has a high affinity for KCN and may be of use in the removal of cyanide at low levels. The temperature optimum was shown to be 20·C and the pH-optimum 6.5. Fatty acids were produced both in the presence and absence of a nitrile substrate, and it is unclear whether carbon from CN degradation can be channeled into fatty acid synthesis by this particular bacterium. This bacterium was found to be very effective in the degradation of nitrile compounds. The removal of cyanide from mine effluents is of particular interest in South Africa today and no effective biological method is currently in use.
8

A study of the Hoesch reaction

Langley, Wilson Davis, Adams, Roger, January 1900 (has links)
Thesis (Ph. D.)--University of Illinois, 1922. / Vita. Caption title: Condensation of certain nitriles and various polyhydroxyphenols to form phenolic acids, by Wilson D. Langley with Roger Adams. "Reprinted from the Journal of the American Chemical Society. vol. XLVI, no.10. October, 1922."
9

I. Preparation of nitriles. II. Catalytic preparation of nitriles ...

Van Epps, George Dudley, January 1900 (has links)
Thesis (Ph. D.)--Johns Hopkins University, 1916. / Biographical sketch.
10

Catalytic hydrogenation of nitriles

Juday, Richard Evans, January 1943 (has links)
Thesis (Ph. D.)--University of Wisconsin--Madison, 1943. / Typescript. Vita. eContent provider-neutral record in process. Description based on print version record. Includes bibliographical references (leaf [62]).

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