Synthesis of indium phthalocyanines for photodynamic antimicrobial chemotherapy and photo-oxidation of pollutants
- Authors: Sindelo, Azole
- Date: 2019
- Subjects: Phthalocyanines , Azo dyes , Indium compounds , Photochemotherapy , Nanoparticles , Photodegradation , Pollutants , Water -- Purification
- Language: English
- Type: text , Thesis , Masters , MSc
- Identifier: http://hdl.handle.net/10962/67581 , vital:29116
- Description: Indium (III) octacarboxyl phthalocyanine (ClInOCPc) alone and when conjugated to magnetic nanoparticles (MNP-ClInOCPc), 2(3),9(10),16(17),23(24)-octapyridylsulfanyl phthalocyaninato chloroindium (III) (ClInOPyPc) and its quaternized derivative 2(3),9(10),16(17),23(24)-octamethylpyridylsulfanyl phthalocyaninato chloroindium (III) (ClInOMePyPc) were synthesized. All Pcs were tested for both photodynamic antimicrobial chemotherapy (PACT) of an unknown water sample and photo-degradation of methyl red (MR). The singlet quantum yield (ΦΔ) for the ClInOCPc and MNP-ClInOCPc in PAN polymer fibers were 0.36 and 0.20 respectively using ADMA as a quencher in water. The photo-inactivation of bacteria in a water sample with unknown microbes was tested, with the MNP-ClInOCPc inactivating 90.6 % of the microbes and the ClInOCPc with 84.8 %. When embedded to the polymer, there was 48% bacterial clearance for ClInOCPc and 64% clearance for the MNP-ClInOCPc. The rate of degradation of MR increased with decrease of the MR concentration, with the MNP-ClInOCPc having the fastest rate. For ClInOPyPc and ClInOMePyPc, the singlet quantum yields were 0.46 and 0.33 in dimethylformamide (DMF), respectively. The PACT activity of ClInOMePyPc (containing 8 positive charges) was compared to those of 9(10),16(17),23(24)-tri-N-methyl-4-pyridylsulfanyl-2(3)-(4-aminophenoxy) phthalocyaninato chloro indium (III) triiodide (1) (containing 3 positive charges) and 2-[4-(N-methylpyridyloxy) phthalocyaninato] chloroindium (III) iodide (2) (containing 4 positive charges). When comparing ClInOMePyPc, 1 and 2, the largest log reduction for E. coli were obtained for complex 2 containing four positive charges hence showing it is not always the charge that determines the PACT activity, but the bridging atom in the phthalocyanine plays a role.
- Full Text:
Characterization and application of phthalocyanine-gold nanoparticle conjugates
- Authors: Tombe, Sekai Lana
- Date: 2013
- Subjects: Phthalocyanines , Gold , Zinc , Nanoparticles , Bioconjugates , Photochemistry , Photocatalysis , Electrospinning , Polymers , Pollutants , Phenols , Azo dyes
- Language: English
- Type: Thesis , Masters , MSc
- Identifier: vital:4293 , http://hdl.handle.net/10962/d1004517 , Phthalocyanines , Gold , Zinc , Nanoparticles , Bioconjugates , Photochemistry , Photocatalysis , Electrospinning , Polymers , Pollutants , Phenols , Azo dyes
- Description: This work presents the syntheses, photophysical and photochemical characterization of arylthio zinc phthalocyanines and their gold nanoparticle conjugates. Spectroscopic and microscopic studies confirmed the formation of the phthalocyanine-gold nanoparticle conjugates which exhibited enhanced photophysicochemical properties in comparison to the phthalocyanines. The studies showed that the presence of gold nanoparticles significantly lowered fluorescence quantum yields and lifetimes. However, this interaction did not restrict the formation of excited singlet and triplet states and hence the formation of singlet oxygen required for photocatalysis. The conjugates showed significantly higher singlet oxygen quantum yields and therefore enhanced photocatalytic activity compared to the phthalocyanines. The zinc phthalocyanines and their gold nanoparticle conjugates were successfully incorporated into electrospun polymer fibers. Spectral characteristics of the functionalized electrospun fibers indicated that the phthalocyanines and phthalocyanine-gold nanoparticle conjugates were bound and their integrity was maintained within the polymeric fiber matrices. The photophysical and photochemical properties of the complexes were equally maintained within the electrospun fibers. The functionalized fibers were applied for the photoconversion of 4-chlorophenol and Orange G as model organic pollutants. , Microsoft� Word 2010 , Adobe Acrobat 9.53 Paper Capture Plug-in
- Full Text:
Capillary membrane-immobilised polyphenol oxidase and the bioremediation of industrial phenolic effluent
- Authors: Edwards, Wade
- Date: 1999
- Subjects: Membranes (Technology) , Effluent quality , Pollutants , Phenols , Water -- Purification
- Language: English
- Type: Thesis , Doctoral , PhD
- Identifier: vital:4095 , http://hdl.handle.net/10962/d1008458
- Description: Waste-generating industrialisation is intrinsically associated with population and economic proliferation. This places considerable emphasis on South Africa's water shortage due to the integral relationship between population growth rate and infrastructure development. Of the various types of industry-generated effluents, those containing organic pollutants such as phenols are generally difficult to remediate. Much work has been reported in the literature on the use of enzymes for the removal of phenols from these waste-streams but little application of this bioremediation approach has reached practical fruition. This study focuses on integrating and synergistically combining the advantages of enzyme-mediated dephenolisation of synthetic and industrial effluent with that of membrane teclmology. The ability of the enzyme polyphenol oxidase to convert phenol and a number of its derivatives to chemically reactive o-quinones has been reported extensively in the literature. These o-quinones can then physically be removed from solution using various precipitation or adsorption techniques. The enzyme is, however, plagued by a product-induced phenomenon known as suicide inactivation, which renders it inactive and thus limits its application as a bioremediation tool. Integrating membrane technology with the enzyme's catalytic ability by immobilising polyphenol oxidase onto polysulphone and poly(ether sulphone) capillary membranes enabled the physical removal of these inhibitory products from the micro-environment of the immobilised enzyme which therefore increased the phenol conversion capability of the immobilised biocatalyst. Under non-immobilised conditions it was found that when exposed to a mixture of various phenols the substrate preference of the enzyme is a function of the R-group. Under immobilised conditions, however, the substrate preference of the enzyme becomes a function of certain transport constraints imposed by the capillary membrane itself. Furthermore, by integrating a quinone-removal process in the enzyme-immobilised bioreactor configuration, a 21-fold increase in the amount of substrate converted per Unit enzyme was observed when compared to the conversion capacity of the inunobilised enzyme without the product removal step. Comparisons were also made using different membrane bioreactor configurations (orientating the capillaries transverse as opposed to parallel to the module axis) and different immobilisation matrices (poly(ether sulphone) and polysulphone capillary membranes). Conversion efficiencies as high as 77% were maintained for several hours using the combination of transverse-flow modules and novel polysulphone capillary membranes. It was therefore concluded that immobilisation of polyphenol oxidase on capillary membranes does indeed show considerable potential for future development.
- Full Text:
The development of an immobilised-enzyme bioprobe for the detection of phenolic pollutants in water
- Authors: Russell, Ingrid Margaret
- Date: 1999
- Subjects: Pollutants -- Biodegradation , Pollutants , Chemical reactors , Membrane reactors , Fungi -- Biotechnology
- Language: English
- Type: Thesis , Masters , MSc
- Identifier: vital:4069 , http://hdl.handle.net/10962/d1006211 , Pollutants -- Biodegradation , Pollutants , Chemical reactors , Membrane reactors , Fungi -- Biotechnology
- Description: The possibility of developing an immobilised-enzyme bioprobe, based on mushroom polyphenol oxidase, for the purely biological detection and quantification of phenolic pollutants in water was investigated. Polyphenol oxidase catalyses the bioconversion of many phenolic compounds into quinone-related coloured products. Thus, in an immobilised form, the enzyme serves as a visible indicator of the presence and concentration of phenolic pollutants in water. The objective of this research was to develop a portable, disposable bioprobe incorporating polyphenol oxidase for this purpose. The intensity of the colour changes produced by the enzyme on reaction with p-cresol, p-chlorophenol and phenol was found to increase proportionally with increasing concentrations of these substrates in solution. Immobilisation of the enzyme on various supports did not appear to significantly affect the catalytic activity of the enzyme. The enzyme was immobilised by adsorption and cross-linking on polyethersulphone, nitrocellulose and nylon membranes with the production of various colour ranges on reaction with the phenolic substrates. The most successful immobilisation of the enzyme, in terms of quantity and distribution of enzyme immobilised and colour production, was obtained with the enzyme immobilised by adsorption on nylon membranes in the presence of 3-methyl-2-benzothiazolinone hydrazone (MBTH). The enzyme, immobilised using this method, produced ranges of maroon colours in phenolic solutions and orange colours in cresylic solutions. The colour intensities produced were found to increase proportionally with increasing substrate concentration after 5 minutes exposure to the substrates. The bioprobe had a broad substrate specificity and was sensitive to substrate concentrations down to 0.05 mg/L. The enzyme activity of the bioprobe was not significantly affected in a pH range from 4 to 10 and in a temperature range from 5-25⁰C. The bioprobe activity was not affected by various concentrations of salt and metal ions and the bioprobe was able to detect and semi-quantify phenolic substrates in industrial effluent samples. These features of the bioprobe indicate that the commercialisation of such a bioprobe is feasible and this technology has been patented (Patent No. SA 97/0227). , KMBT_363 , Adobe Acrobat 9.54 Paper Capture Plug-in
- Full Text: