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:
- Date Issued: 1999
- 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:
- Date Issued: 1999
Evaluation of a 'defouling on demand' strategy for the ultrafiltration of brown water using activatable enzymes
- Authors: Buchanan, K
- Date: 1999
- Subjects: Water -- Purification , Ultrafiltration , Enzymes , Membranes (Technology)
- Language: English
- Type: Thesis , Masters , MSc
- Identifier: vital:3904 , http://hdl.handle.net/10962/d1003963 , Water -- Purification , Ultrafiltration , Enzymes , Membranes (Technology)
- Description: New approaches to the application of membranes for the production of potable water are constantly being sought after in anticipation of future demands for increasingly rigorous water quality standards and reduced environmental impact. A major limitation, however, is membrane fouling, which manifests itself as a continual reduction in flux over time and thus restricts the practical implementation to restore flux. Mechanical and chemical methods have been implemented to restore flux to ultrafiltration systems, but these either result in a break in the process operation or lead to membrane damage or additional pollution problems. This project was aimed to develop a 'defouling on demand' stategy for cleaning membranes used during brown water ultrafiltration. The process involves the use of activatable peroxidase enzymes, which were immobilised onto flat sheet polysulphone membranes. Following flux decline which reaches a critical level with the build-up of the foulant layer, the immobilised enzyme layer was activated by the addition of a chemical activator solution, in this case hydrogen peroxidase and manganous sulphate. Manganese peroxidase was found to be the most effective enzyme at alleviating fouling by degrading the foulant layer formed on the membrane surface and hence restored flux to the ultrafiltration system. A 93% flux improvement was observed when manganese peroxidase was activated when 800uM manganous sulphate, 100mM hydrogen peroxide were added in the presence of a manganese chelator, lactate. The concept and the potential benefits this system holds will be discussed in further detail.
- Full Text:
- Date Issued: 1999
- Authors: Buchanan, K
- Date: 1999
- Subjects: Water -- Purification , Ultrafiltration , Enzymes , Membranes (Technology)
- Language: English
- Type: Thesis , Masters , MSc
- Identifier: vital:3904 , http://hdl.handle.net/10962/d1003963 , Water -- Purification , Ultrafiltration , Enzymes , Membranes (Technology)
- Description: New approaches to the application of membranes for the production of potable water are constantly being sought after in anticipation of future demands for increasingly rigorous water quality standards and reduced environmental impact. A major limitation, however, is membrane fouling, which manifests itself as a continual reduction in flux over time and thus restricts the practical implementation to restore flux. Mechanical and chemical methods have been implemented to restore flux to ultrafiltration systems, but these either result in a break in the process operation or lead to membrane damage or additional pollution problems. This project was aimed to develop a 'defouling on demand' stategy for cleaning membranes used during brown water ultrafiltration. The process involves the use of activatable peroxidase enzymes, which were immobilised onto flat sheet polysulphone membranes. Following flux decline which reaches a critical level with the build-up of the foulant layer, the immobilised enzyme layer was activated by the addition of a chemical activator solution, in this case hydrogen peroxidase and manganous sulphate. Manganese peroxidase was found to be the most effective enzyme at alleviating fouling by degrading the foulant layer formed on the membrane surface and hence restored flux to the ultrafiltration system. A 93% flux improvement was observed when manganese peroxidase was activated when 800uM manganous sulphate, 100mM hydrogen peroxide were added in the presence of a manganese chelator, lactate. The concept and the potential benefits this system holds will be discussed in further detail.
- Full Text:
- Date Issued: 1999
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