by Wong Yuk Hang. / Thesis (M.Phil.)--Chinese University of Hong Kong, 1994. / Includes bibliographical references (leaves 110-114). / Abstract --- p.i / Acknowledgement --- p.iv / Dedication --- p.v / Table of Contents --- p.vi / List of Tables --- p.xi / List of Figures --- p.xii / Chapter Chapter 1 --- Introduction and literature review / Chapter 1.1 --- Introduction --- p.2 / Chapter 1.2 --- Literature review --- p.5 / Chapter 1.2.1 --- General considerations --- p.5 / Chapter 1.2.2 --- Nature of glucosinolate --- p.6 / Chapter 1.2.3 --- Degradation of glucosinolates by myrosinase --- p.7 / Chapter 1.2.4 --- Toxicology of glucosinolate and hydrolysis products --- p.8 / Chapter 1.2.5 --- Plant myrosinase --- p.9 / Chapter 1.2.6 --- Fungal myrosinase --- p.11 / Chapter 1.2.7 --- Purification and properties of fungal myrosinase --- p.11 / Chapter Chapter 2 --- Screening of fungi with myrosinase activity and physiological studies of myrosinase production in Aspergillus oryzae / Chapter 2.1 --- Introduction --- p.15 / Chapter 2.2 --- Materials and methods --- p.16 / Chapter 2.2.1 --- Fungal strains --- p.16 / Chapter 2.2.2 --- Media --- p.16 / Chapter 2.2.3 --- Screening --- p.17 / Chapter 2.2.4 --- Enzyme assay and protein determination --- p.18 / Chapter 2.2.4.1 --- Myrosinase assay --- p.18 / Chapter 2.2.4.2 --- Definition of myrosinase unit and specific activity --- p.19 / Chapter 2.2.4.3 --- Protein determination --- p.19 / Chapter 2.2.5 --- Physiological studies of myrosinase production in Aspergillus oryzae --- p.19 / Chapter 2.2.5.1 --- Incubation time --- p.20 / Chapter 2.2.5.2 --- Inducer concentration --- p.20 / Chapter 2.3 --- Results --- p.21 / Chapter 2.3.1 --- Screening --- p.21 / Chapter 2.3.1.1 --- Degradation of sinigrin in culture medium --- p.21 / Chapter 2.3.1.2 --- Confirmation of myrosinase activity --- p.21 / Chapter 2.3.2 --- Physiological studies of myrosinase production in Aspergillus oryzae --- p.21 / Chapter 2.3.2.1 --- Incubation time --- p.21 / Chapter 2.3.2.2 --- Inducer concentration --- p.22 / Chapter 2.4 --- Discussion --- p.23 / Chapter 2.4.1 --- Fungi selection in screening programme --- p.23 / Chapter 2.4.2 --- Medium composition --- p.23 / Chapter 2.4.3 --- Screening --- p.24 / Chapter 2.4.4 --- Physiological studies of myrosinase production in Aspergillus oryzae --- p.25 / Chapter 2.4.4.1 --- Incubation time --- p.25 / Chapter 2.4.4.2 --- Inducer concentration --- p.25 / Chapter Chapter 3 --- Purification and characterization of myrosinase in Aspergillus oryzae / Chapter 3.1 --- Introduction --- p.33 / Chapter 3.2 --- Materials and methods --- p.35 / Chapter 3.2.1 --- Reagents --- p.35 / Chapter 3.2.2 --- Fungal propagation --- p.35 / Chapter 3.2.3 --- Purification of the fungal myrosinase --- p.36 / Chapter 3.2.3.1 --- Preparation of crude extract --- p.36 / Chapter 3.2.3.2 --- Dialysis --- p.37 / Chapter 3.2.3.3 --- DEAE-Sepharose CL-6B ion-exchange chromatography --- p.37 / Chapter 3.2.3.4 --- Sephacryl S-200 molecular sieving chromatography --- p.37 / Chapter 3.2.3.5 --- FPLC Phenyl Superose hydrophobic interaction chromatography --- p.38 / Chapter 3.2.3.6 --- FPLC Mono P chromatofocusing --- p.38 / Chapter 3.2.4 --- Myrosinase assay and protein concentration determination --- p.39 / Chapter 3.2.4.1 --- Spot test for myrosinase activity --- p.39 / Chapter 3.2.4.2 --- Standard end-point assay --- p.40 / Chapter 3.2.4.3 --- Determination of protein concentration --- p.42 / Chapter 3.2.5 --- Physicochemical characterization of the myrosinase isozymes --- p.42 / Chapter 3.2.5.1 --- Sodium dodecyl sulfate polyacrylamide gel electrophoresis --- p.42 / Chapter 3.2.5.2 --- Protein staining and glycoprotein detection --- p.43 / Chapter 3.2.5.3 --- Chromatofocusing --- p.43 / Chapter 3.2.5.4 --- Gel filtration with FPLC Superose 6 --- p.44 / Chapter 3.2.6 --- Enzymatic properties --- p.44 / Chapter 3.2.6.1 --- Effect of pH on crude enzyme stability --- p.44 / Chapter 3.2.6.2 --- Effect of substrate concentration on enzyme activity --- p.45 / Chapter 3.2.6.3 --- Effect of pH on enzyme activity --- p.45 / Chapter 3.2.6.4 --- Effect of temperature on enzyme activity --- p.46 / Chapter 3.2.6.5 --- Effects of metallic ions on enzyme activity --- p.46 / Chapter 3.2.6.6 --- Effects of various compounds on enzyme activity --- p.46 / Chapter 3.2.6.7 --- Effects of various buffers on enzyme activity --- p.47 / Chapter 3.3 --- Results --- p.48 / Chapter 3.3.1 --- Fungal propagation --- p.48 / Chapter 3.3.2 --- Purification of fungal myrosinase in Aspergillus oryzae --- p.48 / Chapter 3.3.2.1 --- Extraction of the enzyme --- p.48 / Chapter 3.3.2.2 --- Dialysis --- p.49 / Chapter 3.3.2.3 --- DEAE-Sepharose ion-exchange chromatography --- p.49 / Chapter 3.3.2.4 --- Sephacryl S-200 molecular sieving chromatography --- p.50 / Chapter 3.3.2.5 --- FPLC Phenyl Superose hydrophobic interaction chromatography --- p.50 / Chapter 3.3.2.6 --- FPLC Mono P chromatofocusing --- p.51 / Chapter 3.3.3 --- Physicochemical characterization --- p.52 / Chapter 3.3.3.1 --- Sodium dodecyl sulfate polyacrylamide gel electrophoresis --- p.52 / Chapter 3.3.3.2 --- Chromatofocusing --- p.53 / Chapter 3.3.3.3 --- Gel filtration --- p.53 / Chapter 3.3.4 --- Enzymatic properties --- p.53 / Chapter 3.3.4.1 --- Effect of pH on the crude enzyme stability --- p.53 / Chapter 3.3.4.2 --- Effect of substrate concentration on enzyme activity --- p.54 / Chapter 3.3.4.3 --- Effect of pH on enzyme activity --- p.54 / Chapter 3.3.4.4 --- Effect of temperature on enzyme activity --- p.55 / Chapter 3.3.4.5 --- Effects of metallic ions on enzyme activity --- p.55 / Chapter 3.3.4.6 --- Effects of various compounds on enzyme activity --- p.56 / Chapter 3.3.4.7 --- Effects of various buffers on enzyme activity --- p.57 / Chapter 3.4 --- Discussion --- p.58 / Chapter 3.4.1 --- Purification of Aspergillus oryzae myrosinase --- p.58 / Chapter 3.4.1.1 --- Dialysis --- p.58 / Chapter 3.4.1.2 --- Enzyme purification --- p.58 / Chapter 3.4.2 --- Physicochemical properties --- p.60 / Chapter 3.4.2.1 --- Glycoprotein --- p.60 / Chapter 3.4.2.2 --- Molecular weights --- p.60 / Chapter 3.4.2.3 --- Isoelectric points --- p.61 / Chapter 3.4.3 --- Enzymatic properties --- p.61 / Chapter 3.4.3.1 --- pH and temperature optima --- p.61 / Chapter 3.4.3.2 --- Substrate affinity --- p.62 / Chapter 3.4.3.3 --- Inhibitions by various compounds and metallic ions --- p.63 / Chapter 3.4.3.4 --- Inhibitions by various buffer systems --- p.64 / Chapter Chapter 4 --- Summary --- p.106 / References --- p.110

by Siu-tai Tsim. / Thesis (M.Phil.)--Chinese University of Hong Kong, 1993. / Includes bibliographical references (leaves 382-403). / Statement --- p.4 / Acknowledgements --- p.5 / Abstract --- p.6 / Abbreviation --- p.8 / Chapter Chapter 1. --- General introduction --- p.10 / Chapter PART I. --- Biodegradation of Indigo carmine / Chapter Chapter 2. --- Introduction to indigo/indigo carmine --- p.29 / Chapter Chapter 3. --- Purification and characterization of crude indigo carmine degrading enzyme --- p.59 / Chapter Chapter 4. --- Characterization of indigo carmine degradation products --- p.181 / Chapter Chapter 5. --- Toxicity of indigo carmine and its degradation products --- p.219 / Chapter Chapter 6. --- A new method to determine the concentration of indigo dye --- p.301 / Chapter PART II. --- Biosorption of Sulfur black dye / Chapter Chapter 7. --- "An efficient method for removal of sulfur black dye, a contaminant in sodium thiosulfate, a side product of sulfur black production" --- p.319 / References --- p.382

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Os compostos BTEX (benzeno, tolueno, etilbenzeno e xilenos) são os contaminantes mais frequentemente encontrados dentre os hidrocarbonetos de petróleo. A remoção destes compostos é dependente da atividade de uma população de micro-organismos adaptados capazes de promover a biodegradação dos mesmos. Neste estudo, foram utilizadas cinco cepas isoladas de área contaminada capazes de degradar estes compostos. As concentrações de BTEX foram determinadas por análises quantitativas realizadas por cromatografia gasosa com extração por headspace. Uma série de experimentos foi realizada para investigar a capacidade destas cepas de remover os compostos BTEX de forma individual e simultânea. Os ensaios de indução de vias metabólicas mostraram que cada um dos BTEX foi capaz de induzir as vias de degradação de todos os quatro substratos, resultado que foi visualizado a partir do crescimento das cepas em cada um dos BTEX após as mesmas terem sido ambientadas em apenas um deles. Para os ensaios de degradação, Os resultados revelaram que as cinco cepas foram capazes de degradar todos os BTEX, tanto na forma de um único substrato bem como em forma de mistura. As taxas de remoção de um único substrato ficaram entre 63,9% e 97,9%. Houve um aumento da degradação dos compostos quando os mesmo foram fornecidos em forma de mistura. Com exceção do benzeno, todos os compostos foram degradados até atingirem concentrações que ficaram abaixo do limite de potabilidade estipulados, dentro de 9 horas. / BTEX (benzene, toluene, ethylbenzene and xylenes) compounds are the most frequently encountered subsurface contaminants among the various petroleum hydrocarbons. Removal of these compounds is dependent on the activity of a population of microorganisms adapted to promote biodegradation of them. In this study, five strains isolated from contaminated groundwater .able to degrade BTEX compounds were used. BTEX concentrations were determined by quantitative analysis performed by gaseous chromatography with headspace extraction. A series of batch experiments were carried out to investigate the ability of the strains for removing BTEX compounds using single and mixed substrates. The pathway induction assays showed that each one of the BTEX compounds was able to induce the degradation pathways of all four substrates, result that was visualized from the growth of the strains in each of the BTEX after they had been set in only one of them. For the degradation assays, the results revealed that the five strains were able to degrade all BTEX, both in the form of a single substrate as well as in the form of a mixture. The rates of removal of a single substrate were between 63.9% and 97.9%. There was an increased degradation of the compounds when they were provided as a mixture. With the exception of benzene, all compounds were degraded to concentrations below the stipulated drinking limit within 9 hours.

Orientador: Ederio Dino Bidoia / Banca: Marcia Nitschke / Banca: Adriano Pinto Mariano / Banca: Roberta Barros Lovaglio / Banca: Maria Aparecida Marin Morales / Resumo: Grande atenção vem sendo dada a contaminação por hidrocarbonetos resultante das atividades da indústria petroquímica. Dentre as tecnologias utilizadas na remediação e tratamento de áreas impactadas, a biodegradação vem despontando como um dos principais campos de pesquisa em microbiologia, se apresentando como uma técnica bastante eficaz. Dessa forma, o presente trabalho visou estudar a biodegradação de gasolina, óleo diesel e dos compostos benzeno, tolueno, etilbenzeno e o-xileno (BTE(o-)X) por Pseudomonas putida CCMI 852 com plasmídeo TOL pWW0, com aplicação de biossurfactante, para aumentar a biodisponibilidade de compostos hidrofóbicos, produzido por Pseudomonas aeruginosa LBI a partir do soro de ricota, como fonte de carbono e com avaliação da toxicidade com sementes de alface (Lactuca sativa) e genotoxicidade com sementes de cebola (Allium cepa), antes e após a biodegradação. Foi observado um potencial de produção de biossurfactantes do tipo ramnolipídios em soro de ricota como substrato alternativo para produção, com rendimento de 0,45 g L-1 . O monitoramento da biodegradação dos hidrocarbonetos, foi realizado por ensaios colorimétricos utilizando os indicadores redox DCPIP e TTC e a quantificação foi realizada por cromatografia gasosa acoplada com espectrometria de massa (CG/MS). Os testes colorimétricos foram eficientes e bastante eficaz para verificar a atividade bacteriana, indicando o potencial do microorganismo em degradar esses compostos, fato este que comprovou... (Resumo completo, clicar acesso eletrônico abaixo) / Abstract: Great attention has been given to the contamination by hydrocarbons from the petrochemical industry. Among the technologies used in the remediation and treatment of impacted areas, biodegradation has emerged as a very effective technique, which is now among the main research fields in microbiology. Thus, this thesis aimed to study the biodegradation of benzene, toluene, ethylbenzene and o-xylene (BTE(o-)X) by Pseudomonas putida CCMI 852 with the TOL pWW0 plasmid, as well as biosurfactant application to increase the bioavailability of hydrophobic compounds produced by Pseudomonas aeruginosa LBI using ricotta serum as the source of carbon. The evaluation of toxicity with lettuce seeds (Lactuca sativa) and genotoxicity with onion seeds (Allium cepa), before and after biodegradation, was also considered. The potential production of rhamnolipidic biosurfactants in ricotta whey as an alternative substrate yielded 0.45 g L-1. Monitoring the biodegradation of hydrocarbons was performed by colorimetric assays using the both DCPIP and TTC redox indicators. Quantification was performed by gas chromatography coupled with mass spectrometry (GC / MS). The colorimetric tests were efficient and quite effective to verify the bacterial activity, indicating the potential of the microorganism to degrade these compounds. This fact was evidenced by GC / MS analysis. The plasmid TOL pWW0 found naturally in the bacterial line P. putida CCMI 852, gives the cells the ability to degrade hydrocarbons present in gasoline more easily relative to diesel oil. P. putida CCMI 852 was not able to metabolize benzene, nor individually, or in mixtures, indicating that the route of degradation of this specific strain is the TOL route. In the BTE(o-)X mixture, benzene caused a negative effect on the degradation of toluene, which had a degradation rate of 33.5% lower than its individual ... (Complete abstract click electronic access below) / Doutor

Plants accumulate and store proteins in protein storage vacuoles (PSVs) during seed development and maturation. Upon seed germination, these storage proteins are mobilized to provide nutrients for seedling growth. However, little is known about the molecular mechanisms of protein degradation during seed germination and post-germination. Here I test the hypothesis that vacuolar sorting receptor (VSR) proteins play a role in mediating protein degradation in germinating and post-germination seeds. It is demonstrated that both VSR proteins and hydrolytic enzymes are synthesized de novo during mung bean seed germination and post-germination. Immunogold electron microscopy (EM) with VSR antibodies demonstrates that VSRs mainly locate to the peripheral membrane of multivesicular bodies (MVBs), presumably as recycling receptors in Day-1 germinating seeds, but become internalized to the MVB lumen, presumably for degradation at Day-3 post-germination. Chemical cross-linking and immunoprecipitation with VSR antibodies have identified the cysteine protease aleurain as a specific VSR-interacting protein in germinating and post-germination seeds. Further immunogold EM studies demonstrate that VSR and aleurain colocalize to MVBs, as well as PSVs in germinating and post-germination seeds. Thus, MVBs in germinating and post-germination seeds exercise dual functions: as a storage compartment for proteases that are physically separated from PSVs in the mature seed, and as an intermediate compartment for VSR-mediated delivery of proteases from the Golgi apparatus to the PSV for protein degradation during seed germination and post-germination. / Storage proteins synthesized during seed development are transported to PSVs for storage. However, relatively little is known about the mechanisms of storage protein transport. A putative VSR-interacting protein termed S2 was identified as mung bean 8S globulin. Thus, I test the hypothesis that VSR proteins may be involved in storage protein transport to PSVs in developing mung bean seeds. Immunogold EM with 52 (8S globulin) antibody demonstrates that transport of 8S globulin to PSVs is Golgi-mediated, involving dense vesicle (DV) and a novel prevacuolar compartment (PVC). The novel PVC consists of storage protein aggregates and small internal vesicles. Immunogold EM with S2 (8S globulin) antibody demonstrates that MVBs contain 8S globulin at early stage of seed development. Further immunogold EM studies demonstrate that VSR and 8S globulin colocalize to DVs and the novel PVCs. In vitro binding study demonstrates that calcium ion can stabilize interaction between VSRs and 8S globulin. Thus, VSR proteins may mediate storage protein transport to PSVs via a novel PVC. / Wang, Junqi. / "March 2007." / Adviser: Jiang Liwen. / Source: Dissertation Abstracts International, Volume: 69-01, Section: B, page: 0052. / Thesis (Ph.D.)--Chinese University of Hong Kong, 2007. / Includes bibliographical references (p. 120-131). / Electronic reproduction. Hong Kong : Chinese University of Hong Kong, [2012] System requirements: Adobe Acrobat Reader. Available via World Wide Web. / Electronic reproduction. [Ann Arbor, MI] : ProQuest Information and Learning, [200-] System requirements: Adobe Acrobat Reader. Available via World Wide Web. / Abstracts in English and Chinese. / School code: 1307.

by Yung-Ho Chow. / Thesis (M.Phil.)--Chinese University of Hong Kong, 1997. / Includes bibliographical references (leaves 162-173). / ACKNOWLEDGEMENT --- p.i / ABSTRACT --- p.ii / LIST OF TABLES --- p.iii / LIST OF FIGURES --- p.iv / ABBREVIATION --- p.vi / Chapter CHAPTER 1 --- INTRODUCTION --- p.1 / Chapter 1.1 --- Azo dyes --- p.3 / Chapter 1.2 --- Chemistry of azo dyes --- p.3 / Chapter 1.2.1 --- Synthesis of azo dyes --- p.3 / Chapter 1.2.2 --- Oxidation and reduction --- p.4 / Chapter 1.2.3 --- Dyeing --- p.4 / Chapter 1.2.4 --- Staining to biological materials --- p.5 / Chapter 1.3 --- Toxicity of azo dyes --- p.5 / Chapter 1.3.1 --- Toxicity to mammals --- p.6 / Chapter 1.3.2 --- Toxicity to microorganisms --- p.6 / Chapter 1.4 --- Degradation of azo dyes --- p.9 / Chapter 1.4.1 --- Degradation of azo dyes by mammalian system --- p.9 / Chapter 1.4.2 --- Degradation of azo dyes by fungi system --- p.10 / Chapter 1.4.3 --- Degradation of azo dyes by bacteria --- p.11 / Chapter 1.4.3.1 --- Requirement of cofactors --- p.12 / Chapter 1.4.3.2 --- Effect of oxygen --- p.13 / Chapter 1.4.3.3 --- Effect of cell permeability --- p.14 / Chapter 1.4.3.4 --- Redox potential and rate of dye degradation --- p.15 / Chapter 1.4.3.5 --- Rate of dye degradation --- p.15 / Chapter 1.4.4 --- Azo-reductase --- p.18 / Chapter 1.4.4.1 --- Microsomal azo-reductase --- p.18 / Chapter 1.4.4.2 --- Bacterial azo-reductase --- p.19 / Chapter 1.5 --- Immobilization of microorganisms --- p.19 / Chapter 1.5.1 --- Gel matrix for entrapment --- p.20 / Chapter 1.5.2 --- Effect of gel entrapment to microbial cells --- p.21 / Chapter 1.5.2.1 --- Reduced diffusion of substrates in gel --- p.22 / Chapter 1.5.2.2 --- Effects in growth patterns --- p.22 / Chapter 1.5.2.3 --- Protection of entrapped microbial cells --- p.23 / Chapter 1.5.2.4 --- Increase metabolic activities --- p.26 / Chapter 1.5.2.5 --- Reduction of water activity --- p.27 / Chapter 1.5.2.6 --- Prolongation of products formation --- p.27 / Chapter 1.6 --- Application of immobilized microorganisms in bio-remediation of azo dyes --- p.28 / Chapter 1.7 --- Purpose of study --- p.28 / Chapter CHAPTER 2 --- MATERIALS AND METHODS --- p.29 / Chapter 2.1 --- Materials --- p.31 / Chapter 2.1.1 --- Chemicals --- p.31 / Chapter 2.1.2 --- Bacteria --- p.36 / Chapter 2.1.3 --- Instruments --- p.36 / Chapter 2.1.4 --- Media --- p.37 / Chapter 2.1.4.1 --- Luria Broth medium --- p.37 / Chapter 2.1.4.2 --- Minimal medium --- p.37 / Chapter 2.2 --- Methods --- p.38 / Chapter 2.2.1 --- Culture of Pseudomonas sp. ADD16-2 --- p.38 / Chapter 2.2.2 --- Purification and characterization of azo-reductase --- p.38 / Chapter 2.2.2.1 --- Preparation of crude extract --- p.38 / Chapter 2.2.2.2 --- Purification of azo-reductase --- p.39 / Chapter 2.2.2.2a --- Preparation of SDS-polyacrylamide gel --- p.40 / Chapter 2.2.2.2b --- Sample preparation and application --- p.41 / Chapter 2.2.2.2c --- Electrophoresis condition --- p.41 / Chapter 2.2.2.2d --- Staining of gel by Commasie blue --- p.41 / Chapter 2.2.2.3 --- Measurement of azo-reductase activity --- p.41 / Chapter 2.2.2.4 --- Determination of effect of pH to azo- reductase activity --- p.42 / Chapter 2.2.3 --- Measurement of azo dye decolourization rate by whole cells of Pseudomonas sp. ADD16-2 --- p.42 / Chapter 2.2.3.1 --- Preparation of cells --- p.42 / Chapter 2.2.3.2 --- Measurement of azo dye decolourization rate --- p.43 / Chapter 2.2.4 --- Measurement of azo dye decolourization rate by crude extract of Pseudomonas sp. ADD16-2 --- p.43 / Chapter 2.2.5 --- Determination of dye degradation products by High Performance Liquid Chromatography (HPLC) --- p.46 / Chapter 2.2.6 --- Measurement of redox potential of azo dyes --- p.47 / Chapter 2.2.7 --- Determination of the effect of cell permeation agents on dye degradation --- p.48 / Chapter 2.2.8 --- Determination of cell permeability --- p.48 / Chapter 2.2.9 --- To study the effect of the presence of dye degradation products or added aromatic amines to dye degradation --- p.49 / Chapter 2.2.9.1 --- Whole cell reactions --- p.50 / Chapter 2.2.9.2 --- Crude extract or purified azo-reductase reaction --- p.50 / Chapter 2.2.10 --- Immobilization of cells by different matrix --- p.50 / Chapter 2.2.10.1 --- Preparation of cells for immobilization --- p.50 / Chapter 2.2.10.2 --- Immobilization by calcium alginate --- p.51 / Chapter 2.2.10.3 --- Immobilization by K-carrageenan --- p.51 / Chapter 2.2.10.4 --- Immobilization by polyacrylamide gel --- p.52 / Chapter 2.2.10.5 --- Immobilization by agarose gel --- p.52 / Chapter 2.2.10.6 --- Measurement of viability of immobilized cells --- p.53 / Chapter 2.2.10.7 --- Measurement of azo dye degradation rate in immobilized cell system --- p.53 / Chapter 2.2.10.8 --- Measurement of intracellular K in calcium alginate immobilized cells --- p.53 / Chapter 2.2.10.9 --- Long term batch culture of immobilized cells --- p.53 / Chapter 2.2.11 --- Determination of toxicities of azo dyes and aromatic amines --- p.54 / Chapter CHAPTER 3 --- RESULTS --- p.55 / Chapter 3.1 --- Purification of azo-reductase 、 --- p.56 / Chapter 3.2 --- Properties of azo-reductase --- p.63 / Chapter 3.3 --- Degradation of azo dyes --- p.73 / Chapter 3.3.1 --- Degradation profiles --- p.73 / Chapter 3.3.2 --- Products of dye degradation --- p.80 / Chapter 3.3.3 --- Effect of cell permeability on dye degradation rate --- p.94 / Chapter 3.3.4 --- Induction of dye degradation rate by prior dye degradation exercise or by direct addition of aromatic amines --- p.97 / Chapter 3.4 --- Effect of immobilization --- p.114 / Chapter 3.4.1 --- Effect of different immobilization matrix --- p.114 / Chapter 3.4.2 --- Toxicities of different azo dyes and aromatic amines to free and immobilized cells --- p.124 / Chapter 3.4.3 --- Effect of azo dyes and aromatic amines at high concentrations on free and on immobilized cells --- p.124 / Chapter CHAPTER 4 --- DISCUSSION --- p.145 / Chapter 4.1 --- Degradation of azo dyes by Pseudomonas sp. ADD16-2 --- p.146 / Chapter 4.2 --- Permeability of azo dyes in Pseudomonas sp. ADD 16-2 --- p.150 / Chapter 4.3 --- Induction of dye degradation rate --- p.155 / Chapter 4.4 --- Effect of immobilization --- p.159 / CONCLUSION --- p.161 / REFERENCE --- p.162 / APPENDIX --- p.174 / appendix 1 Structures of azo dyes that have similar structures to Orange G --- p.175 / appendix 2 Absorption profiles of azo dye degradation products taken at different time intervals --- p.178 / appendix 3 Effect of pre-incubation time to dye degradation rate of Orange I by Pseudomonas sp. ADD16-2 --- p.183 / appendix 4 Effect of calcium ions (0-0.2 M) to (A) dye degradation and (B) viability of cells --- p.185 / appendix 5 Effect of ATP on induction effect of Orange I on whole cells of Pseudomonas sp. ADD16-2 --- p.187 / appendix 6 Summary of azo dyes that were degraded by Pseudomonas putida AD1 cells --- p.189

by Carmen, Ka-man Lai. / Thesis (M.Phil.)--Chinese University of Hong Kong, 1997. / Includes bibliographical references (leaves 237-269). / Abstract also in Chinese. / Acknowledgments --- p.i / Abstract --- p.ii / List of Figures --- p.vi / List of Tables --- p.xii / Chapter 1 --- Introduction --- p.1 / Chapter 1.1 --- History of development of textile dyes --- p.1 / Chapter 1.2 --- Development of azo dyes --- p.2 / Chapter 1.3 --- Chemistry of color and dyes --- p.4 / Chapter 1.4 --- Classification of textile dyes --- p.12 / Chapter 1.5 --- Reactive dyes --- p.19 / Chapter 1.6 --- General properties of fibres --- p.21 / Chapter 1.7 --- Dye-fibre bonds --- p.27 / Chapter 1.8 --- Ecological aspect and toxicity of dyes --- p.32 / Chapter 1.9 --- Physical and chemical methods --- p.47 / Chapter 1.9.1 --- Physical methods --- p.48 / Chapter 1.9.2 --- Chemical methods --- p.51 / Chapter 1.10 --- Biological methods --- p.57 / Chapter 1.10.1 --- Biosorption --- p.58 / Chapter 1.10.2 --- Biodegradation --- p.62 / Chapter 2 --- Objectives --- p.71 / Chapter 3 --- Materials and Methods --- p.74 / Chapter 3.1 --- Source of materials --- p.74 / Chapter 3.1.1 --- Selected dyes --- p.74 / Chapter 3.1.2 --- "Adsorbents (Pseudomonas sp. K-l, activated carbon and fly ash)" --- p.74 / Chapter 3.1.3 --- Identification of procion red MX-5B-degrading fungus --- p.79 / Chapter 3.2 --- Isolation and selection of microorganisms for biosorption and biodegradation --- p.79 / Chapter 3.3 --- Effect of growth phase of Pseudomonas sp. K-l on the dye adsorption capacity --- p.81 / Chapter 3.4 --- Effect of growth conditions (age of inoculum and agitation rate) of Pseudomonas sp. K-l on the dye adsorption capacity --- p.81 / Chapter 3.5 --- Preparation of Pseudomonas sp. K-l for biosorption --- p.82 / Chapter 3.6 --- "Removal capacity of adsorbents (Pseudomonas sp. K-l, activated carbon and fly ash) for different azo and non-azo dyes" --- p.83 / Chapter 3.7 --- "Effect of physico-chemical parameters (pH, agitation rate and temperature) on procion red MX-5B and remazol brilliant violet 5R removal capacities of different adsorbents (Pseudomonas sp K-l, activated carbon and fly ash)" --- p.83 / Chapter 3.8 --- "Effect of dye concentration on the removal capacity of procion red MX-5B and remazol brilliant violet 5R of different adsorbents (Pseudomonas sp. K-l, activated carbon and fly ash)" --- p.85 / Chapter 3.9 --- Optimization of growth yield and dye removal capacity of Pseudomonas sp. K-1 --- p.87 / Chapter 3.9.1 --- Effect of agitation rate and nutrient contents on the growth yield of Pseudomonas sp. K-l --- p.87 / Chapter 3.9.2 --- Effect of glucose concentration on the growth yield and dye removal capacity of Pseudomonas sp. K-l --- p.87 / Chapter 3.9.3 --- Effect of volume of inoculum from 2.5 mg/1 of glucose screening culture on procion red MX-5B removal capacity of Pseudomonas sp. K-l --- p.89 / Chapter 3.10 --- "Study on the surface structure of adsorbents (Pseudomonas sp. K-1, activated carbon and fly ash) by scanning electron microscopy" --- p.89 / Chapter 3.11 --- Effect of temperature on the growth of Geotrichum candidum CU-1 on complete medium plate --- p.90 / Chapter 3.12 --- Effect of agitation rate on the growth of Geotrichum candidum CU-1 in complete medium --- p.90 / Chapter 3.13 --- Effect of age of Geotrichum candidum CU-1 culture on the dye removal efficiency (RE) of procion red MX-5B --- p.90 / Chapter 3.14 --- Preparation of mycelia of Geotrichum candidum CU-1 for biosorption and biodegradation --- p.91 / Chapter 3.15 --- Removal efficiency of Geotrichum candidum CU-1 for different azo and non-azo dyes --- p.92 / Chapter 3.16 --- "Effect of physico-chemical parameters (pH, agitation rate and temperature) on procion red MX-5B removal efficiency of Geotrichum candidum CU-1 under aerobic and anaerobic conditions" --- p.92 / Chapter 3.16.1 --- pH --- p.92 / Chapter 3.16.2 --- Agitation rate --- p.93 / Chapter 3.16.3 --- Temperature --- p.94 / Chapter 3.17 --- Effect of glucose concentration on procion red MX-5B removal efficiency of Geotrichum candidum CU-1 --- p.94 / Chapter 3.18 --- Effect of pH on procion red MX-5B removal efficiency of Geotrichum candidum CU-1 with the addition of glucose --- p.95 / Chapter 3.19 --- Effect of procion red MX-5B concentration on the dye removal efficiency of Geotrichum candidum CU-1 under aerobic and anaerobic conditions --- p.95 / Chapter 3.20 --- Dye removal efficiency of Geotrichum candidum CU-1 in a recycle system --- p.96 / Chapter 3.21 --- Recovery of Geotrichum candidum CU-1 mycelia for biodegradation --- p.96 / Chapter 3.22 --- Effect of procion red MX-5B concentration on the growth of Geotrichum candidum CU-1 in complete medium --- p.97 / Chapter 3.23 --- Microtox® test --- p.97 / Chapter 3.24 --- Determination of the degradation products of procion red MX-5B by Geotrichum candidum CU-1 using high performance liquid chromatography (HPLC) --- p.98 / Chapter 3.25 --- Determination of the degradation products of procion red MX-5B by Ti2O and H2O2 photocatalytic method using high performance liquid chromatography (HPLC) --- p.100 / Chapter 3.26 --- Integration of biosorption and biodegradation --- p.100 / Chapter 3.26.1 --- Pseudomonas sp. K-l and Geotrichum candidum CU-1 --- p.100 / Chapter 3.26.2 --- Pseudomonas sp. K-l and Geotrichum candidum CU-1 in dye solution --- p.100 / Chapter 3.26.3 --- Effect of H2O2 on the adsorbed procion red MX-5B removal capacity by Geotrichum candidum CU-1 --- p.100 / Chapter 4 --- Results --- p.102 / Chapter 4.1 --- Isolation and selection of microorganisms for biosorption and biodegradation --- p.102 / Chapter 4.1.1 --- Dye-contaminated sediment in Tuen Mun River --- p.102 / Chapter 4.1.2 --- Dye-contaminated sediment in Yuen Long River --- p.102 / Chapter 4.1.3 --- Activated sludge from Shatin Sewage Treatment Works --- p.102 / Chapter 4.1.4 --- Air sample from a laboratory --- p.105 / Chapter 4.2 --- Identification of procion red MX-5B-degrading fungus --- p.105 / Chapter 4.3 --- Effect of growth phase of Pseudomonas sp. K-l on the dye adsorption capacity --- p.105 / Chapter 4.4 --- Effect of growth conditions (age of inoculum and agitation rate) of Pseudomonas sp. K-l on the dye adsorption capacity --- p.111 / Chapter 4.4.1 --- Age of inoculum --- p.111 / Chapter 4.4.2 --- Agitation rate --- p.111 / Chapter 4.5 --- "Removal capacity of adsorbents (Pseudomonas sp. K-l, activated carbon and fly ash) for different azo and non-azo dyes" --- p.111 / Chapter 4.6 --- "Effect of physico-chemical parameters (pH, agitation rate and temperature) on procion red MX-5B and remazol brilliant violet 5R removal capacities of different adsorbents" --- p.116 / Chapter 4.6.1 --- pH --- p.116 / Chapter 4.6.2 --- Agitation rate --- p.116 / Chapter 4.6.3 --- Temperature --- p.123 / Chapter 4.7 --- "Effect of dye concentration on the removal capacity of procion red MX-5B and remazol brilliant violet 5R of different adsorbents (Pseudomonas sp. K-l, activated carbon and fly ash)" --- p.123 / Chapter 4.8 --- Optimization of growth yield and dye removal capacity of Pseudomonas sp. K-1 --- p.131 / Chapter 4.8.1 --- Effect of agitation rate and nutrient contents on the growth yield of Pseudomonas sp. K-l --- p.131 / Chapter 4.8.2 --- Effect of glucose concentration on the growth yield and dye removal capacity of Pseudomonas sp. K-l --- p.131 / Chapter 4.8.3 --- Effect of volume of inoculum from 2.5 mg/1 of glucose screening culture on procion red MX-5B removal capacity of Pseudomonas sp. K-l --- p.134 / Chapter 4.9 --- "Study on the surface structure of adsorbents (Pseudomonas sp. K-l, activated carbon and fly ash) by scanning electron microscopy" --- p.134 / Chapter 4.9.1 --- Pseudomonas sp. K-l --- p.134 / Chapter 4.9.2 --- Activated carbon --- p.134 / Chapter 4.9.3 --- Fly ash --- p.134 / Chapter 4.10 --- Effect of temperature on the growth of Geotrichum candidum CU-1 on complete medium plate --- p.138 / Chapter 4.11 --- Effect of agitation rate on the growth of Geotrichum candidum CU-1 in complete medium --- p.138 / Chapter 4.12 --- Effect of age of Geotrichum candidum CU-1 culture on the dye removal efficiency of procion red MX-5B --- p.138 / Chapter 4.13 --- Removal efficiency of Geotrichum candidum CU-1 for different azo and non-azo dyes --- p.145 / Chapter 4.14 --- "Effect of physico-chemical parameters (pH, agitation rate and temperature) on procion red MX-5B removal efficiency of Geotrichum candidum CU-1 under aerobic and anaerobic conditions" --- p.145 / Chapter 4.14.1 --- pH --- p.145 / Chapter 4.14.2 --- Agitation rate --- p.150 / Chapter 4.14.3 --- Temperature --- p.150 / Chapter 4.15 --- Effect of glucose concentration on procion red MX-5B removal efficiency of Geotrichum candidum CU-1 --- p.155 / Chapter 4.16 --- Effect of pH on procion red MX-5B removal efficiency of Geotrichum candidum CU-1 with the addition of glucose --- p.155 / Chapter 4.17 --- Effect of procion red MX-5B concentration on the dye removal efficiency of Geotrichum candidum CU-1 under aerobic and anaerobic conditions --- p.158 / Chapter 4.18 --- Dye removal efficiency of Geotrichum candidum CU-1 in a recycle system --- p.164 / Chapter 4.19 --- Recovery of Geotrichum candidum CU-1 mycelia for biodegradation --- p.164 / Chapter 4.20 --- Effect of procion red MX-5B concentration on the growth of Geotrichum candidum CU-1 in complete medium --- p.164 / Chapter 4.21 --- Microtox® test --- p.168 / Chapter 4.22 --- Determination of the degradation products of procion red MX-5B by Geotrichum candidum CU-1 using high performance liquid chromatography (HPLC) --- p.168 / Chapter 4.23 --- Integration of biosorption and biodegradation --- p.178 / Chapter 4.23.1 --- Pseudomonas sp. K-l and Geotrichum candidum CU-1 --- p.178 / Chapter 4.23.2 --- Pseudomonas sp. K-l and Geotrichum candidum CU-1 in dye solution --- p.178 / Chapter 4.23.3 --- Effect of H202 on the adsorbed procion red MX-5B removal capacity by Geotrichum candidum CU-1 --- p.178 / Chapter 5 --- Discussion --- p.180 / Chapter 5.1 --- Isolation and selection of microorganisms for biosorption and biodegradation --- p.180 / Chapter 5.2 --- Identification of procion red MX-5B-degrading fungus --- p.182 / Chapter 5.3 --- Effect of growth phase of Pseudomonas sp. K-l on the dye adsorption capacity --- p.184 / Chapter 5.4 --- Effect of growth conditions (age of inoculum and agitation rate) of Pseudomonas sp. K-l on the dye adsorption capacity --- p.187 / Chapter 5.4.1 --- Age of inoculum --- p.187 / Chapter 5.4.2 --- Agitation rate --- p.188 / Chapter 5.5 --- Preparation of Pseudomonas sp. K-l for dye adsorption --- p.188 / Chapter 5.6 --- "Removal capacity of adsorbents (Pseudomonas sp. K-l, activated carbon and fly ash) for different azo and non-azo dyes" --- p.189 / Chapter 5.7 --- "Effect of physico-chemical parameters (pH, agitation rate and temperature) on procion red MX-5B and remazol brilliant violet 5R removal capacities of different adsorbents" --- p.191 / Chapter 5.7.1 --- pH --- p.191 / Chapter 5.7.2 --- Agitation rate --- p.193 / Chapter 5.7.3 --- Temperature --- p.194 / Chapter 5.8 --- "Effect of dye concentration on the removal capacity of procion red MX-5B and remazol brilliant violet 5R of different adsorbents (Pseudomonas sp. K-l, activated carbon and fly ash)" --- p.195 / Chapter 5.9 --- Optimization of growth yield and dye removal capacity of Pseudomonas sp. K-l --- p.199 / Chapter 5.9.1 --- Effect of agitation rate and nutrient contents on the growth yield of Pseudomonas sp. K-l --- p.1197 / Chapter 5.9.2 --- Effect of glucose concentration on the growth yield and dye --- p.201 / Chapter 5.9.3 --- Effect of volume of inoculum from 2.5 mg/1 of glucose screening culture on procion red MX-5B removal capacity of Pseudomonas sp. K-l --- p.202 / Chapter 5.10 --- "Study on the surface structure of adsorbents (Pseudomonas sp. K-l, activated carbon and fly ash) by scanning electron microscopy" --- p.203 / Chapter 5.10.1 --- Pseudomonas sp. K-l --- p.203 / Chapter 5.10.2 --- Activated carbon --- p.203 / Chapter 5.10.3 --- Fly ash --- p.203 / Chapter 5.11 --- Effect of temperature on the growth of Geotrichum candidum CU-1 on complete medium plate --- p.204 / Chapter 5.12 --- Effect of agitation rate on the growth of Geotrichum candidum CU-1 in complete medium --- p.204 / Chapter 5.13 --- Effect of age of Geotrichum candidum CU-1 culture on the dye removal efficiency of procion red MX-5B --- p.205 / Chapter 5.14 --- Removal efficiency of Geotrichum candidum CU-1 for different azo and non-azo dyes --- p.206 / Chapter 5.15 --- "Effect of physico-chemical parameters (pH, agitation rate and temperature) on procion red MX-5B removal efficiency of Geotrichum candidum CU-1 under aerobic and anaerobic conditions" --- p.207 / Chapter 5.15.1 --- pH --- p.207 / Chapter 5.15.2 --- Agitation rate --- p.210 / Chapter 5.15.3 --- Temperature --- p.210 / Chapter 5.16 --- Effect of glucose concentration on procion red MX-5B removal efficiency of Geotrichum candidum CU-1 --- p.212 / Chapter 5.17 --- Effect of pH on procion red MX-5B removal efficiency of Geotrichum candidum CU-1 with the addition of glucose --- p.213 / Chapter 5.18 --- Effect of procion red MX-5B concentration on the dye removal efficiency of Geotrichum candidum CU-1 under aerobic and anaerobic conditions --- p.215 / Chapter 5.19 --- Dye removal efficiency of Geotrichum candidum CU-1 in a recycle system --- p.217 / Chapter 5.20 --- Recovery of Geotrichum candidum CU-1 mycelia for biodegradation --- p.219 / Chapter 5.21 --- Effect of procion red MX-5B concentration on the growth of Geotrichum candidum CU-1 in complete medium --- p.221 / Chapter 5.22 --- Microtox® test --- p.221 / Chapter 5.23 --- Determination of the degradation products of procion red MX-5B by Geotrichum candidum CU-1 using high performance liquid chromatography (HPLC) --- p.225 / Chapter 5.24 --- Integration of biosorption and biodegradation --- p.229 / Chapter 6 --- Conclusion --- p.233 / Chapter 7 --- References --- p.237 / Appendix 1 --- p.270 / Appendix 2 --- p.271

by Diao, Zhenyu = 模板辅助下制备有生物形态的MoO₃化合物以及它对降解甲基紫的催化作用 / 刁振玉. / Thesis (M.Phil.)--Chinese University of Hong Kong, 2010. / Includes bibliographical references. / Abstracts in English and Chinese. / by Diao, Zhenyu = Mo ban fu zhu xia zhi bei you sheng wu xing tai de MoO₃ hua he wu yi ji ta dui jiang jie jia ji zi de cui hua zuo yong / Diao Zhenyu. / Abstract --- p.I / 摘要 --- p.II / Acknowledgement --- p.III / Table of contents --- p.IV / List of figures --- p.VII / List of tables --- p.X / Chapter Chapter 1 --- Introduction --- p.1 / Chapter 1.1 --- Biomorphic materials --- p.1 / Chapter 1.2 --- Semiconductor catalysts --- p.2 / Chapter 1.3 --- Methyl violet --- p.3 / Chapter 1.4 --- Photocatalysis --- p.4 / Chapter 1.5 --- Synthesis of biomorphic catalysts --- p.8 / Chapter 1.6 --- Objectives and thesis layout --- p.10 / References / Chapter Chapter 2 --- Methodology and Instrumentation --- p.17 / Chapter 2.1 --- Sample preparation --- p.17 / Chapter 2.1.1 --- Synthesis --- p.17 / Chapter 2.1.2 --- Paper templates and precursors --- p.18 / Chapter 2.2 --- Characterization --- p.18 / Chapter 2.2.1 --- Scanning electron microscope (SEM) --- p.18 / Chapter 2.2.2 --- X-ray powder diffractometry (XRD) --- p.20 / Chapter 2.2.3 --- Fourier transform infrared (FTIR) spectroscopy --- p.21 / Chapter 2.2.4 --- Differential thermal analysis (DTA) --- p.23 / Chapter 2.2.5 --- Thermogravimetric analysis (TGA) --- p.24 / Chapter 2.2.6 --- Ultraviolet-Visible spectroscopy (UV-Vis) --- p.24 / Chapter 2.3 --- Catalytic performance --- p.26 / References --- p.26 / Chapter Chapter 3 --- Results Introduction --- p.30 / Chapter 3.1 --- Paper template --- p.31 / Chapter 3.1.1 --- Thermal properties --- p.31 / Chapter 3.1.2 --- Composition of paper template --- p.32 / Chapter 3.1.3 --- Morphology of paper --- p.35 / Chapter 3.2 --- Chemical precursors --- p.40 / Chapter 3.3 --- Infiltrated paper templates --- p.43 / Chapter 3.4 --- Biomorphic products --- p.46 / Chapter 3.4.1. --- Influence of annealing temperature --- p.46 / Chapter 3.4.1.1 --- Phase and composition --- p.46 / Chapter 3.4.1.2. --- Surface morphology --- p.48 / Chapter 3.4.2 --- Effects of annealing durations --- p.50 / Chapter 3.4.2.1 --- Phase and composition --- p.50 / Chapter 3.4.2.2 --- Surface morphology --- p.54 / Chapter 3.5 --- Formation mechanism --- p.56 / References --- p.57 / Chapter Chapter 4 --- Catalytic performance Introduction --- p.59 / Chapter 4.1 --- Degradation of MV under visible light --- p.60 / Chapter 4-2 --- Effects of the UV irradiation on MV --- p.64 / Chapter 4-3 --- Degradation of MV dye using M0O3 under UV light --- p.65 / Chapter 4.4 --- Mechanism of photocatalysis --- p.69 / References --- p.70 / Chapter Chapter 5 --- Conclusions and future work --- p.72 / Chapter 5.1 --- Conclusions --- p.72 / Chapter 5.2 --- Future work --- p.73 / References --- p.74

Bacterial strain Pseudomonas sp. ADP is capable of degrading atrazine via an enzymatic pathway in six sequential steps to yield carbon dioxide and ammonia. Atrazine is a persistent herbicide that frequently contaminates soil, drinking water, and ground water throughout areas of heavy use in the United States. A biological remediation approach using Pseudomonas sp. APD is considered as an effective, cost-efficient, and environmentally conscious method of decreasing atrazine concentration in areas of high contamination. Each enzyme in the degradation pathway is encoded by a corresponding gene, AtzA-AtzF, and is located on a self-transmissible 108-kb plasmid. Due to their prevalence in nature, and their unique genetic and physical characteristics, biofilms are of great interest in the field of bioremediation. Biofilms exhibit high tolerance for harsh environmental stressors/conditions, prodigious potential for recalcitrant compound entrapment via an extracellular polymeric matrix, quorum sensing, and increased horizontal gene transfer compared to their planktonic counterparts. Despite frequent genetic and chemical analyses performed on atrazine-degrading genes on planktonic cells of strain Pseudomonas sp. APD, the genetics and degradation potential of Pseudomonas sp. ADP biofilms is relatively unexplored. Real-time quantitative PCR was used to differentiate the expression of six genes involved in the process of atrazine degradation. Relative expression experiments revealed no statistically significant difference in the expression of atrazine-degrading genes in Pseudomonas sp. ADP cells grown as biofilms relative to Pseudomonas sp. ADP cells grown as planktonic cells. In biofilms alone, the expression of genes AtzDEF was differentiated via temperature of biofilm growth in cells grown at 25, 30, and 37 degrees. Analytical techniques, including GC-MS and HPLC, were used to elucidate atrazine remediation potential of Pseudomonas sp. ADP biofilms and our previously collected genetic data. Stable decreases in atrazine degradation following a first-order kinetic model have been demonstrated for planktonic cells compared to a complex degradation pattern, including transient increases, observed for corresponding biofilm-mediated cells. This is attributed to the unique structure of the biofilm and the potential of atrazine to be entrapped in the substances of the extracellular polymeric matrix and subsequently released into the effluent. Overall, the biodegradation efficiency was higher for Pseudomonas sp. ADP biofilm-mediated cells compared to their planktonic counterparts. A novel methodology of using confocal microscopy and in situ reverse transcription was proposed for optimization to visualize the expression of atrazine-degrading genes in fixed Pseudomonas sp. ADP biofilms. The sugar composition of Pseudomonas sp. ADP was evaluated using fluorescent lectin binding analysis and was determined to exhibit a prominent level of diversity and dependent upon growth medium. The results from these experiments will play a role in application of biofilms grown in bioreactors for atrazine remediation throughout areas of persistent and high contamination throughout the US. The new step in methodology development of an in situ visual gene expression technique can be extended to bioremediation of alternate recalcitrant compounds. The results may also be aid progress in alternate biofilm-related studies in medicine & human health, metallurgy, and engineering.