by Deng Yu. / Thesis (M.Phil.)--Chinese University of Hong Kong, 1999. / Includes bibliographical references (leaves 111-120). / Abstract also in Chinese. / Acknowledgements --- p.i / Abstract --- p.ii / List of Abbreviations --- p.viii / List of Tables --- p.ix / List of Figures --- p.x / Chapter 1 --- Introduction / Chapter 1.1 --- Primary nitrogen metabolism in fungi --- p.1 / Chapter 1.1.1 --- Ammonium assimilation --- p.4 / Chapter 1.1.2 --- Regulation of ammonium assimilating enzymes --- p.8 / Chapter 1.2 --- Relevant central carbon metabolism in fungi --- p.11 / Chapter 1.2.1 --- Glyoxylate cycle and isocitrate metabolism --- p.11 / Chapter 1.2.2 --- GABA shunt --- p.15 / Chapter 1.3 --- Relationship between nitrogen metabolism and fungi morphogenesis --- p.15 / Chapter 1.4 --- General background of Volvariella volvacea --- p.17 / Chapter 1.5 --- Objectives of the study --- p.20 / Chapter 2 --- Materials and methods / Chapter 2.1 --- Organism --- p.22 / Chapter 2.2 --- Growth media --- p.22 / Chapter 2.2.1 --- Basal medium --- p.22 / Chapter 2.2.2 --- Solid-state cultivation --- p.23 / Chapter 2.3 --- Effect of different nitrogen sources on the mycelial growth of V volvacea in submerged culture --- p.26 / Chapter 2.4 --- Effect of different carbon and nitrogen sources and concentrations on the production of selected enzymes involved in central carbon and nitrogen metabolism --- p.27 / Chapter 2.5 --- Enzyme extraction --- p.28 / Chapter 2.6 --- Enzyme assays --- p.28 / Chapter 2.6.1 --- NAD-dependent glutamate dehydrogenase --- p.28 / Chapter 2.6.2 --- NADP-dependent glutamate dehydrogenase --- p.29 / Chapter 2.6.3 --- NAD- dependent isocitrate dehydrogenase --- p.29 / Chapter 2.6.4 --- Isocitrate lyase --- p.30 / Chapter 2.7 --- Protein determination --- p.30 / Chapter 2.8 --- Determination of optimum pH for enzyme assays --- p.31 / Chapter 2.9 --- Determination of optimum temperatures for enzyme assays --- p.31 / Chapter 2.10 --- Transfer experiments --- p.31 / Chapter 2.11 --- Enzyme stability --- p.32 / Chapter 2.12 --- Purification of NAD-dependent glutamate dehydrogenase --- p.33 / Chapter 2.12.1 --- Ammonium sulphate precipitation --- p.33 / Chapter 2.12.2 --- Ion exchange chromatography --- p.33 / Chapter 2.12.3 --- Ultrafiltrartion --- p.34 / Chapter 2.12.4 --- Gel filtration chromatography --- p.34 / Chapter 2.12.5 --- Affinity chromatography --- p.34 / Chapter 2.13 --- Electrophoresis --- p.35 / Chapter 2.13.1 --- SDS polyacrylamide gel electrophoresis --- p.35 / Chapter 2.13.2 --- Native polyacrylamide gel electrophoresis --- p.35 / Chapter 2.13.3 --- Activity staining for NAD-dependent glutamate dehydrogenase --- p.36 / Chapter 2.13.4 --- Protein staining --- p.36 / Chapter 2.14 --- NAD-dependent glutamate dehydrogenase characterization studies --- p.37 / Chapter 2.14.1 --- Effect of substrate concentration --- p.37 / Chapter 2.14.2 --- Molecular weight determination --- p.37 / Chapter 2.14.2.1 --- Molecular weight determination by gel filtration chromatography --- p.37 / Chapter 2.14.2.2 --- Molecular weight determination by native PAGE --- p.38 / Chapter 2.14.2.3 --- Protein subunit molecular weight determination by SDS- PAGE --- p.38 / Chapter 3 --- Results / Chapter 3.1 --- Effect of different nitrogen sources on the mycelial growth of V. volvacea in submerged culture --- p.39 / Chapter 3.2 --- Optimum assay conditions for NAD-dependent glutamate dehydrogenase --- p.42 / Chapter 3.3 --- Optimum assay conditions for NADP-dependent glutamate dehydrogenase --- p.46 / Chapter 3.4 --- Optimum assay conditions for NAD-dependent isocitrate dehydrogenase --- p.50 / Chapter 3.5 --- Optimum assay conditions for isocitrate lyase --- p.54 / Chapter 3.6 --- Biomass production and enzyme activities in extracts of in vegetative mycelia grown with different nitrogen and carbon sources provided at different concentrations --- p.58 / Chapter 3.6.1 --- Mycelia growth under different conditions --- p.58 / Chapter 3.6.2 --- NAD- and NADP-dependent glutamate dehydrogenases in extracts of vegetative mycelia grown with different nitrogen and carbon sources provided at different conditions --- p.58 / Chapter 3.6.3 --- NAD-dependent isocitrate dehydrogenase and isocitrate lyase in vegetative mycelia grown with different nitrogen and carbon sources provided at different conditions --- p.64 / Chapter 3.7 --- Transfer experiments --- p.67 / Chapter 3.7.1 --- Activities of glutamate dehydrogenases in extracts of myceila transferred to media containing different carbon sources --- p.67 / Chapter 3.7.2 --- Effect of different carbon sources on the glutamate dehydrogenases in submerged cultures --- p.67 / Chapter 3.8 --- Glutamate dehydrogenase activity in various parts of the fruit body during different stages of fruit body development --- p.70 / Chapter 3.9 --- Stabilization of NAD-dependent glutamate dehydrogenase activity --- p.75 / Chapter 3.10 --- Purification of NAD-dependent glutamate dehydrogenase --- p.77 / Chapter 3.10.1 --- Ammonium sulphate precipitation --- p.77 / Chapter 3.10.2 --- Partial purification by column chromatography --- p.78 / Chapter 3.10.3 --- Electrophoretic determination of the protein profiles of crude extract and partially purified samples --- p.83 / Chapter 3.11 --- Characterization of partially purified NAD-dependent glutamate dehydrogenase from V. volvacea --- p.86 / Chapter 3.11.1 --- Optimum pH and temperature --- p.86 / Chapter 3.11.2 --- Kinetic parameters --- p.86 / Chapter 3.11.3 --- Molecular weight --- p.92 / Chapter 3.11.3.1 --- Molecular weight determination by gel filtration chromatography --- p.92 / Chapter 3.11.3.2 --- Molecular weight determination by native PAGE --- p.92 / Chapter 3.11.3.3 --- Subunit molecular weight determination by SDS-PAGE --- p.92 / Chapter 4 --- Discussion / Chapter 4.1 --- Nutrient nitrogen for the growth of Volvariella volvacea --- p.97 / Chapter 4.1.1 --- Mycelial growth on simple nitrogen compounds --- p.97 / Chapter 4.1.2 --- Nutrient nitrogen in mushroom compost --- p.98 / Chapter 4.2 --- Production and regulation of selected enzymes in vegetative mycelia --- p.98 / Chapter 4.2.1 --- Production and regulation of glutamate dehydrogenases --- p.98 / Chapter 4.2.2 --- Production and regulation of isocitrate dehydrogenase and isocitrate lyase --- p.103 / Chapter 4.3 --- Glutamate dehydrogenases and fruit body development --- p.104 / Chapter 4.4 --- Purification and characterization of NAD-dependent glutamate dehydrogenase --- p.105 / Chapter 4.4.1 --- Enzyme purification --- p.105 / Chapter 4.4.2 --- Enzyme stability --- p.106 / Chapter 4.4.3 --- Enzyme properties --- p.107 / Chapter 4.5 --- Future works: nitrogen metabolism and the growth of Vohariella volvacea --- p.109 / References --- p.111

by Shicheng Chen. / "July, 2003." / Thesis (Ph.D.)--Chinese University of Hong Kong, 2003. / Includes bibliographical references (p. 206-232). / Electronic reproduction. Hong Kong : Chinese University of Hong Kong, [2012] System requirements: Adobe Acrobat Reader. Available via World Wide Web. / Mode of access: World Wide Web. / Abstracts in English and Chinese.

Sandra J. Chapman. / Thesis (M.Phil.)--Chinese University of Hong Kong, 1994. / Includes bibliographical references (leaves 95-103). / Chapter 1. --- Introduction --- p.1 / Chapter 1.1 --- History of zinc --- p.1 / Chapter 1.2 --- The biological role of zinc --- p.2 / Chapter 1.3 --- Zinc toxicosis --- p.6 / Chapter 1.4 --- Mechanisms of zinc uptake and transport in fungi --- p.7 / Chapter 1.5 --- Bioremediation --- p.11 / Chapter 1.6 --- Uptake of heavy metals by fruit bodies of edible mushrooms --- p.13 / Chapter 1.7 --- Mushroom fungi selected for study --- p.15 / Chapter 1.8 --- Purpose of study --- p.17 / Chapter 2. --- Materials and Methods --- p.18 / Chapter 2.1 --- Organisms --- p.18 / Chapter 2.2 --- Media --- p.18 / Chapter 2.3 --- Media chelation --- p.20 / Chapter 2.4 --- Chemicals --- p.20 / Chapter 2.5 --- Zinc content of fruit bodies grown on substrates containing different concentrations of zinc --- p.21 / Chapter 2.5.1 --- Substrate preparation for V. volvacea inoculum --- p.21 / Chapter 2.5.2 --- Cultivation of V. volvacea fruit bodies --- p.21 / Chapter 2.5.3 --- Cultivation of P.sajor-caju fruit bodies --- p.22 / Chapter 2.5.4 --- Cultivation of L. edodes fruit bodies --- p.23 / Chapter 2.5.5 --- Preparation of biological material for atomic absorption spectrophotometry --- p.24 / Chapter 2.6 --- Effect of different concentrations of zinc on the growth of six mushroom fungi --- p.25 / Chapter 2.6.1 --- Radial growth study --- p.25 / Chapter 2.6.2 --- Biomass study --- p.26 / Chapter 2.7 --- Microscopic studies of V. volvacea --- p.27 / Chapter 2.7.1 --- "Coomassie Blue preparation, staining of V.volvacea hyphae" --- p.27 / Chapter 2.7.2 --- Dithizone staining of V. volvacea hyphae --- p.27 / Chapter 2.7.3 --- Fluorescence microscopy --- p.28 / Chapter 2.7.4 --- Scanning electron microscopy --- p.28 / Chapter 2.8 --- Preparation and analysis of V. volvacea proteins using gel electrophoresis --- p.29 / Chapter 3. --- Results --- p.33 / Chapter 3.1 --- Zinc Uptake by Fruit Bodies --- p.33 / Chapter 3.1.1 --- Uptake of zinc by V. volvacea --- p.33 / Chapter 3.1.2 --- Uptake of zinc by P. sajor-caju --- p.33 / Chapter 3.1.3 --- Uptake of zinc by L. edodes --- p.34 / Chapter 3.1.4 --- Symptoms of zinc toxicity in L. edodes --- p.44 / Chapter 3.2 --- Growth studies --- p.49 / Chapter 3.2.1 --- Radial growth measurements --- p.49 / Chapter 3.2.2 --- Biomass measurements --- p.56 / Chapter 3.2.3 --- Morphological alterations due to zinc observed with light and electron microscopy --- p.63 / Chapter 3.3 --- V. volvacea staining studies --- p.73 / Chapter 3.3.1 --- Protein staining using Coomassie Blue --- p.73 / Chapter 3.3.2 --- Zinc staining by dithizone and fluorescence staining by DAPI --- p.75 / Chapter 3.4 --- V. volvacea protein profile comparisons after gel electrophoresis --- p.81 / Chapter 4. --- Discussion --- p.83 / Chapter 4.1 --- Zinc uptake by fruit bodies / Chapter 4.1.1 --- Uptake of zinc by V. volvacea and P. sajor-caju fruit bodies --- p.83 / Chapter 4.1.2 --- Accumulation of zinc by L. edodes fruit bodies and mechanism of toxicity --- p.84 / Chapter 4.2 --- Effects of zinc on growth --- p.88 / Chapter 4.3 --- V. volvacea mechanisms of tolerance --- p.89 / Chapter 4.4 --- Differences in protein profiles of V. volvacea grown on different concentrations of zinc --- p.93 / Chapter 5. --- References

Sandra Jane Chapman. / "October 2002." / Thesis (Ph.D.)--Chinese University of Hong Kong, 2002. / Includes bibliographical references (p. 163-178). / Electronic reproduction. Hong Kong : Chinese University of Hong Kong, [2012] System requirements: Adobe Acrobat Reader. Available via World Wide Web. / Mode of access: World Wide Web. / Abstracts in English and Chinese.

Cai Yi Jin. / Thesis (M.Phil.)--Chinese University of Hong Kong, 1993. / Includes bibliographical references (leaves 118-128). / Chapter 1. --- Introduction / Chapter 1.1 --- Importance and Cultivation history of edible mushroom --- p.1 / Chapter 1.2 --- Variety and structure of growth substrates for mushroom --- p.4 / Chapter 1.3 --- Mushroom growth and substrate-degrading enzymes --- p.8 / Chapter 1.4 --- Purpose of study --- p.15 / Chapter 2. --- Methods and Materials / Chapter 2.1 --- Organisms --- p.17 / Chapter 2.2 --- Media --- p.17 / Chapter 2.3 --- Culture conditions --- p.21 / Chapter 2.3.1 --- Growth temperature --- p.21 / Chapter 2.3.2 --- Growth Studies --- p.21 / Chapter 2.3.2.1 --- Effect of pH on mycelial growth --- p.21 / Chapter 2.3.2.2 --- Effect of different carbon sources on mycelial growth --- p.21 / Chapter 2.3.2.3 --- Effect of lignin-related phenolic monomers and tannin derivatives on fungal growth --- p.22 / Chapter 2.3.3 --- Culture conditions for production of extracellular enzymes --- p.23 / Chapter 2.3.3.1 --- Tyrosinase --- p.23 / Chapter 2.3.3.2 --- Laccase --- p.23 / Chapter 2.3.3.3 --- Manganese-dependent Peroxidase and Lignin Peroxidase --- p.23 / Chapter 2.3.3.4 --- Cellulytic and Xylanolytic enzymes --- p.24 / Chapter 2.3.3.5 --- Lipase --- p.25 / Chapter 2.3.4 --- Culture conditions for studying properties of cellulases of V. volvacea --- p.26 / Chapter 2.3.4.1 --- CMCase --- p.26 / Chapter 2.3.4.2 --- "CMCase, FPase and β-Glucosidase" --- p.26 / Chapter 2.3.4.3 --- β-Glucosidase --- p.26 / Chapter 2.4 --- Enzyme assay --- p.27 / Chapter 2.4.1 --- Tyrosinase --- p.27 / Chapter 2.4.2 --- Laccase --- p.27 / Chapter a. --- o-Tolidine Method --- p.27 / Chapter b. --- ABTS Method --- p.28 / Chapter c. --- Syringaldazine Method --- p.28 / Chapter 2.4.3 --- Lignin peroxidase --- p.29 / Chapter 2.4.4 --- Manganese-dependent peroxidase --- p.29 / Chapter 2.4.5 --- Exoglucanase (avicelase) --- p.30 / Chapter 2.4.6 --- Endoglucanase (carboxymethylcellulase or CMCase) --- p.31 / Chapter 2.4.7 --- Filter paper digesting enzyme (FPase) --- p.32 / Chapter 2.4.8 --- P-Glucosidase --- p.32 / Chapter 2.4.9 --- Xylanase --- p.34 / Chapter 2.4.10 --- β-Xylosidase --- p.34 / Chapter 2.4.11 --- Lipase --- p.36 / Chapter 2.5 --- Other analytical methods --- p.36 / Chapter 2.5.1 --- Determination of phenol oxidase activity by the Bavendamm reaction --- p.36 / Chapter 2.5.2 --- Qualitative evaluation of CMCase by Congo red staining --- p.37 / Chapter 2.5.3 --- Effect of phenolic monomers and tannic acid on CMCase activity of V. volvacea --- p.38 / Chapter 2.5.4 --- Protein determination --- p.39 / Chapter 2.5.5 --- Non-denaturing gel electrophoresis pattern of fungal laccases --- p.39 / Chapter 2.6 --- Chemicals --- p.39 / Chapter 3. --- Results / Chapter 3.1 --- Growth and Nutritional characteristics --- p.44 / Chapter 3.1.1 --- Fungal growth on defined and non-defined culture media --- p.44 / Chapter 3.1.2 --- Effect of carbon source on fungal --- p.45 / Chapter 3.1.3 --- Effect of pH on fungal growth --- p.45 / Chapter 3.2 --- Effect of lignin-related phenolic monomers and tannin derivatives on fungal growth --- p.45 / Chapter 3.2.1 --- Effect of lignin-related phenolic monomers on fungal growth --- p.45 / Chapter 3.2.2 --- Effect of tannin derivatives on fungal growth --- p.61 / Chapter 3.3 --- Phenol Oxidase --- p.67 / Chapter 3.3.1 --- Phenol oxidase --- p.67 / Chapter 3.3.1.1 --- Guaiacol-reacting enzyme --- p.67 / Chapter 3.3.1.2 --- o-Anisidine oxidizing enzyme --- p.68 / Chapter 3.3.2 --- Tyrosinase --- p.69 / Chapter 3.3.3 --- Laccase --- p.69 / Chapter 3.3.3.1 --- "Laccase detected by o-Tolidine, ABTS Syringaldazine" --- p.69 / Chapter 3.3.3.2 --- Effect of pH on laccase activity --- p.69 / Chapter 3.4 --- Lignin-Transforming Enzymes --- p.73 / Chapter 3.4.1 --- Lignin peroxidase (LP) --- p.73 / Chapter 3.4.2 --- Manganese-dependent peroxidase (MnP) --- p.74 / Chapter 3.5 --- Cellulases --- p.78 / Chapter 3.5.1. --- Cellulases of V. volvacea --- p.78 / Chapter 3.5.1.1 --- Qualitative estimation of cellulose-degrading enzymes of V. volvacea grown on different substrates --- p.78 / Chapter 3.5.1.2 --- Influence of pH and temperature --- p.79 / Chapter 3.5.1.3 --- Cellulolytic activities in cultures grown on cellulose --- p.83 / Chapter 3.5.1.4 --- Cellulolytic activities in cultures grown on paddy straw --- p.91 / Chapter 3.5.1.5 --- β-Glucosidase activity in cultures grown on cellobiose --- p.91 / Chapter 3.5.1.6 --- Effect of lignin-related phenolic monomers and tannic acid on CMCase of V. volvacea --- p.95 / Chapter 3.5.2 --- Cellulases of P.sajor-caju --- p.96 / Chapter 3.5.3 --- Cellulases of L. edodes --- p.96 / Chapter 3.6 --- Xylanase --- p.96 / Chapter 3.6.1 --- "Xylanase of V. volvacea, strain V34" --- p.96 / Chapter 3.6.2 --- Xylanase of P.sajor-caju --- p.100 / Chapter 3.6.3 --- Xylanase of L. edodes --- p.100 / Chapter 3.7 --- Lipase of V. volvacea --- p.103 / Chapter 4. --- Discussion / Chapter 4.1. --- Carbon nutrition and pH for fungal growth --- p.104 / Chapter 4.1.1 --- Carbon nutrition --- p.104 / Chapter 4.1.2 --- pH --- p.104 / Chapter 4.2 --- "Effect of lignin-related phenolic monomers and tannin derivatives on fungal growth of L. edodes, P. sajor-caju and V, volvacea" --- p.105 / Chapter 4.2.1 --- Lignin-related phenolic monomers --- p.105 / Chapter 4.2.2 --- Tannin derivatives --- p.107 / Chapter 4.3 --- "Production of phenoloxidases by V. volvacea, L. edodes and P. sajor-caju" --- p.108 / Chapter 4.3.1 --- Guaiacol- and Anisidine reacting enzymes and Tyrosinase --- p.108 / Chapter 4.3.2 --- Laccase --- p.109 / Chapter 4.4. --- "Lignin-degrading Enzymes of V. volvacea, P. sajor-caju and L. edodes" --- p.110 / Chapter 4.5. --- "Cellulolytic and Hemicellulolytic Activity of V. volvacea, P.sajor-caju and L. edodes" --- p.113 / References --- p.118 / Appendix1 --- p.129