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APPENDIX A
Stains and solutions for microscopic examination of fungi
1. India ink: was used to observing gelatinous appendages of ascospores in
some fungal species.
2. Lactophenol: was routinely used for observing fungi and preparing
semipermanant slides. The components: phenol, which will kill any living
organisms; lactic acid which preserves fungal structures.
Phenol (crystals) 10 g
Lactic acid 10 ml
Glycerol 10 ml
Distilled water 10 ml
Dissolve 10 g of phenol in 10 ml distilled water (do not heat). Then add 10 ml
glycerol and 10 ml lactic acid.
3. Lactophenol cotton blue (LPCB): widely used for staining and observing
fungi. The preparation has three components: phenol, which will kill any live
organisms; lactic acid which preserves fungal structures, and cotton blue
which stains the chitin in the fungal cell walls.
Phenol (crystals) 20 g
Lactic acid 16 ml
Glycerol 31 ml
Distilled water 20 ml
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Dissolve phenol in distilled water, then add lactic acid and glycerol. Add 0.05
g Poirrier's (cotton) blue or acid fuchsin.
4. Melzer's reagent: specifically for amyloid and dextrinoid reactions in spores,
asci, hymenial tissues. The staining result use for identification of ascomycete
fungi.
Chloral hydrate 100 g
Potassium iodide 5 g
Iodine 1.5 g
Distilled water 100 ml
Agar medium
1. Corn meal agar (CMA)
Blend 50.0 g corn meal in 800 ml of distilled water. Leave overnight in the
refrigerator. Heat at 60 °C for one hour. Filter and make up volume to 1000
ml. Add 15.0 g agar and heat to dissolve, then autoclave for 15 minutes at 15
psi pressure-121 °C
2. Malt extract agar (MEA)
Agar 15.0 g
Glucose 20.0 g
Malt extract 20.0 g
Peptone 1.0 g
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Add components to distilled water and bring volume to 1000 ml. Mix
thoroughly and gently heat and bring to boiling. Autoclave for 15 minutes at
15 psi pressure-121 °C. Pour into sterile Petri dishes.
3. Poly R-478 agar (Pointing, 1999) (per liter)
Glucose 20 g
KH2PO4 1 g
C4H12N2O6 0.5 g
MgSO4.7H2O 0.5 g
CaCl2.2H2O 0.01 g
Yeast extract 0.01 g
CuSO4.5H2O 0.01 g
Fe2(SO4)3 0.001 g
MnSO4.H2O 0.001 g
Poly R-478 0.02 g
Agar 15 g
pH 5.5
4. Potato dextrose agar (PDA)
Glucose 20.0 g
Agar 15.0 g
Potato, infusion form 1000 ml
Preparation of potato, infusion form:
Peel and dice potatoes. Add 300 g of potato to 500 ml of distilled water.
Gently heat and bring to boiling. Continue boiling for 30 minutes. Filter
through gauze. Bring volume of filtrate to 1000 ml.
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Preparation of medium:
Add glucose and agar to 1000 ml of potato infusion. Mix, gently heat and
bring to boiling. Autoclave for 15 minutes at 15 psi pressure-121 °C.
5. Rose Bengal agar
Agar 15.0 g
Glucose 10.0 g
Malt extract agar 20.0 g
Rose Bengal 0.05 g
Chloramphenicol 10.0 ml
Preparation of chloramphenicol solution:
Add 0.10 g of chloramphenicol to distilled water and bring volume to 10.0 ml.
Mix thoroughly. Filter sterilize.
Preparation of medium:
Add components, except chloramphenicol solution, to distilled water and
bring volume to 990 ml. Mix thoroughly. Gently heat and bring to boiling.
Autoclave for 15 minutes at 15 psi pressure-121 °C. Cool to 45 °C.
Aseptically add sterile chloramphenicol solution. Mix thoroughly. Pour into
sterile Petri dishes.
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APPENDIX B
Reagents for molecular techniques
1. 2× CTAB buffer (50 ml)
Cetyltrimethylammonium bromide (CTAB) 1.0 g (= 2%)
100 mM Tris-HCl (pH 8.0) 5.0 ml (= 100 mM)
5M NaCl 14.0 ml (= 1.4 M)
0.5 M EDTA 2.0 ml (= 20 mM)
2. Phenol-Chloroform: 25 parts phenol (saturated with extraction buffer), 24
parts chloroform, 1 part isoamyl alcohol, 0.1% (w/v) 8-hydroxyquinone. Store
refrigerated.
3. 10× TAE buffer (1000 ml)
Tris-base 48.4 g
Glacial Acetic Acid 10.9 g
EDTA (free acid f.w. 292.25) 2.92 g
Deionized water 1000 ml
4. TE buffer
10 M Tris-HCl (pH 7.4)
1 mM EDTA (pH 8.0)
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APPENDIX C
Solutions for enzyme assay
1. 1.0 % Congo red
Congo red 10 g
NaNO3 0.5 g
Dissolve the components in 0.2 M K2HPO4. Prepare fresh before use.
2. DNS reagent
3,5-dinitrosalicylic acid 1.0 %
phenol 0.2 %
Na2SO3 0.05 %
NaOH 1.0 %
Dissolve 3,5-dinitrosalicylic acid and NaOH in 50 ml of distilled water, mix
thoroughly. Add phenol and Na2SO3. Adjust volume to 100 ml.
3. 40% Na-K tartrate
Dissolve Na-K tartrate 40 g in 100 ml of distilled water. Mix thoroughly.
4. 0.2 M K2HPO4
Dissolve 34 g of K2HPO4 in 1000 ml of distilled water. Mix thoroughly.
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Broth medium
Liquid Basal Medium (LBM) (Pointing, 1999)
Carbon sources 1% (w/v)
KH2PO4 1 g/l
NH4NO3 0.1 g/l
MgSO4.7H2O 0.2 g/l
CaCl2.2H2O 0.01 g/l
Yeast extract 0.01 g/l
CuSO4.5H2O 0.001 g/l
MnSO4.H2O 0.001 g/l
Fe2(SO4)3 0.001 g/l
Calculation for enzyme activity
Calculation for cellulase activity
In 30 minutes of reaction, glucose was obtained = x µg
Glucose molecular weight = 180 = x / 180 µmol
.˙. In 1 minute, glucose was obtained = x / 180 / 30 µmol
Using crude enzyme volume = 0.5 ml
.˙. Cellulase activity = x / 180 / 30 / 0.5 Unit/ml
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Calculation for xylanase activity
In 30 minutes of reaction, xylose was obtained = x µg
Xylose molecular weight = 150 = x / 150 µmol
.˙. In 1 minute, xylose was obtained = x / 150 / 30 µmol
Using crude enzyme volume = 0.5 ml
.˙. Xylanase activity = x / 150 / 30 / 0.5 Unit/ml
Calculation for mannanase activity
In 30 minutes of reaction, mannose was obtained = x µg
Mannose molecular weight = 180.2 = x / 180.2 µmol
.˙. In 1 minute, mannose was obtained = x / 180.2 / 30 µmol
Using crude enzyme volume = 0.5 ml
.˙. Mannanase activity = x / 180.2 / 30 / 0.5 Unit/ml
Calculation for polygalacturonase activity
In 30 minutes of reaction, D-galacturonic acid = x µg
was obtained
D-Galacturonic acid molecular weight = 212.2 = x / 212.2 µmol
.˙. In 1 minute, D-galacturonic acid was obtained = x / 212.2 / 30 µmol
Using crude enzyme volume = 0.5 ml
.˙. Polygalacturonase activity = x / 212.2/ 30 / 0.5 Unit/ml
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Calculation for laccase activity
Enzyme activity was calculated from the linear phase of the reaction using
molar absorbance of the oxidation product of DMP (ε=49,600 M-1cm-1). One unit of
laccase activity defined as the amount of enzyme that oxidize 1 µmole substrate per
minute under standard assay condition
The enzyme activities will be calculated by using Beer-Lambert’s law. In
mathematical terms:
A = εbC
A: absorbance of the sample at specific wavelength
ε: the adsorptivity coefficient or extinction coefficient of the
material at the wave length
b: the pathlength through the sample in cm
C: the concentration
Calculation
Net absorbance at 469 nm(A) = Y (min-1)
Pathlength of cuvette (b) = 1 (cm)
ε of DMP = 49600 (M-1cm-1)
A = εbC
C = A/εb
C = Y____(min-1) 49600 (M-1cm-1) 1 (cm) C = Y____ M/min 49600
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C = Y____ mole/l/min 49600
C = (Y×106) µmole/ml/min 49.6
Using enzyme volume = 0.1 ml (dilution 10 times)
∴Laccase activity = (Y × 106 × 10) µmole/ml/min 49.6
= (Y × 107) Unit/ml 49.6
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APPENDIX D
Standard curve
1. Standard curve of reducing sugar determination by DNS method (Miller, 1959)
Reagent
1. DNS solution
Dissolve 1 g of NaOH and 1 g of 3,5-dinitrosalicylic acid in 50 ml of
distilled water, add 0.2 g of phenol and 0.05 g of Na2SO3 in mixed solution
and adjust to a final volume of 100 ml.
2. 40% Na-K tartrate
Dissolve 40 g of Na-K tartrate in 100 ml of distilled water.
Procedure
1. Add 1 ml of reducing sugar sample and 2 ml of DNS solution to test tube
and using distilled water as control.
2. Vortex and boil for 15 minutes and place in cold water.
3. Add 1 ml of 40% Na-K tartrate to the test tube and vortex.
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Table 1 Absorbance at 550 nm of various concentration of glucose, xylose, and
mannose by DNS method.
A550 Concentration of sugar (µg/ml) Glucose Xylose Mannose D-galacturonic â
0 0 0 0 0
100 0.099 0.101 0.111 0.127
200 0.264 0.357 0.275 0.395
300 0.441 0.765 0.516 0.661
400 0.676 1.091 0.752 0.923
500 0.911 1.508 0.984 1.232
600 1.141 1.818 1.177 1.469
700 1.375 2.166 1.533 1.676
800 1.675 2.461 1.728 1.871
900 1.900 2.718 1.981 2.235
1000 2.146 2.953 2.278 2.458
1100 2.338 3.111 2.430 -
1200 2.546 3.196 2.650 -
1300 2.670 3.252 2.788 - 1400 2.866 3.307 2.984 -
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Figure 1 Satandard curve of glucose versus absorbance at 550 nm.
Figure 2 Satandard curve of xlucose versus absorbance at 550 nm.
y = 0.0021xR2 = 0.9900
0
0.5
1
1.5
2
2.5
3
3.5
0 200 400 600 800 1000 1200 1400 1600
Glucose concentration (ug/ml)
Abs
orba
nce
at 55
0 nm
y = 0.003xR2 = 0.9877
0
0.5
1
1.5
2
2.5
3
3.5
0 100 200 300 400 500 600 700 800 900 1000 1100
Xylose concentration (ug/ml)
Abs
orba
nce
at 55
0 nm
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Figure 3 Satandard curve of mannose versus absorbance at 550 nm.
Figure 4 Satandard curve of D-galacturonic acid versus absorbance at 550 nm.
y = 0.0022xR2 = 0.9922
0
0.5
1
1.5
2
2.5
3
3.5
0 200 400 600 800 1000 1200 1400 1600
Mannose concentration (ug/ml)
Abs
orba
nce
at 55
0 nm
y = 0.0024xR2 = 0.9947
0
0.5
1
1.5
2
2.5
3
0 200 400 600 800 1000 1200
D-galacturonic acid concentration (ug/ml)
Abs
orba
nce
at 55
0 nm
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2. Standard curve of bovine serum albumin (BSA)
Reagent
1. Reagent A: 0.1 M NaOH with 0.2% Na2CO3
Prepare 0.1 M NaOH by dissolve 1.0 g of NaOH in 250 ml of distilled
water. Dissolve 2.0 g of Na2CO3 in 80 ml of 0.1 M NaOH and adjust to a
final volume of 100 ml
2. Reagent B: 1.0% Na-K tartrate with 0.5% CuSO4.5H2O
Dissolve 1.0 g of Na-K tartrate in 80 ml of distilled water and add 0.5 g of
CuSO4.5H2O. Mix and adjust to a final volume of 100 ml by distilled
water.
3. Reagent C: Mix 50.0 ml of reagent A and 1.0 ml of reagent B (prepare
before use)
4. Reagent D: Folin-Ciocalteau reagent
Dilute Folin reagent with distilled water in 1:1
Procedure
1. Prepare a series of dilutions of 100-1000 µg/ml bovine serum albumin and
place 1 ml of each concentration to test tube.
2. Add 5.0 ml of reagent C and mix. Stand for 10 minutes at room
temperature.
3. Add 0.5 ml of reagent D and mix. Stand for 30 minutes at room
temperature.
4. Measure the absorbance at 750 nm using distilled water instead BSA as a
blank.
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Table 2 Absorbance at 750 nm of various concentration of bovine serum albumin
(BSA) by Lowry method.
y = 0.0021xR2 = 0.9557
0
0.2
0.4
0.6
0.8
1
1.2
1.4
0 100 200 300 400 500 600 700
BSA concentration (ug/ml)
Abs
orba
nce
at 75
0 nm
Figure 5 Satandard curve of bovine serum albumin (BSA) versus absorbance at 750
nm
Concentration of BSA (µg/ml) A750 (average) 0 0
100 0.305
200 0.525
300 0.708
400 0.857
500 0.979
600 1.146
700 1.239
800 1.363
900 1.468
1000 1.534
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APPENDIX E
Native PAGE
Reagent
1. 30% Acrylamide stock (30% (w/v) acrylamide, 0.8% (w/v) N,N΄-
methylenebisacrylamide)
Dissolve 60 g of acrylamide and 1.6 g of N,N΄-methylenebisacrylamide in 200
ml of distilled water. Filter the homogeneous solution through a 0.45 µm filter
membrane.
2. 1.5 M Tris-HCl (pH 8.0) (Resolving buffer)
Dissolve 18.5 g of Tris-Cl in distilled water and adjust to pH 8.0 with HCl and
add water to a final volume of 100 ml.
3. 0.05 M Tris-HCl (pH 6.8) (Stacking buffer)
Dissolve 6.0 g of Tris-Cl in distilled water and adjust to pH 6.8 with HCl and
add water to a final volume of 100 ml.
4. 0.9% ammoniumpersulfate
Dissolve 9 mg of ammoniumpersulfate in 1 ml of distilled water. Prepare fresh
daily.
5. TEMED (N,N,N΄,N΄-tetramethylenediamine)
6. Running buffer
Dissolve 3.0 g of Tris base and 14 g of glycine in 1000 ml of distilled water.
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7. 5× Loading buffer
1 M Tris-HCl pH 6.8 0.6 ml
50% (v/v) glycerol 5.0 ml
10% (w/v) SDS 2.0 ml
Mercaptoethanol 0.5 ml
1% (w/v) bromophenol blue 1.0 ml
Distilled water 0.9 ml
Procedure
1. Clean the glass plates, spacers, combs and upper buffer reservoir of the gel
apparatus with detergent and completely dry.
2. Assemble the glass plate sandwich and the spacers.
3. Prepare the monomer solution for the resolving gel by combining all of the
reagents in Table 3.
4. Mix gently and quickly apply to gel cassette using autopipette to about 2
cm below the short plate.
5. Gently overlay with 1-5 mm of distilled water on top of the gel solution
and allow gel to polymerize for 1 hour.
6. Prepare stacking gel as recipe Table 3 on top of the resolving gel and insert
the well-forming comb into the solution.
7. Leave for polymerize about 30 minutes.
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Table 3 Recipe for preparing 10% acrylamide gel for native PAGE.
Reagent Resolving gel (ml) Stacking gel (ml)
Resolving buffer (1.5 M Tris-HCl pH 8.0) 5.7
Stacking buffer (0.05 M Tris-HCl pH 6.8) 2.03
30% Acrylamide stock 3.3 0.6
0.9% Ammoniumpersulfate 1.0 0.3
Gently mix and degas for 30 second
TEMED 10 µl 4 µl
Gently mix and quickly apply to gel cassette
Sample preparation
1. Combine protein sample and 5X loading buffer (1:1) in an eppendorff tube.
2. Load 10 µl of sample in each well of gel
Electrophoresis
1. Place the gel into electrophoresis chamber and attach gel to electrode
assembly.
2. Add running buffer to inner and outer reservoir and remove the comb from
the gel carefully.
3. Load the prepared sample into the well in the stacking gel.
4. Attach the electrode plugs to power supply.
5. Turn on power supply to 200 Volt, 150 mA until the bromophenol blue
tracking dye front reaches the bottom of the gel.
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CURRICULUM VITAE
Name Miss Itthayakorn Promputtha
Date of Birth September 6, 1978
Place of Birth Loei province, Thailand
Home Address 98 Moo 5 Ban Pong, Tambon Na-kham,
Amphur Muang, Loei, 42000, Thailand
E-mail Address [email protected]
Education Background B.Sc. in Medical Technology (Hons.),
Faculty of Associated Medical Science,
Chiang Mai University, Chiang Mai, Thailand,
May, 2001
Scholarship The Royal Golden Jubilee Ph.D. Program (2001-2006)
Publications
1. Promputtha, I., Lumyong, S., Vijaykrishna, D., McKenzie, E.H.C., Hyde,
K.D. and Jeewon, R. (2006). A phylogenetic evaluation of whether
endophytes become saprotrophs at host senescence. Microbial Ecology (In
press).
2. Promputtha, I., Jeewon, R., Lumyong, S., McKenzie, E.H.C. and Hyde, K.D.
(2005). Ribosomal DNA fingerprinting in the identification of non sporulating
endophytes from Magnolia liliifera (Magnoliaceae). Fungal Diversity 20:
167–186.
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3. Promputtha, I., Lumyong, S., Lumyong, P., McKenzie, E.H.C. and Hyde,
K.D. (2005). A new species of Anthostomella on Magnolia liliifera from
northern Thailand. Mycotaxon 91: 413–418.
4. Promputtha, I.; Hyde, K.D.; Lumyong, P.; McKenzie, E.H.C.; Lumyong, S.
(2005). Fungi on Magnolia liliifera: Cheiromyces magnoliae sp. nov. from
dead branches. Nova Hedwigia 80: 527–532.
5. Promputtha, I., Lumyong, S., Lumyong, P., McKenzie, E.H.C. and Hyde,
K.D. (2004). Fungal saprobes on dead leaves of Magnolia liliifera
(Magnoliaceae) in Thailand. Cryptogamie Mycologie 25: 315–321.
6. Promputtha, I., Lumyong, S., Lumyong, P., McKenzie, E.H.C. and Hyde,
K.D. (2004). A new species of Pseudohalonectria from Thailand.
Cryptogamie Mycologie 25: 43–47.
7. Promputtha, I., Hyde, K.D., Lumyong, P., McKenzie, E.H.C. and Lumyong,
S. (2002). Dokmaia monthadangii gen. et sp. nov., a synnematous anamorphic
fungus on Manglietia garrettii. Sydowia 51: 99–103.
8. Promputtha, I., Lumyong, S., Lumyong, P., McKenzie, E.H.C. and Hyde,
K.D. (2002). Fungal succession on senescent leaves of Manglietia garrettii in
Doi Suthep-Pui National Park, northern Thailand. Fungal Diversity 10: 89–
100.
295
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Presentations in international conference
1. Promputtha, I., Hyde, K.D., Peberdy, J.F. and Lumyong, S. (2006).
Enzymatic activity of endophytic fungi on leaf decomposition. 8th
International Mycological Congress, 21-25 August 2006, Cairns Convention
Centre, Queensland, Australia (Poster presentation).
2. Promputtha, I., Jeewon, R., Hyde, K.D., Vijaykrishna. D., McKenzie, E.H.C.
and Lumyong, S. (2006). Do fungal endophytes of Magnolia liliifera become
saprobes at host senescence? RGJ-Ph.D. Congress VII, 20–22 April 2006,
Jontein Palmbeach Resort, Pattaya, Chonburi, Thailand (Oral presentation).
3. Promputtha, I., Lumyong, P., Hyde, K.D., Peberdy, J.F. and Lumyong, S.
(2005). The production pattern of carbohydrases during the decomposition of
Magnolia liliifera leaves. British Mycological Society Annual Scientific
Meeting, 5–8 September 2005, Hulme Hall, University of Manchester,
England (Oral presentation).
4. Promputtha, I., Lumyong, S., Lumyong, P., McKenzie, E.H.C. and Hyde,
K.D. (2004). Diversity and succession of fungi on senescent leaves of
Meliosma simplicifolia (Sabiaceae). The IV Asia-Pacific Mycological
Congress and The IX International Marine and Freshwater Mycology
Symposium, 14–19 November 2004, Chiang Mai, Thailand (Poster
presentation).
5. Promputtha, I., Lumyong, S., Lumyong, P., McKenzie, E.H.C. and Hyde,
K.D. (2002). Fungal succession on senescent leaves of Manglietia garrettii in
Doi Suthep-Pui National Park, northern Thailand. 3rd Asia-Pacific
Mycological Conference on Biodiversity and Biotechnology (AMC2002), 4–8
296
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November 2002, Yunnan University, Kunming, China (Oral presentation).
6. Promputtha, I., Lumyong, S., Lumyong, P., McKenzie, E.H.C. and Hyde,
K.D. (2002). Fungal saprobes on dead leaves of Manglietia garrettii in
Thailand. The 14th Annual Meeting of the Thai Society for Biotechnology
“BIOTECHNOLOGY FOR BETTER LIVING IN THE NEW ECONOMY”,
12–15 November 2002, Khonkaen University, Khonkaen, Thailand (Poster
presentation).
7. Promputtha, I., Lumyong, S., Lumyong, P., McKenzie, E.H.C. and Hyde,
K.D. (2001). Saprobic Fungi on Magnolia garrettii. BioThailand 2001: From
Research to Market, 7–10 November 2001, Queen Sirikit National Convention
Center, Bangkok, Thailand (Poster presentation).
Workshops in field specialization
1. Workshop on “Unculturable Microbes: Molecular Techniques and
Biotechnology Application”. At National Center for Genetic Engineering and
Biotechnology (BIOTEC), National Science and Technology Development
Agency (NSTDA), and Ministry of Science and Technology (MOST). At
BIOTEC auditorium room, BIOTEC Building, Thailand Science Park,
Pathumthani, Thailand. 9–10 January 2006.
2. Workshop on “GBIF and EASIANET Proposed Collection/Names/Images
Digitization”. At Centre for Research in Fungal Diversity, Department of
Ecology and Biodiversity, The University of Hong Kong, Hong Kong SAR,
China. 14–19 March 2005.
297
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3. Workshop on “Molecular Phylogenetics”. At Department of Ecology and
Biodiversity, The University of Hong Kong, Hong Kong SAR, China. 17–22
March 2004.
4. Workshop on “Denaturing Gradient Gel Electrophoresis”. At Department of
Biology, Faculty of Science, Chiang Mai University, Chiang Mai, Thailand.
4–6 May 2004.
5. Workshop on “Microbial Production of Surfactants and Their Applications”.
At Department of Biology, Faculty of Science, Chiang Mai University, Chiang
Mai, Thailand. 10–14 May 2004.
6. Workshop on “Mycology Taxonomy, Molecular Systematics and Using Key
Isolation and Preservation of Fungi”. At the Mushroom Research Centre,
Chiang Mai, Thailand. 7–27 July 2003
7. Workshop on “Fungal Diversity of Thailand: Towards a Checklist of Thai
Fungi, Fungi and Their Biotechnological Application”. At National Science
and Technology Development Agency (NSTDA), Bangkok, Thailand. 15–16
November 2001.
298
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ÅÔ¢ÊÔ·¸Ô ìÁËÒÇÔ·ÂÒÅÑÂàªÕ§ãËÁèCopyright by Chiang Mai UniversityA l l r i g h t s r e s e r v e d
ÅÔ¢ÊÔ·¸Ô ìÁËÒÇÔ·ÂÒÅÑÂàªÕ§ãËÁèCopyright by Chiang Mai UniversityA l l r i g h t s r e s e r v e d
ÅÔ¢ÊÔ·¸Ô ìÁËÒÇÔ·ÂÒÅÑÂàªÕ§ãËÁèCopyright by Chiang Mai UniversityA l l r i g h t s r e s e r v e d
ÅÔ¢ÊÔ·¸Ô ìÁËÒÇÔ·ÂÒÅÑÂàªÕ§ãËÁèCopyright by Chiang Mai UniversityA l l r i g h t s r e s e r v e d
ÅÔ¢ÊÔ·¸Ô ìÁËÒÇÔ·ÂÒÅÑÂàªÕ§ãËÁèCopyright by Chiang Mai UniversityA l l r i g h t s r e s e r v e d
ÅÔ¢ÊÔ·¸Ô ìÁËÒÇÔ·ÂÒÅÑÂàªÕ§ãËÁèCopyright by Chiang Mai UniversityA l l r i g h t s r e s e r v e d
ÅÔ¢ÊÔ·¸Ô ìÁËÒÇÔ·ÂÒÅÑÂàªÕ§ãËÁèCopyright by Chiang Mai UniversityA l l r i g h t s r e s e r v e d
ÅÔ¢ÊÔ·¸Ô ìÁËÒÇÔ·ÂÒÅÑÂàªÕ§ãËÁèCopyright by Chiang Mai UniversityA l l r i g h t s r e s e r v e d
ÅÔ¢ÊÔ·¸Ô ìÁËÒÇÔ·ÂÒÅÑÂàªÕ§ãËÁèCopyright by Chiang Mai UniversityA l l r i g h t s r e s e r v e d
ÅÔ¢ÊÔ·¸Ô ìÁËÒÇÔ·ÂÒÅÑÂàªÕ§ãËÁèCopyright by Chiang Mai UniversityA l l r i g h t s r e s e r v e d
ÅÔ¢ÊÔ·¸Ô ìÁËÒÇÔ·ÂÒÅÑÂàªÕ§ãËÁèCopyright by Chiang Mai UniversityA l l r i g h t s r e s e r v e d
ÅÔ¢ÊÔ·¸Ô ìÁËÒÇÔ·ÂÒÅÑÂàªÕ§ãËÁèCopyright by Chiang Mai UniversityA l l r i g h t s r e s e r v e d
ÅÔ¢ÊÔ·¸Ô ìÁËÒÇÔ·ÂÒÅÑÂàªÕ§ãËÁèCopyright by Chiang Mai UniversityA l l r i g h t s r e s e r v e d
ÅÔ¢ÊÔ·¸Ô ìÁËÒÇÔ·ÂÒÅÑÂàªÕ§ãËÁèCopyright by Chiang Mai UniversityA l l r i g h t s r e s e r v e d
ÅÔ¢ÊÔ·¸Ô ìÁËÒÇÔ·ÂÒÅÑÂàªÕ§ãËÁèCopyright by Chiang Mai UniversityA l l r i g h t s r e s e r v e d
ÅÔ¢ÊÔ·¸Ô ìÁËÒÇÔ·ÂÒÅÑÂàªÕ§ãËÁèCopyright by Chiang Mai UniversityA l l r i g h t s r e s e r v e d
ÅÔ¢ÊÔ·¸Ô ìÁËÒÇÔ·ÂÒÅÑÂàªÕ§ãËÁèCopyright by Chiang Mai UniversityA l l r i g h t s r e s e r v e d
ÅÔ¢ÊÔ·¸Ô ìÁËÒÇÔ·ÂÒÅÑÂàªÕ§ãËÁèCopyright by Chiang Mai UniversityA l l r i g h t s r e s e r v e d
ÅÔ¢ÊÔ·¸Ô ìÁËÒÇÔ·ÂÒÅÑÂàªÕ§ãËÁèCopyright by Chiang Mai UniversityA l l r i g h t s r e s e r v e d
ÅÔ¢ÊÔ·¸Ô ìÁËÒÇÔ·ÂÒÅÑÂàªÕ§ãËÁèCopyright by Chiang Mai UniversityA l l r i g h t s r e s e r v e d
ÅÔ¢ÊÔ·¸Ô ìÁËÒÇÔ·ÂÒÅÑÂàªÕ§ãËÁèCopyright by Chiang Mai UniversityA l l r i g h t s r e s e r v e d
ÅÔ¢ÊÔ·¸Ô ìÁËÒÇÔ·ÂÒÅÑÂàªÕ§ãËÁèCopyright by Chiang Mai UniversityA l l r i g h t s r e s e r v e d
ÅÔ¢ÊÔ·¸Ô ìÁËÒÇÔ·ÂÒÅÑÂàªÕ§ãËÁèCopyright by Chiang Mai UniversityA l l r i g h t s r e s e r v e d
ÅÔ¢ÊÔ·¸Ô ìÁËÒÇÔ·ÂÒÅÑÂàªÕ§ãËÁèCopyright by Chiang Mai UniversityA l l r i g h t s r e s e r v e d
ÅÔ¢ÊÔ·¸Ô ìÁËÒÇÔ·ÂÒÅÑÂàªÕ§ãËÁèCopyright by Chiang Mai UniversityA l l r i g h t s r e s e r v e d
ÅÔ¢ÊÔ·¸Ô ìÁËÒÇÔ·ÂÒÅÑÂàªÕ§ãËÁèCopyright by Chiang Mai UniversityA l l r i g h t s r e s e r v e d
ÅÔ¢ÊÔ·¸Ô ìÁËÒÇÔ·ÂÒÅÑÂàªÕ§ãËÁèCopyright by Chiang Mai UniversityA l l r i g h t s r e s e r v e d