• Korean Journal of Environmental Biology
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• v.20 no.2
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• pp.130-135
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• 2002

Species of Genus Trichoderma are commercially applied as biological control agents against fungal Pathogens. A powerful biocontrol agent, Trichoderma sp. SJG-99721 was isolated from 305 isolates by morphological characters, chitinase activities and antifungal activities against Phytophthora capsiei. The isolate was identified as Trichoderma harzianum from various features such as growth rate at $27^\circ{C}$, significant growth ratio of $27^\circ{C}$ to $17^\circ{C}$, amount of aerial mycelium, types of branching: system, and disposition patterns of phialide and phialospore. Trichoderma harzianum SJG-99721 have been shown to act as a powerful biological agent against fungal phytopathogens; Botrytis cinerea, Rhizoctonia solani, Phytophthora cryptogea, Phytophthora capsiei, Sclerotinia sclerotiorum, Mycoshaerella melonis, Alternaria sotani, Fusarium oxysporum, Collectotrichum gloesporioodes, Alternaria alternata, Phythium ultimum, Phytophthora drechsleri, Pyricularia grisea.

• Microbiology and Biotechnology Letters
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• v.26 no.5
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• pp.406-412
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• 1998

The endoglucanase gene, egl6, of Trichoderma sp. was connected with the yeast ADH1 promoter, and the resultant plasmid, pVT-C4, was introduced into three S. cerevisiae host strains (YNN27, 2805, and SEY2102). Among each 80 transformants, the cell growth and expression level of endoglucanase were compared in test-tube cultivation, and three respective transformants for each host cells showing the highest expression level and cell growth were selected. When three recombinant yeast cells were batchwise cultivated for 48 hr in flask, the total activities of endoglucanase expressed were about 1140 unit/l with 2805/pVT-C4, 1020 unit/l with SEY2102/pVT-C4, and 590 unit/l with YNN27/pVT-C4. Irrespective of host strain, about 80% of the expressed endoglucanase was detected in the extracellular medium. In addition, it was also found that the recombinant enzyme was secreted into the culture medium as two major forms of lightly and heavily glycosylated proteins.

• Korean Journal of Microbiology
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• v.27 no.1
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• pp.35-42
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• 1989

The mode of transglycosylation reaction observed during the action of low-molecular-weigh $\beta$-D-glucosidase ($\beta$-D-glucoside glucohydrolase, EC3.2.1.21) purified from Trichoderma koningii ATCC 26113 was investigated using $^{1}H$-NMR spectroscopy. The enzyme was purified by the series of procedures including ammonium sulfate precipitation, and fractionations by column chromatographies on Bio-Gel P-150, DEAE-Sephadex A-50, and SP-Sephadex C-50. The final purification was performed by the band eluation after preparative polyacrylamide gel electrophoresis. The enzyme showed its molecular size of 78,000 through the analysis of sodium dodecyl sulfate-polyacrylamide gel electrophoresis and its isoelectric point of 5.80 through the analysis of analytical isoelectric focusing. The H-1 proton resonances were analyzed. After the reaction of the enzyme with cellobiose, the reaction products were separated by high performance liquid chromatography using refractive index detector. H-1 resonances of the products were consisted with those of gentiobiose [$\beta$-D-glucopyranosyl--(1,6)-D-glucopyranose], and cellotriose [$\beta$-D glucopyranosyl-(1,4)-$\beta$-D-glucopyranosyl]-(1,4)-D-glucopyranose] with minor resonances of sophorose [$\beta$-D-glucopyranosyl-(1,2)-D-glucopyranose], respectively.

• Microbiology and Biotechnology Letters
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• v.39 no.3
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• pp.245-251
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• 2011

[ ${\alpha}$ ]Galactosidase was purified from a culture filtrate of Mortierella sp. by CM-sephadex C-50, and subsequent Sephadex G-100 column chromatography. The final preparation thus obtained showed a single band on SDS-polyacrylamide gel electrophoresis. The molecular weight was determined to be 56 kDa. $Gal^3Man^4$ ($6^3$-mono-O-${\alpha}$-D-galactopyranosyl-4-O-${\beta}$-D-mannotetraose), $Gal^{2,3}Man_5$ ($6^{2,3}$-di-O-${\alpha}$-D-galactopyranosyl-4-O-${\beta}$-D-mannopentaose), $Gal_2Man_3$ ($6^2$-mono-O-${\alpha}$-D-galactopyranosyl-4-O-${\beta}$-D-mannotriose), $Gal^2Man_6$ ($6^2$-mono-O-${\alpha}$-D-galactopyranosyl-4-O-${\beta}$-D-mannohexaose) and $Gal^2Man_5$ ($6^2$-mono-O-${\alpha}$-D-galactopyranosyl-4-O-${\beta}$-D-mannopentaose), prepared from 3 types of microbial ${\beta}$-mannnanase, were used as substrates. $Gal^3Man_4$ and $Gal^2Man_3$ had a stubbed ${\alpha}$-galactosyl residue on the $2^{nd}$ and $3^{rd}$ mannose from the reducing end of mannotetraose and mannotriose, thus ${\alpha}$-galactosidase showed a preference for stubbed ${\alpha}$-galactosyl residue. ${\alpha}$-Galactosidase hydrolyzed $Gal^3Man_4$ more rapidly than $Gal^2Man_3$. However, ${\alpha}$-galactosidase hardly acted on $Gal^{2,3}Man_5$, $Gal^2Man_6$ or $Gal^2Man_5$. The enzyme hydrolyzed melibiose to galactose and glucose, raffinose to galactose and sucrose, and also stachyose to galactose and raffinose.

• Korean Journal of Microbiology
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• v.14 no.1
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• pp.17-24
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• 1976

Celluloytic microorgnasims were isolated form the various sources and four of them were identified as Trichoderma roningi, Aspergillus niger, Penicillium chrysogenum, and Streptomyces sp. The induction of extracellular5 cellulase of these species in the liquid culture media containing carboxymethylcellulose (CMC) or Avicel as inducer showed that CMC was a better effective inducer for the production of CMCase(Cx cellulase component) as well as Avicelase(C$_{1}$ cellulase component) than Avicel. It is believed that certain hydrolysis products of cellulose(CMC) could serve as an inducer for an enzyme synthesis. In T. roningi, Asp. niger, and Strptomyces sp., the optimum temperature of CNCase on CMC-culture medium was 50.deg. but temperature around 40.deg.C was found to be optimum for the activities of CMCase prepared from P.ehrysogenum. The optimum temperature for Avicelase activitiles on Avicel-culture media of T. roningi and P. chrysogenum was $40{\circ}C$ whereas temperature $50{\circ}C$ was found to be optimum for Avicelase from A.niger and Streptomyces sp. The optimal activities of these CNCase and Avicelase prepared from. T. ronigi, Pen.chrysogenum and Streptomyces sp. were found similarly to be at pH's around 5.4 and 6.0 while pH 4.8 was optimum for the activities of CMCase and Avicelase from A.niger, indicating that A.niger in acidic media would yield an enzyme of high activity.

• The Korean Journal of Mycology
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• v.20 no.1
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• pp.37-43
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• 1992

Typhula incarnata grew over a temperature range of -5 to $20^{\circ}C$ with maximum growth at 10 to $15^{\circ}C$. Sclerotial production for T. incarnata was greatest at the higher temperature. Maximum mycelial growth of this pathogen occurred from pH 5.4 to 6.2. When carbon sources were added to a basal salt medium (Czapek's dox agar) at 5 g carbon sources/l, inulin, soluble starch, galactose, glucose, mannose, manitol, sucrose, maltose, cellobirose, trehalose, raffinose, and dextrin supported growth better than other carbon sources did. Of the twenty-three nitrogen sources tested, glycine, serine, ammonium sulfate, asparagine, asparatic acid, and ${\beta}-alanine$ were the most favorable for mycelial growth of T. incarnata. Cystine and cysteine were poor nitrogen sources. Ammonium salt of nitrogen sources supported growth better than nitrate salt of nitrogen sources. Potato dextrose agar, oat meal agar, and V-8 juice agar were the most favorable for mycelial growth and sclerotial formation. Appropriate addition of pepton to PDA decreased mycelial dry weight, but sucrose supported good growth of T. incarnata. Percent viable sclerotia of T. incarnate buried in bentgrass soil decreased from 2 months after treatment remarkably. Trichoderma riride and bacteria were isolated from non-germinated sclerotia. Live orchard grass leaf pieces within the soil were colonized by T. incarnata better than sterile and unsterile dead leaf pieces at $0^{\circ}C$. Saprophytic ability of T. incarnate on sterile leaf sheath occurred better at $0^{\circ}C$ than at $10^{\circ}C$. Saprophytic microflora consisting of Cladosporium sp., Fusarium sp., Mucor sp., Pythium sp., and unidentified fungi were the competitors for the sterilized and unsterilized substrate, but their colonization was not find on live leaf sheath buried in the soil at $0^{\circ}C$. In the effect of fungicides to Typhula snow mold disease of creeping bentgrass, mixture of polyoxin and thiram was the most effective, followed by iprodione, mixture of iprodione and oxine copper, thiophanate-methyl, myclobutanil, and tolclofos-methyl.

• Korean Journal of Microbiology
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• v.24 no.3
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• pp.251-262
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• 1986

High-molecular-weight ${\beta}-glucosidase$ (EC 3.2.1.21) was purified from the culture filtrate of Trichoderma koningii through a four-step procedure including chromatography on Bio-Gel P-150, DEAE-Sephadex A-50 and SP-Sephadex C-50; and chromatofocusing on Polybuffer exchanger PBE 94. The molecular weight of the enzyme was determined to be about 101,000 by SDS-polyacrylamide gel electrophoreses, and the isoelectric point was estimated to be 4.96 by analytical isoelectric focusing. The temperature optimum for activity was about $55^{\circ}C$, and the pH optimumwas 3.5. The enzyme was considerably thermostable, for no loss of activity was observed when the enzyme was preincubated at $60^{\circ}C$ for 5h. Km values for cellobiose, gentiobiose, sophorose, salicin and $p-nitrophenyl-{\betha}-D-glucoside$ were 99.2, 14.7, 7.09, 3.15 and 0.70 mM, respectively, which indicates that the enzyme has much higher affinity towards $p-nitrophenyl-{\betha}-D-glucoside$ than towards the other substrates, especially cellobiose. Substrate inhibition by $p-nitrophenyl-{\betha}-D-glucoside$ and salicin was observed at the conecntrations exceeding 5mM. Gluconolactone was a powerful inhibitor against the action of the enzyme on $p-nitrophenyl-{\betha}-D-glucoside\;(K_i\;37.9\;{\mu}M)$, wherease glucose was much less effective ($K_i$ 1.95 mM). Inhibition was of the competitive type in each case. Transglucosylation activity was detected shen the readtion products formed from $p-nitrophenyl-{\betha}-D-glucoside$ by the enzyme were analysed using high-performance liquid chromatography.

• Journal of the Korean Society of Tobacco Science
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• v.7 no.1
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• pp.75-84
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• 1985

A strain of Trichoderm sp. J-30 which strongly products cellulase to reduce the content of cellulose in the stem of leaf tobacco was isolated from leaf tobaco. The Trichoderma sp. J-30 was identified as Trochoderma voride. The cellulase from this strain was purified with the physico-chemical methods and treated in the culled stem of leaf tobacco. The results obtained were summarized as follows. 1. Optimal pH of the enzyme was at pH 5.0. 2. The enzyme shooed a higher activity at $40^{\circ}C$ and its thermal stability began to decrease at $60^{\circ}C$. 3. The enzyme activity was promoted by the metal ions such as $Ca^{2+}, Mg^{2+}, Pb^{2+}and\;Zn^{2+}.$ 4. When the culled stem of leaf tobacco was applied with the 3% of the enzyme solution at $40^{\circ}C$ for 3 days. 15 to 17% of cellulose contents decreased, 12 to 13% of total sugar increased and the filling power was increased by 10-13% in the sample.

• Applied Biological Chemistry
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• v.45 no.2
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• pp.71-76
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• 2002

Several antagonistic bacteria, SD-1, 4, 10, 11, 14, 15, and 16, which have strong CMCase and amylase activities, were isolated from the fermented mushroom media. Among them, SD-1, 10, 11, and 15 have strong antibacterial activities against the mushroom pathogenic bacteria Pseudomonas sp., and SD-1, 10, 11, 14, and 16 have strong antifungal activities against the mushroom pathogenic fungi, Trichoderma sp. SD-14, 15, and 16 did not inhibit the growth of mushroom Pleurotus eryngii ASI-2302, and Pleurotus ostreatus ASI-2042 and ASI-2180. When the culture broth mixture of the seven bacterial strains was applied to the mushroom media, the growths of pathogens, Pseudomonas sp. and Trichoderma sp., were inhibited.

• Proceedings of the Zoological Society Korea Conference
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• 1998.10b
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• pp.286.1-286
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• 1998

No Abstract, See Full Text