• The Korean Journal of Mycology
• /
• v.25 no.1 s.80
• /
• pp.68-76
• /
• 1997

For the purpose of utilizingcellulosesresources by cellulolytic enzymes of Trametes trogii, its cultural conditions for the production of cellulolytic enzymes in synthetic media were investigated. The optimum conditions for the production of cellulase by T. trogii in synthetic media were $30{\sim}35^{\circ}C,\;pH\;4.0{\sim}6.0,\;and\;11{\sim}15$ day's cultivation. Among the carbon sources, carboxymethyl cellulose was good for the production of avicelase and ${\beta}-glucosidase$, but cellulose was good for the production of CMCase. The optimum concentration of Na-CMC was 3% for the production of all the three cellulolytic enzymes. As the nitrogen source, $0.03{\sim}0.04%$ N as ammonium tartrate was effective for the production of the cellulases.

• Microbiology and Biotechnology Letters
• /
• v.18 no.4
• /
• pp.376-382
• /
• 1990

An extracellular cellulase producing bacterium YE-5 was isolated from soil, and identified as a Cellulomonas sp. by its taxonomical characteristics. The maximal activities of avicelase (0.35 units/ml), CMCase (3.18 units/ml), FPase (0.315 units/ml) and $\beta$-glucosidase (0.882 units/ml) were obtained when this strain was cultured for 48 hrs at $30^{\circ}C$ in a medium containing 0.8% (w/v) Solka floc, 0.06010 (wlv) urea, 0.1% (w/v) $K_2HP0_4$, 0.1% (w/v) $MgS0_4.7H2_0$, 0.2% (w/v) bacto peptone, 0.2% (w/v) yeast extract and pH 6.5. The cellulase was purified by ammonium sulfate fractionation, DEAE-Sepharose column chromatography and Sephadex 6-100 column chromatography from culture filtrate of Cellulomonus sp. YE-5. The molecular weights of purified avieelase, CMCase I, and CMCase II were estimated to be about 95,000 ~ 105,000, 46,000 ~ 47,000 and 120,000 ~ 125,000, respectively.

• Journal of the Korean Society of Food Science and Nutrition
• /
• v.24 no.6
• /
• pp.964-969
• /
• 1995

For the effective utilization of cellulosic biomass, conidial protoplast fusion between Aspergillus niger MAN-831(${\beta}-glucosidase$) and A. wentii MAW-538(CMCase and avicelase), which produced potently cellulolytic enzymes was carried out. Optimal conditions for formation and regeneration of protoplast were conidiospore age-5 dyuas. $2-DG-30\mu\textrm{g}/ml$, preincubation time-4 hours, osmotic stabilizer-0.7M KCl, novozyme(7mg/ml)＋driselase(2.5mg/ml) and reaction time of enzyme-5 hours. Optimal conditions for protoplast fusion were obtained by treatment of protoplasts with 15mM CaCl2 and 25% polyethylene glycol 4000(pH 6~7) as fusogenic agent at $36^{\circ}C$ for 25~30 minutes. The frequency was then $7.94{\times}10^{-4}$. CMCase, avicelase and ${\beta}-glucosidase$ activity of fusant F-208 strain was 1.5, 1.3, 1.2 times higher than those of parental strains, respectively.

• The Korean Journal of Mycology
• /
• v.14 no.1
• /
• pp.37-41
• /
• 1986

The production of cellulolytic enzymes by Pleurotus sajor-caju JAFM 1017 was stimulated by folic acid and thiamine-HCl. Among the inorganic salts, optimum concentrations of $KH_2PO_4$ and $MgSO_4{\cdot}7H_2O$ were 0.2% (w/v) and 0.04% (w/v), respectively, but other inorganic salts were not effective for the production of the enzymes. The optimum culture temperature and pH for the production were $25^{\circ}C$ and 5.5 for avicelase, and $30^{\circ}C$ and 5.0 for CMCase, and $30^{\circ}C$ and 6.5 for ${\beta}-glucosidase$, respectively.

• Microbiology and Biotechnology Letters
• /
• v.33 no.4
• /
• pp.267-273
• /
• 2005

To develop effective and powerful probiotic, Saccharomyces cerevisiae strains producing cellulolytic enzymes were genetically brooded. For the production of exoglucanase, the plasmid pVT-TExo (8.8 kb) was constructed, in which Thermomonosporafusca exoglucanase gene (E3) was under the control of ADHl promoter, and introduced into S. cerevisiae SEY2102. When the transformant, S. cerevisiae SEY2102/pVT-TExo, was cultivated on YPD medium, the total expression level of avicelase reached about 190 unit/l. The secretion efficiency and plasmid stability were about $50\%\;and\;91\%$, respectively. Recombination exoglucanase enzyme bound to avicel better than Clostridium endoglucanase (CelA) and Trichoderma endoglucanase (C4) enzymes. The mixing ratio of E3 and CelA displaying the best synergistic hydrolysis for avicel was observed at 4:1. The mixture of endoglucanase (CelA) and exoglucanase (E3) resulted in 3.2-fold increase of avicelase activity and 2.5-fold enhanced production of sugar production from avicel, compared to the single enzyme treatment.

• KSBB Journal
• /
• v.17 no.2
• /
• pp.195-202
• /
• 2002

The production conditions of cellulolytic enzymes by a fungus, strain FJ1, were optimized using response surface analysis. The culture factors which largely affected the production of enzymes such as cultivation time, carbon source concentration, nitrogen source concentration, and composition ratio of carbon sources were employed. Optimizedconditions of the factors above corresponding to each cellulolytic enzyme production were as fellowing: CMCase production was obtained in the conditions of cultivation time of 5.4 days, carbon source concentration of 3.5%, nitrogen source concentration of 0.6%, and composition ratio of carbon sources of 52:48 (avicel:CMC), xylanase appeared in the conditions of 5.3 days, 3.5%, 0.8%, and 54:46, respectively, and $\beta$-glucosidase were 7.0 days, 5.0%, 1.0%, and 83:17, respectively, and avicelase were 6.5 days, 4.0%, 0.9%, and 64:36, respectively. The activities of CMCase, xylanase, p-glucosidase, and avicelase predicted by the response surface methodology were 33.5, 52.6, 2.88, and 1.84 U/mL, respectively, and $\beta$-glucosidase activity was enhanced up to 74% when compared to that obtained in the experimental conditions.

• Korean Journal of Microbiology
• /
• v.35 no.4
• /
• pp.277-282
• /
• 1999

A bacterium producing the extracellular cellulase was isolated from cattle feces and screened as cellulase activity was excellent upon congo red straining method and activity measurements. Isolate was identified as Bacillus subtilis CH-10 on the basis of morphological and biochemical properties as well as cellular fatty acids composition. The enzyme which the isolate secretes had the optimum initial pH and temperature for its induction was 7.5 and 50${\circ}C$, respectively. The maximum CMCase activity in crude enzyme solution was observed at pH 7.5 and 75${\circ}C$ and was stable for pH 7.5 to 9.0 to maintain 70% activity. When the isolate was cultured in CMC media at 37${\circ}C$ for 24 hrs, CMCase and FPase activity was 1.13 U/㎖and 0.16U/㎖, respectively whereas Avicelase and ${\beta}$-glucosidase activity was not detected. When crude supernatant was used for zymogram, three major bands, cel 1, cel 2 and cel 3, were detected approximately 39, 41 and 57 KDa, respectively on CMC-SDS-PAGE.

• 한국생물공학회:학술대회논문집
• /
• 2002.04a
• /
• pp.453-456
• /
• 2002

The production conditions of cellulolytic enzymes by Trichoderma sp. FJ1, were optimized using response surface analysis. The culture factors which largely affected to the production of enzymes such as cultivation time, carbon source concentration, nitrogen source concentration, and composition ratio of carbon sources were employed. Optimized conditions of the factors above to each cellulolytic enzyme production was as follow: CMCase production was obtained in the conditions of cultivation time of 5.4 days, 3.5% of carbon source concentration, 0.6% of nitrogen source concentration, and 52:48 (avicel:CMC) of composition ratio of carbon sources, respectively, xylanase appeared in the conditions of 5.3 day, 3.5%, 0.8%, and 54:46, respectively, and ${\beta}-glucosidase$ were 7.0 day, 5.0%, 1.0%, and 83:17, respectively, and avicelase were 6.5 day, 4.0%, 0.9%, and 64:36, respectively. The activities of CMCase, xylanase, ${\beta}-glucosidase$, and avicelase predicted by the response surface methodology were 33.5, 52.6, 2.88, and 1.84 U/ml, respectively, and ${\beta}-glucosidase$ was enhanced up to 74% compared to that obtained in the experimental conditions.

• The Korean Journal of Mycology
• /
• v.42 no.1
• /
• pp.86-90
• /
• 2014

Button mushroom (Agaricus bisporus) strains from diverse origins were compared in this study to obtain basic information on their growth and biochemical properties that are helpful for breeding. Among 31 dikaryotic strains tested, most strains showed better mycelial growth on oatmeal agar than on MEA and PDA. Mycelia of the mushroom strains revealed ${\beta}$-glucosidase activity the most clearly among the seven extracellular enzymes tested. All the strains showed protease activity, but ${\beta}$-glucosidase activity was found in 27 strains and xylanase activity was found in 30 strains. The activity of avicelase, CM-cellulase, amylase, and pectinase was detected in less than 20 strains. These results implied that enzymatic characteristics could be used as a criterion of strain selection for breeding study.

• Microbiology and Biotechnology Letters
• /
• v.18 no.5
• /
• pp.460-465
• /
• 1990

Regeneration of protoplast was effective by preincubating spore suspension containing 30$\mu g$/ml of 2-DG for 4 hours, and CBE medium containing casamino acid, bovine serum albumin, ergosterol and myoinositol was found to be more efficient than any other regeneration medium tested in this experiment. The regeneration frequency was about 30%. Optimal conditions for conidial protoplast fusion were obtained by treatment of protoplasts with 10 mM $CaCl_2$ and 30% polyethylene glycol 4000 (pH 7.5) as fusogenic agent at $37^{\circ}C$ for 10 minutes. The fusion frequency was $8.2\times 10^{-4}$. The higher productivity of enzyme of fusant FWN-56 was achived: 2.3-fold for CMCase, 1.5-fold for avicelase, 1.8-fold for $\beta$-glucosidase and 2.5-fold for xylanase compared to that obtained in two parental strains. The genetic stability of fusant after maintenance on minimal medium for more than 4 weeks was high because segregant rate was below 1%. The conidial DNA content of fusant was 1.4-1.6 times higher than that of the parental strains, The nucleus size of fusants were also higher than that of each parental strains.