• The Korean Journal of Mycology
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• v.13 no.4
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• pp.213-219
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• 1985

Among the eight strains, Pleurotus sajor-caju JAFM 1017 was selected as most potent producer of cellulolytic enzymes. The avicelase and CMCase activity reached maximum levels after 10 days, and ${\beta}-glucosidase$ activity reached a maximum level after 19 days. Among the various carbon sources, cellulose powder was most effective for the production of avicelase and ${\beta}-glucosidase$, and Na-CMC (sodium carboxymethyl cellulose) was good for the production of CMCase. The optimum concentration of cellulose powder was 1.0% (w/v), and glucose (1.0%) completely depressed the production of enzymes. Nitrates were effective for the production of enzymes, but nitrites did not support growth. The production of cellulolytic enzymes increased as the concentration of urea increased. The appropriate concentration of urea was 0.054% (w/v).

• Biotechnology and Bioprocess Engineering:BBE
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• v.10 no.1
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• pp.52-59
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• 2005

The study was targeted to saccharify foodwastes with the cellulolytic and amylolytic enzymes obtained from culture supernatant of Trichoderma harzianum FJ1 and analyze the kinetics of the saccharification in order to enlarge the utilization in industrial application. T. harzianum FJ1 highly produced various cellulolytic (filter paperase 0.9, carboxymethyl cellulase 22.0, ${\beta}$-glucosidase 1.2, Avicelase 0.4, xylanase 30.8, as U/mL-supernatant) and amylolytic (${alpha}$-amylase 5.6, ${\beta}$-amylase 3.1, glucoamylase 2.6, as U/mL-supernatant) enzymes. The $23{\sim}98\;g/L$ of reducing sugars were obtained under various experimental conditions by changing FPase to between $0.2{\sim}0.6\;U/mL$ and foodwastes between $5{\sim}20\%$ (w/v), with fixed conditions at $50^{\circ}C$, pH 5.0, and 100 rpm for 24 h. As the enzymatic hydrolysis of foodwastes were performed in a heterogeneous solid-liquid reaction system, it was significantly influenced by enzyme and substrate concentrations used, where the pH and temperature were fixed at their experimental optima of 5.0 and $50^{\circ}C$, respectively. An empirical model was employed to simplify the kinetics of the saccharification reaction. The reducing sugars concentration (X, g/L) in the saccharification reaction was expressed by a power curve ($X=K{\cdot}t^n$) for the reaction time (t), where the coefficient, K and n. were related to functions of the enzymes concentrations (E) and foodwastes concentrations (S), as follow: $K=10.894{\cdot}Ln(E{\cdot}S^2)-56.768,\;n=0.0608{\cdot}(E/S)^{-0.2130}$. The kinetic developed to analyze the effective saccharification of foodwastes composed of complex organic compounds could adequately explain the cases under various saccharification conditions. The kinetics results would be available for reducing sugars production processes, with the reducing sugars obtained at a lower cost can be used as carbon and energy sources in various fermentation industries.

• Proceedings of the Korean Society for Applied Microbiology Conference
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• 2005.06a
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• pp.245-247
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• 2005

A cellulolytic fungus isolated from Agave plantation in northeastern Thailand was identified as Acrophialophora nainiana. The fungus was capable of growing at pH between 3 - 7 and 25 - 45 $^{\circ}C$, with the optimum conditions at pH 5.0 and 40 $^{\circ}C$. The wild isolate produced cellulases, comprising of exoglucanase (0.019 U/mg protein), endoglucanase (0.366 U/mg protein), and ${\beta}$-glucosidase (0.001 U/mg protein). Mutations with UV and NTG produced the UV 10-2 mutant with cellulases activities including exoglucanase (0.093 U/mg protein), endoglucanase (0.585 U/mg protein), and ${\beta}$-glucosidase (0.013 U/mg protein). Purification of the enzymes with ultrafiltration, ammonium sulfate precipitation, and ion-exchange chromatography yielded the maximal cellulase specific activities of 2.736 U/mg protein (exoglucanase), 0.235 U/mg protein (endoglucanase), and 0.008 U/mg protein (${\beta}$-glucosidase). The mutant's cellulases were the most active at pH 5.0 and 60 $^{\circ}C$. Ion-exchange chromatography revealed that A. nainiana UV 10-2 cellulases were comprised of two peaks with one peak showing the single endoglucanase activity while the other peak showed a mixture of the three enzyme activities. Production of A. nainiana UV 10-2 cellulases using banana leaf stalk as the sole carbon source gave comparable yields to that of the pure ${\alpha}$-cellulose. The enzymes were used in the simultaneous saccharification and fermentation (SSF) of plant residue (Coix aquatica) along with Kluveromyces marxianus to produce ethanol. Moreover, when the enzymes were used in the bioscouring process of fabric, the desiravle traits of textile processing including immediate water absorbency, increased in whiteness and reduction of yellowness of the treated fabric were observed.

• Mycobiology
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• v.34 no.4
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• pp.159-165
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• 2006

One of the most economically viable processes for the bioconversion of many lignocellulosic waste is represented by white rot fungi. Phanerochaete chrysosporium is one of the important commercially cultivated fungi which exhibit varying abilities to utilize different lignocellulosic as growth substrate. Examination of the lignocellulolytic enzyme profiles of the two organisms Phanerochaete chrysosporium and Rhizopus stolonifer show this diversity to be reflected in qualitative variation in the major enzymatic determinants (ie cellulase, xylanase, ligninase and etc) required for substrate bioconversion. For example P. chrysosporium which is cultivated on highly lignified substrates such as wood (or) sawdust, produces two extracellular enzymes which have associated with lignin deploymerization. (Mn peroxidase and lignin peroxidase). Conversely Rhizopus stolonifer which prefers high cellulose and low lignin containg substrates produce a family of cellulolytic enzymes including at least cellobiohydrolases and ${\beta}-glucosidases$, but very low level of recognized lignin degrading enzymes.

• KSBB Journal
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• v.22 no.2
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• pp.114-118
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• 2007

In this study, an amylase-producing fungus, strain 15 was isolated from soil in order to saccharify food wastes with cellulolytic and amylolytic enzymes. The amylase production cultures were performed in Mandel's medium with 1% rice straw and 1% paper wastes as carbon sources. The strain produced various cellulolytic (FPase 0.25, xylanase 20.09, CMCase 3.15 U/mL-supernatant) and amylolytic ($\alpha$-amylase 1.20, gluco-amylase 0.70, $\beta$-amylase 2.40 U/mL-supernatant) enzymes in Mandel's medium. In 10 L jar fermenter, maximum amylase and FPase activities, 3.25 and 0.23 U/mL, were obtained when the culture was grown at 30$^{\circ}C$, 200 rpm and 0.6 vvm for 3 days. In 100 mL flask level and 10 L jar fermenter, amylase produced by the strain 15 showed similar cellulolytic and amylolytic enzyme activities with Trichoderma inhamatum KSJ1 isolated from rotten woods by previous researcher. The ability of saccharification to food wastes also showed similar degree. However, the isolate 15 appeared to be yellowish in YMEA plate comparing to Trichoderma inhamatum KSJ1 in greenish.

• Journal of Microbiology and Biotechnology
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• v.9 no.4
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• pp.514-517
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• 1999

Hydrolysis of EFB (empty fruit bunch) derived from oil palm was studied using crude enzyme from Aspergillus terreus IMI 282743 along with commercial enzymes from Trichoderma reesei and Aspergillus niger. Hydrolysis at $40^{\circ}C$ and $50^{\circ}C$ with $\alpha$-cellulose or EFB gave significantly lower yield when commercial enzymes of T. reesei and A. niger were used and the hydrolysis time extended beyond 10 h. After 24 h of hydrolysis at $40^{\circ}C$ and $50^{\circ}C$, the filter paper activity (Fpase) from A. terreus retained as much activity as A. niger and it was significantly higher than T. reesei. Glucose concentration of 0.25% and 0.5% caused significant inhibition in the crude enzyme, but in regards to the commercial enzymes it only showed a slight effect. Crude enzymes from A. terreus could produce the highest reducing sugars when compared to commercial enzymes from T. reesei or A. niger. Nevertheless, low yield of sugar was observed for EFB for all treatments.

• Fisheries and Aquatic Sciences
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• v.18 no.4
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• pp.349-357
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• 2015

To reutilize fisheries waste, we isolated a bacterial strain from a coastal area located in Busan. It was identified as Bacillus licheniformis TK3-Y. Using plate assay and 500-mL flask experiments, we found that the isolate simultaneously possessed cellulolytic, proteolytic, and lipolytic activities with salt tolerance. 10% (v/v) inoculums, were used to examine the biodegradation characteristics of the TK3-Y strain on carboxymethylcellulose, skim milk, and olive oil media. The optimum conditions for pH, temperature, agitation speed, and NaCl concentration on each 1% substrate were 6, $50^{\circ}C$, 180 rpm, and 17.5%, respectively. Under optimal conditions, the TK3-Y strain showed 1.07 U/mL cellulolytic, 1,426 U/mL proteolytic, and 6.45 U/mL lipolytic activities. Each enzyme was stable within a range of 17.5-35% NaCl. Therefore, the salt tolerance ability of strain TK3-Y was superior to other related strains. In degradation of a mixed medium containing all three substrates, both the cellulolytic and proteolytic activities were somewhat lower than those on each single substrate, while the lipolytic activity was somewhat higher. From the above results, the TK3-Y strain appears to be a good candidate for use in the efficient treatment of fisheries waste in which components are not collected separately.

• Mycobiology
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• v.29 no.4
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• pp.210-217
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• 2001

Seventy-three species and five varieties belonging to 36 genera were collected from leaf surfaces of banana plants on glucose and cellulose-Czapek's agar at $28^{\circ}C$. The results obtained from leaf surfaces(phyllosphere and phylloplane) were basically similar on the two types of media and the most common fungi were Alternaria, Aspergillus, Chaetomium, Cladosporium, Cochliobolus, Curvularia, Gibberella, Memnoniella, Mycosphaerella, Setosphaeria and Stachybotrys. The monthly counts of these fungi were irregularly fluctuated giving maxima at various months. Chaetomium globosum was in the top of fungi in producing both exo- and endo-$\beta$-l,4-glucanases among the 34 tested isolates obtained from leaves(phylloplane) on cellulose-Czapek's agar. Maximum production of these enzymes by C. globosum was 6 and 8 days after incubation at $25^{\circ}C$ with culture medium containing wheat bran as a carbon source and peptone as a nitrogen source and initially adjusted to pH 6.

• Korean Journal of Microbiology
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• v.25 no.1
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• pp.28-33
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• 1987

Celluloytic bacteria, -Gram positive, Gram negative and actionmycetes-were used to study their catabolic pathways of carbohydrate. It was found that Embden-Meyerhof-Parnas(EMP) pathway and hexose monophosphate(MHP) shunt were operated in Cellulomonase sp. CS1-1, C. flavigena, and Pseudomonas fluorescens subsp. cellulosa when they were cultured in a glucose containing medium, whilst gluconate was catabolised mainly via Entner-Doudoroff(ED) pathway, and to some extend through HMP shunt. Enzymes of ED pathway in the orgamisms were induced by gluconate. On the other hand Nocardia cellulans catabolised glucose and gluconate via EMP pathway and HMP shunt. The growth rate of N. Cellulans on gluconate were much slower than that on glucose.

• The Korean Journal of Mycology
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• v.12 no.4
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• pp.133-140
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• 1984

Some properties of cellulolytic enzymes produced by Pleurotus sajor-caju JAFM 1017 during its growth in synthetic medium were investigated. The optimum pH of avicelase, CMCase, and ${\beta}-glucosidase$ was pH 5.5, pH 4.5 and pH 6.0, respectively. Avicelase and CMCase were stable within pH 5.0 to 6.0 and 4.0 to 6.0, respectively, and ,${\beta}-glucosidase$ was within pH 5.5 to 6.5. The optimum temperature of avicelase, CMCase and ${\beta}-glucosidase$ was the same of $40^{\circ}C$. The enzymes were stable below the optimum temperature, but the enzymes were unstable over the temperature of $50^{\circ}C$, and avicelase was losing about 91.7% of activity at $70^{\circ}C$ for 10 min. The enzyme activity of avicelase and CMCase was increased in proportion to the substrate concentration within 1% and 0.7%, respectively, and ${\beta}-glucosidase$ was within 0.1%. The Michaelis constants (Km) of avicelase and CMCase were 30.77mg avicel/ml and 14.64m Na-CMC/ml, respectively and ${\beta}-glucosidase$ was 5. 13mg salicin/ml. The reducing sugar production of avicelase was proportionaly increased until 120 min. and CMCase and ${\beta}-glucosidase$ were until 60min. The activity of three cellulolytic enzymes were increased by $Ca^{2+}$ at the concentration of $10^{-2}M$, but were inhibited by $Hg^{2+}$, $Ag^+$.