• Applied Biological Chemistry
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• 제38권6호
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• pp.490-495
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• 1995

Cellulomonas sp. KL-6 균주가 생산하는 cellulase 중 CMCase나 FPase는 세포외로 다량 분비되나 ${\beta}-glucosidase$는 cell bound form으로 존재하여 배양액에서의 생산은 극히 미약하였다. CMCase와 FPase는 배양 5일째에, ${\beta}-glucosidase$는 배양 4일째에 각각 최대생산을 나타내었다. $CaCO_3(0.1%)$가 첨가된 효소생산 최적조건에서 CMCase는 $82\;unit/m{\ell}$를, FPase는 $80\;unit/m{\ell}$를 그리고 ${\beta}-glucosidase$는 $1.2\;unit/m{\ell}$를 각각 생산하였고 이는 기본배지에서 보다 $60{\sim}70%$의 생산증가를 가져왔다. KL-6 균주는 lignase와 laccase의 생산은 없었다.

• 생명과학회지
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• 제18권8호
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• pp.1049-1052
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• 2008

Aspergillus niger가 액체발효(SF) 와 고체발효의 시험 규모 조건에서의 셀루로오스계 효소의 생산을 비교하였다. 액체배지는 0.5% 셀루로오스가 함유된 Czapek Dox를 사용하였고, 고체 지지체로 사용한 쌀겨는 셀루로오스로 적시고 SSF 발효를 위하여 Czapek Dox 배지를 첨가하였다. CMCase, 여지 paperase 그리고 ${\beta}$-Glucosidase 의 생산을 경시적으로 측정하였다. SSF 배양에서의 3일간의 효소 생산량은 SF 에서의 7일간 배양과 같았다. 따라서 SSF 조건이 SF 배양 조건보다 많은 효소를 생산함을 알 수 있었다. SSF 조건에서 FPase, CMCase 및 ${\beta}$-glucosidase의 최대 활성은 0.40, 0.62 및 0.013 U/ml 였으나, SF 조건에서는 0.13, 0.06 및 0.0013 U/ml의 활성을 나타내었다. 결론적으로 Aspergillus niger에 의해 생산되는 셀루로오스계 효소의 생산을 위해서는 SSF 발효 조건의 선택이 유리하다는 것을 알 수 있었다.

• Journal of Microbiology and Biotechnology
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• 제14권6호
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• pp.1196-1199
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• 2004

A bacterium, isolated from rabbit's waste and identified as Cellulomonas sp., had cellulase and thermostable $\alpha$-amylase activity when grown on wheat bran. Maximum activity of thermostable $\alpha$-amylase was obtained by adding $3\%$ soluble starch. However, soybean oil (1 ml $1^{-1}$) could increase the production of $\alpha$-amylase and cellulase in 'wheat bran. The $\alpha$-amylase was characterized by making a . demonstration of optimum activity at $90^{\circ}C$ and pH 6- 9, with soluble starch as a substrate. The effect of ions on the activity and the stability of this enzyme were investigated. This strain secreted carboxymethyl cellulase (CMCase), cellobiase ($\beta$­glucosidase), and filter paperase (Fpase) during growth on wheat bran. Carboxymethy1cellulase, cellobiase, and Fpase activities had pH optima of 6, 5.5, and 6, respectively. CMCase and cellobiase activities both had an optimum temperature of $50^{\circ}C$, whereas Fpase had an optimum temperature of $45^{\circ}C$.

• Journal of Applied Biological Chemistry
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• 제51권4호
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• pp.155-159
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• 2008

A local isolate of Aspergillus niger was cultivated under optimal growth conditions on wheat bran in solid state fermentation. Filter paperase from fermented bran was separately extracted with different solvents to test the recovery of the enzyme. Among solvents tested, distilled water served as the best leachate, thus the conditions were further optimized with distilled water. After two washes of fermented bran with distilled water for 1.5 h each under stationary conditions at 1 g wheat bran: 5 mL distilled water, the maximum recovery of 13.5 $Ug^{-1}$ of wheat bran was obtained.

• Biotechnology and Bioprocess Engineering:BBE
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• 제10권1호
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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.