scholarly journals Carboxymethyl cellulase production from a Paenibacillus sp.

2016 ◽  
Vol 70 (3) ◽  
pp. 329-338 ◽  
Author(s):  
Katarina Mihajlovski ◽  
Sladjana Davidovic ◽  
Milica Carevic ◽  
Neda Radovanovic ◽  
Slavica Siler-Marinkovic ◽  
...  
Keyword(s):  
Culture Supernatant ◽  
Soluble Sugars ◽  
Cellulase Activity ◽  
Cellulase Production ◽  
Carboxymethyl Cellulase ◽  
Carbon And Nitrogen ◽  
Cmcase Activity ◽  
Working Volume ◽  
Paenibacillus Sp ◽  
Initial Ph

Cellulases are industrially important enzymes with a potential to convert cellulose into fermentable sugars. Novel bacterial isolate Paenibacillus sp. CKS1 was tested for cellulase activity and the optimal conditions for carboxymethyl cellulase (CMCase) production were determined. Maximum CMCase activity was obtained in the third passage of the bacterial culture after 3 days of incubation at 30?C. Cellobiose and yeast extract was the optimal source of carbon and nitrogen for induction of CMCase activity. In addition, with initial pH 7 of the medium and 40 ml of working volume in 500 ml culture flasks with shaking at 150 rpm, the maximum CMCase activity in a crude culture supernatant reached value of 0.532?0.006 U/ml. For crude CMCase, optimal temperature was 50?C and optimal pH 4.8, respectively. HPLC analysis confirmed the bacterium is capable to hydrolise CMC to glucose and other soluble sugars.

Optimization of Culture Conditions for Cold-Active Cellulase Production by Penicillium cordubense D28 Using Response Surface Methodology

2011 ◽  
Vol 183-185 ◽  
pp. 994-998
Author(s):  
Shuo Dong ◽  
Nai Yu Chi ◽  
Qing Fang Zhang
Keyword(s):  
Response Surface Methodology ◽  
Response Surface ◽  
Cellulase Activity ◽  
Cellulase Production ◽  
Culture Conditions ◽  
Batch Reactors ◽  
Corn Meal ◽  
Cold Active ◽  
Initial Ph ◽  
Cost Efficient

The design of an optimum and cost-efficient medium for production of cold-active cellulase by Penicillium cordubense D28 was attempted by using response surface methodology (RSM). Based on the Plackett–Burman design, corn meal, (NH4)2SO4 and branc were selected as the most critical nutrient. Subsequently, they were investigated by the Box-Behnken design. Results showed that the maximum cold-active cellulase activity of 110.4U/mL was predicted when the concentration of corn meal, (NH4)2SO4 and branc were 21.97 g/L, 2.39 g/L and 14.99 g/L, respectively. The results were further verified by triplicate experiments. The batch reactors were operated under an optimized condition of the respective corn meal, (NH4)2SO4 and branc concentration of 22 g/L , 2.4 g/L and 15 g/L , the initial pH of 6.0 and experimental temperature of 20 ± 1°C. Without further pH adjustment, the maximum cold-active cellulase activity of 109.8 U/mL was obtained based on the optimized medium with further verified the practicability of this optimum strategy.

Production and Optimization of Cellulase Activity of Thermomonospora Viridis Isolated From Rice Straw

2021 ◽  
Vol 50 (2) ◽  
pp. 395-404
Author(s):  
Faozia Faleha Sadida ◽  
Ma Manchur
Keyword(s):  
Enzyme Activity ◽  
Metal Ions ◽  
Rice Straw ◽  
Cellulase Activity ◽  
Nitrogen Sources ◽  
Cellulase Production ◽  
Tetraacetic Acid ◽  
Carbon And Nitrogen Sources ◽  
Carbon And Nitrogen ◽  
Optimum Ph

A highly cellulolytic actinomycete SR1 was locally isolated from rice straw and provisionally identified as Thermomonospora viridis. Optimum pH, temperature, carbon and nitrogen sources for its cellulase production were 6.5, 35°C, Carboxymethyl cellulase (CMC) and yeast extract, respectively whereas those of cellulase activity were 7.5, 40°C, CMC and peptone respectively. The effects of various metal ions and different reductant and inhibitors on its cellulase activity were investigated. Univalent Ag+ was found to decrease the enzyme activity whereas increased by bivalent Mg2+. Ethylene diamine tetraacetic acid (EDTA) caused remarkable decrease of cellulase activity but β-Mercaptoethanol stimulated its cellulase activity. Bangladesh J. Bot. 50(2): 395-404, 2021 (June)

Plackett-Burman Design for Screening Culture Conditions in Cellulase Production by Penicillium decumbens and Enzyme Characterization

2012 ◽  
Vol 518-523 ◽  
pp. 5578-5585
Author(s):  
Nan Ban ◽  
Yu Jie Zhou ◽  
Yan Ping Ye ◽  
Lin Mei Dai ◽  
Alatangaole Damirn ◽  
...  
Keyword(s):  
Cellulase Activity ◽  
Enzyme Characterization ◽  
Cellulase Production ◽  
Culture Conditions ◽  
Penicillium Decumbens ◽  
Initial Ph ◽  
Effects Of Ph ◽  
Burman Design ◽  
The Stability ◽  
Plackett Burman Design

Plackett-Burman design was employed for screening culture conditions for cellulase production by Penicillium decumbens in submerged fermentation. The results showed that wheat bran was the most significant factor influencing Filter Paper Activity (FPA) of the cellulase, followed by cellulose microcrystalline and initial pH, which could be further optimized for improving the cellulase activity. The effects of pH and temperature on FPA assay were investigated, and optimal FPA could be obtained at pH 4.5 and 60 °C. The stabilities of endo-glucanase (EG), exo-glucanase (CBH) and β-glucosidase (BG) were investigated and compared with that of FPA under different pH and temperature. The results indicated that CBH and FPA were more sensitive to pH and temperature than EG and BG and the stability of CBH was very similar to that of FPA under the conditions.

scholarly journals ISOLATION, SCREENING AND THE INFLUENCE OF CULTIVATION FACTORS ON CELLULASE OF BACTERIA ISOLATED FROM TERMITES GUT

2018 ◽  
Vol 54 (4A) ◽  
pp. 89
Author(s):  
Hien Thi Nguyen
Keyword(s):  
Bacillus Subtilis ◽  
Cellulase Production ◽  
Soy Flour ◽  
Rrna Gene ◽  
Optimal Conditions ◽  
16S Rrna Gene Sequences ◽  
Cultivation Temperature ◽  
Cmcase Activity ◽  
Initial Ph ◽  
Sequences Analysis

From five termites guts samples collected in different places in Ha Noi and Vinh, 11 isolates which formed halo on agar plates with CMC were isolated. Among them strain G4 possessed the highest CMCase activity. Based on morphology and 16S rRNA gene sequences analysis, G4 was identified as Bacillus subtilis G4. The results from cultivation study revealed that M3 medium containing rice bran 1 %, soy flour 1 %, casein 1 % and 1 % NaCl  was the best medium for cellulase production of B. subtilis G4. At optimal conditions for G4 which were  inoculums ratio 1 %, cultivation temperature 37ºC, cultivation time 72 hours, shaking speed 150 rpm and initial pH medium 7, CMCase and FPase activity reached 3.36 U/ml and 0.35 U/ml, respectively.

scholarly journals Enhanced Cellulase Production from Bacillus subtilis by Optimizing Physical Parameters for Bioethanol Production

2013 ◽  
Vol 2013 ◽  
pp. 1-11 ◽  
Author(s):  
Deepmoni Deka ◽  
Saprativ P. Das ◽  
Naresh Sahoo ◽  
Debasish Das ◽  
Mohammad Jawed ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Cell Growth ◽  
Desirability Function ◽  
Scale Up ◽  
Cellulase Production ◽  
Maximum Activity ◽  
Physical Parameters ◽  
Bioethanol Production ◽  
Cmcase Activity ◽  
Initial Ph

Effect of physical parameters such as initial pH, agitation (rpm), and temperature (°C) for cellulase production from Bacillus subtilis AS3 was investigated. Central composite design of experiments followed by multiple desirability function was applied for the optimization of cellulase activity and cell growth. The effect of the temperature and agitation was found to be significant among the three independent variables. The optimum levels of initial pH, temperature, and agitation for alkaline carboxymethylcellulase (CMCase) production predicted by the model were 7.2, 39°C, and 121 rpm, respectively. The CMCase activity with unoptimized physical parameters and previously optimized medium composition was 0.43 U/mL. The maximum activity (0.56 U/mL) and cell growth (2.01 mg/mL) predicted by the model were in consensus with values (0.57 U/mL, 2.1 mg/mL) obtained using optimized medium and optimal values of physical parameters. After optimization, 33% enhancement in CMCase activity (0.57 U/mL) was recorded. On scale-up of cellulase production process in bioreactor with all the optimized conditions, an activity of 0.75 U/mL was achieved. Consequently, the bacterial cellulase employed for bioethanol production expending (5%, w/v) NaOH-pretreated wild grass with Zymomonas mobilis yielded an utmost ethanol titre of 7.56 g/L and 11.65 g/L at shake flask and bioreactor level, respectively.

Identification of Locally Isolated Cellulolytic Stenotrophomonas maltophilia from Rice Straw and Optimization of its Cellulase Activity

2020 ◽  
Vol 37 (1) ◽  
pp. 15-22
Author(s):  
Faozia Faleha Sadida ◽  
Fatima Binte Kamal ◽  
Mohammed Abul Manchur
Keyword(s):  
Nitrogen Source ◽  
Rice Straw ◽  
Stenotrophomonas Maltophilia ◽  
Cellulase Activity ◽  
Cellulolytic Bacterium ◽  
Carbon And Nitrogen ◽  
Cmcase Activity ◽  
Sds Page ◽  
Extracellular Protein Production ◽  
Rdna Analysis

A highly cellulolytic bacterium was locally isolated from rice straw and identified as Stenotrophomonas maltophilia. Identification of the isolate based on the morphological, cultural and biochemical characteristics was confirmed with 16S rDNA analysis. The bacterium showed the highest level of reducing sugar and extracellular protein production when incubated for 3 days (348.75 μg/ml and 288.5 μg/ml respectively) at 40°C temperature (463.0 μg/ ml and 333.0 μg/ml respectively) and pH 6.5 (360.0 μg/ml and 349.0 μg/ml respectively) in Winstead’s broth having 1.5% CMC and 0.2% Yeast Extract as carbon and nitrogen source respectively. Crude cellulase enzymes produced by the bacterium showed the highest CMCase activity rather than FPase, Avicelase and ²-Glucosidase activities. Cellulase activity of the crude enzyme was also determined using the same parameters. The crude cellulase enzyme showed the highest CMCase activity when incubated for 60 minutes (232.5 U/ml), at pH 6.5 (105.0 U/ml), 35°C temperature (69.75 U/ml) using CMC and Peptone as carbon and nitrogen source respectively. Crude cellulase showed the highest activity in presence of mercury and SDS as metal and detergent respectively. Substrate specificity and SDS-PAGE analysis reveals that the cellulase may be an endo-1,4-glucanase. Bangladesh J Microbiol, Volume 37 Number 1 June 2020, pp 15-22

scholarly journals Improvement of carboxymethyl cellulase production from Chaetomium cellulolyticum NRRL 18756 by mutation and optimization of solid state fermenttion

1970 ◽  
Vol 40 (2) ◽  
pp. 139-147 ◽  
Author(s):  
Eman M Fawzi ◽  
Hossam S Hamdy
Keyword(s):  
Solid State ◽  
Solid State Fermentation ◽  
Industrial Process ◽  
Tween 80 ◽  
Cellulase Production ◽  
Potential Candidate ◽  
Wild Type ◽  
Carboxymethyl Cellulase ◽  
Optimal Moisture Content ◽  
Initial Ph

Cellulase producing fungus Chaetomium cellulolyticum NRRL 18756 was subjected to various doses of gamma irradiation to enhance the production of the industrially important enzyme carboxymethyl cellulase (CMCase). Among all the mutants tested, M-7 obtained through 0.5 KGy irradiation showed highest extracellular CMCase production which is 1.6-fold higher than that of the wild type. Optimal conditions for the production of CMCase by the mutant fungal strain using solid-state fermentation were examined. The optimized medium consisted of sugarcane bagasse supplemented with 1% (w/w) peptone, 2.5mM MgSO4, and 0.05% (v/w) Tween 80. Optimal moisture content and initial pH was 40% (v/w) and 5.0-6.5, respectively. The medium was fermented at 40° C for 4 days. The resulting CMCase yield was 4.0-fold more than that of the wild type strain grown on the basal wheat bran medium. Some characteristics of partially purified CMCase from the mutant and wild type of C. cellulolyticum were investigated. The partially purified mutant CMCase was more stable than the wild type CMCase. Thus, the higher thermostability of mutant CMCase makes it a potential candidate for commercial and industrial process. Key words: Chaetomium cellulolyticum; Carboxymethyl cellulase; Mutation; Optimization; Solid state fermentation DOI: http://dx.doi.org/10.3329/bjb.v40i2.9769   Bangladesh J. Bot. 40(2): 139-147, 2011 (December)

scholarly journals Parametric Optimization of Cultural Conditions for Carboxymethyl Cellulase Production Using Pretreated Rice Straw by Bacillus sp. 313SI under Stationary and Shaking Conditions

2014 ◽  
Vol 2014 ◽  
pp. 1-7 ◽  
Author(s):  
Varsha Goyal ◽  
Arpana Mittal ◽  
Anish Kumari Bhuwal ◽  
Gulab Singh ◽  
Anita Yadav ◽  
...  
Keyword(s):  
Rice Straw ◽  
Cellulase Activity ◽  
Nitrogen Sources ◽  
Cellulase Production ◽  
Cellulosic Biomass ◽  
Ecological Niches ◽  
Bacillus Sp ◽  
Carboxymethyl Cellulase ◽  
Cultural Conditions ◽  
Optimized Conditions

Carboxymethyl cellulase (CMCase) provides a key opportunity for achieving tremendous benefits of utilizing rice straw as cellulosic biomass. Out of total 80 microbial isolates from different ecological niches one bacterial strain, identified as Bacillus sp. 313SI, was selected for CMCase production under stationary as well as shaking conditions of growth. During two-stage pretreatment, rice straw was first treated with 0.5 M KOH to remove lignin followed by treatment with 0.1 N H2SO4 for removal of hemicellulose. The maximum carboxymethyl cellulase activity of 3.08 U/mL was obtained using 1% (w/v) pretreated rice straw with 1% (v/v) inoculum, pH 8.0 at 35°C after 60 h of growth under stationary conditions, while the same was obtained as 4.15 U/mL using 0.75% (w/v) pretreated substrate with 0.4% (v/v) inoculum, pH 8.0 at 30°C, under shaking conditions of growth for 48 h. For maximum titre of CMCase carboxymethyl cellulose was optimized as the best carbon source under both cultural conditions while ammonium sulphate and ammonium nitrate were optimized as the best nitrogen sources under stationary and shaking conditions, respectively. The present study provides the useful data about the optimized conditions for CMCase production by Bacillus sp. 313SI from pretreated rice straw.

Pengaruh Penambahan Molases Pada Kulit Pisang Kapendis Untuk Media Produksi Xilanase B.Stearothermophillus DSM 22

2019 ◽  
Vol 15 (3) ◽  
Author(s):  
Trismillah
Keyword(s):  
Enzyme Activity ◽  
Ammonium Sulfate ◽  
Banana Peel ◽  
Partial Purification ◽  
Temperature Conditions ◽  
Cavendish Banana ◽  
Working Volume ◽  
Initial Ph ◽  
Xylanase Enzyme

Cavendish banana peel can be used as a substitute for the expensive xylan, while molasses than as a source of carbon as well as nitrogen, minerals and nutrients needed for the growth of microbes that can produce the enzyme. Xylanase produced from Bacillus stearothermopillus DSM 22, using media cavendish banana peels with the addition of molasses 1%, 2%, and 3%. Fermentation is done in a shaker incubator at 550C temperature conditions, initial pH 8, and 250 rpm agitation. The result showed the highest enzyme activity of 4,14 ± 0,16 U/mL min., on the addition 2% molasses after 24 hours. Further fermentation carried out in the fermenter working volume of 3.5 liters, with the condition of temperature 550C, pH 8, aeration 1 vvm, agitation 250 rpm, the highest spesific enzyme of activity of 51,62 ± 0,16 U/mg after 24 hours. Partial purification of xylanase enzyme fermentation is done with the results of microfiltration, ultrafiltration, ammonium sulfate (0-80%) and dialysis. There is an increase in the purity of the enzyme at each stage of purification, the highest purity on dialysis 3.23 times of crude enzymes.Kulit buah pisang kapendis dapat digunakan sebagai pengganti xilan yang harganya mahal, sementara molases selain sebagai sumber karbon serta nitrogen, mineral dan nutrisi dibutuhkan untuk pertumbuhan mikroba yang dapat menghasilkan enzim. Xilanase yang dihasilkan dari Bacillus stearothermopillus DSM 22, menggunakan media kulit pisang kapendis dengan penambahan molase 1%, 2%, dan 3%. Fermentasi dilakukan dalam shaker inkubator pada temperatur 550C, pH awal 8, dan agitasi 250 rpm. Hasilnya menunjukkan aktivitas enzim tertinggi 4,14 ± 0,16 U/mL min., pada penambahan 2% molases setelah 24 jam. Selanjutnya fermentasi dilakukan di dalam fermentor, volume kerja dari 3,5 liter, dengan kondisi temperatur 550C, pH 8, aeration 1 vvm, agitasi 250 rpm, aktivitas spesifik tertinggi 51,62 ± 0,16 U/mg setelah 24 jam. Pemurnian parsial fermentasi enzim xilanase dilakukan dengan hasil mikrofiltrasi, ultrafiltrasi, amonium sulfat (0-80%) dan dialisis. Ada peningkatan kemurnian enzim pada setiap tahap pemurnian, kemurnian tertinggi pada dialisis 3,23 kali dari enzim kasar.Keywords: Xylanase, B. stearothermophillus DSM 22, Cavendish banana peel, molasses, enzyme activity

scholarly journals Wild type Bacillus subtilis treated with ethyl methyl sulphonate produced catabolite insensitive mutants with improved cellulase production

2021 ◽  
Author(s):  
Oladipo Olaniyi
Keyword(s):  
Bacillus Subtilis ◽  
Carbon Source ◽  
Enzyme Production ◽  
Cellulase Activity ◽  
Cellulase Production ◽  
Minimal Salt Medium ◽  
Salt Medium ◽  
Production Medium ◽  
Wild Type ◽  
Ethyl Methyl

Abstract The goal of this present investigation was to mutagenize Bacillus subtilis with Ethyl Methyl Sulphonate (EMS), screen the mutants for cellulase production and evaluate the influence of different glucose concentrations on their cellulase production potentials. The wild type B. subtilis was treated with 20, 40, 60 and 80 µl of EMS and the mutants generated were screened for cellulase production in minimal salt medium containing carboxylmethylcellulose (CMC) as the carbon source. Quantitatively, cellulase activity and protein contents were determined by dinitrosalicylic acid and Lowry methods respectively. Seven mutants were developed from each of the EMS concentration bringing the total to twenty-eight from all the concentrations. Approximately 14 and 57% of the mutants developed from 40 and 60µl of EMS had higher cellulase activities than the wild type, while none of the mutants developed from 20 and 80 µl of EMS had better activities than the wild type. The supplementation of 0.2, 0.5, 1.0 and 1.5% glucose in enzyme production medium caused approximately 100, 14, 29 and 14% cellulase repression respectively in the mutants developed from 60µl EMS. Mutants MSSS02 and MSSS05 were considered as catabolite insensitive mutants because their cellulase production were enhanced in comparison to wild type.

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