scholarly journals Induction of Cellulase Biosynthesis by Cellobiose Octaacetate in Aspergillus humicola

1970 ◽  
Vol 23 (2) ◽  
pp. 174-176 ◽  
Author(s):  
Meher Nigad Nipa ◽  
Sharmin Sultana ◽  
M Abdul Hakim

Aspergillus humicola, one of the major cellulase-producing fungi, was used in this study for carboxymethylcellulase (CMCase) production using Winstead's basal broth supplanted with cellobiose octaacetate (COA), a synthetic carbon source. Under all conditions, the enzyme biosynthesis was remarkably increased when the inducer COA was added to the production medium containing carboxymethylcellulose (CMC). Maximum enzyme production (1.62 U/ml) was achieved in COA-containing at 37°C. The enzyme production was highest at initial pH 5.5 and after 7 days incubation. The enzyme exhibited maximum activity at 40°C with a reaction pH 5.5. CMCase activity was inhibited by its own substrate CMC at concentration higher than 1.0%. The study clearly demonstrated that COA is a good inducer for extracellular CMCase production by the fungus. Keywords: Aspergillus humicola, Carboxymethylcellulase (CMCase), Carboxymethylcellulose (CMC), Cellobiose octaacetate (COA)DOI: http://dx.doi.org/10.3329/bjm.v23i2.889 Bangladesh J Microbiol, Volume 23, Number 2, December 2006, pp 174-176

2021 ◽  
Author(s):  
Oladipo Olaniyi

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.


Hoehnea ◽  
2018 ◽  
Vol 45 (1) ◽  
pp. 134-142 ◽  
Author(s):  
Flaviane Lopes Ferreira ◽  
Cesar Barretta Dall'Antonia ◽  
Emerson Andrade Shiga ◽  
Larissa Juliani Alvim ◽  
Rosemeire Aparecida Bom Pessoni

ABSTRACT The aim of the present work was to assess the enzymatic activity of six strains of filamentous fungi grown in liquid media containing 1% sugarcane bagasse as the sole carbon source. All fungal strains were able to use this agro-industrial residue, producing various types of enzymes, such as cellulases, xylanases, amylases, pectinases, and laccases. However, Aspergillus japonicus Saito was the most efficient producer, showing the highest enzymatic activity for laccase (395.73 U L-1), endo-β-1,4-xylanase (3.55 U mL-1) and β-xylosidase (9.74 U mL-1) at seven, fourteen and twenty-one days in culture, respectively. Furthermore, the endo-β-1,4-xylanases and β-xylosidases of A. japonicus showed maximum activity at 50°C, and pH 5.5 and pH 3.5-4.5, respectively. Thus, these results indicate that A. japonicus has a great biotechnological potential for the production of these enzymes using sugarcane bagasse as the sole source of carbon.


2013 ◽  
Vol 2013 ◽  
pp. 1-11 ◽  
Author(s):  
Deepmoni Deka ◽  
Saprativ P. Das ◽  
Naresh Sahoo ◽  
Debasish Das ◽  
Mohammad Jawed ◽  
...  

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.


1970 ◽  
Vol 24 (1) ◽  
pp. 70-72 ◽  
Author(s):  
Sanit Kumar Das ◽  
M Zobaidul Alam ◽  
M Abul Manchur ◽  
M Nural Anwar

The cellulolytic mesophilic isolate Streptomyces albolongus (A5) was used to determine the effect of nitrogen and carbon sources on the production of cellulolytic enzymes using cellobiose octaacetate (COA) as an inducer. The isolate was able to degrade various cellulosic carbon sources. However, the rate of degradation, production of extracellular protein, reducing sugar, saccharification and production of enzyme were enhanced when 0.6% COA was used as an inducer in addition to the main substrate. Among the nitrogen sources tested, beef extract showed maximum production of the enzyme (136.7 U/ml CMCase) in Winstead's medium. The enzyme production was further enhanced in the medium supplemented with 0.6% COA, which corresponded to 154.69 U/ml CMCase activity. Among the carbon sources, carboxymethylcellulose (CMC) was found to be the best carbon source and again supplementation of the medium with 0.6% COA enhances CMCase production. Other than CMCase activity, the organism also produced appreciable levels of filter paper cellulase (FPase), avicelase and â-glucosidase activities.Keywords: Streptomyces albolongus, Carboxymethylcellulose (CMC), Cellobiose octaacetate (COA), InductionDOI: http://dx.doi.org/10.3329/bjm.v24i1.1243   Bangladesh J Microbiol, Volume 24, Number 1, June 2007, pp 70-72


2013 ◽  
Vol 3 (2) ◽  
Author(s):  
Amrullah Hamdan Rahmadani ◽  
Evi Susanti

AbstrakAvicelase dan CMCase mewakili aktivitas eksoselulase dan endoselulase, termasuk dua dari tiga jenis selulase dalam sistem selulase yang dihasilkan oleh Bacillus circulans. Ekspresi keduanya sangat dipengaruhi oleh jumlah dan jenis sumber karbon dalam media produksi. Penelitian ini bertujuan mengetahui jenis dan konsentrasi limbah pertanian terbaik untuk menghasilkan avicelase dan CMCase dari B. circulans serta kemampuan sistem selulase tersebut untuk mendegradasi substrat lignoselulosa. Limbah pertanian yang diteliti berupa ampas tebu, bonggol jagung dan sekam. Limbah pertanian tersebut digunakan sebagai satu-satunya sumber karbon pada media produksi. Avicel digunakan sebagai sumber karbon pembanding. Aktivitas avicelase dan CMCase ditentukan berdasar jumlah gula pereduksi yang dihasilkan dengan menggunakan metoda Somogy-Nelson. Hasil penelitian menunjukkan bahwa semua limbah pertanian yang diteliti berpotensi sebagai sumber karbon yang lebih baik dibandingkan dengan avicel untuk produksi avicelase dan CMCase dari B. circulans. Limbah pertanian yang terbaik adalah ampas tebu. Penggunaan ampas tebu pada konsentrasi 0,5 % menghasilkan aviselase dan CMCase sebesar 309,39 dan 405,48 U/mL. Sistem selulase yang dihasilkan mampu mendegradasi ampas tebu, bonggol jagung dan sekam.Kata kunci : avicelase, CMCase, limbah pertanian, sumber kabon, Bacillus circulansAbstractAvicelase and CMCase activity represent exocellulase and endocellulase, including two of the three types of cellulase in the cellulase system produced by Bacillus circulans. Expression both of them strongly influenced by the amount and type of carbon source in the production medium. The aims of this research were to determine the type and concentration of the best agricultural waste to generate avicelase and CMCase from B. circulans and their ability to degrade lignocellulosic substrates. Studied agricultural wastes are bagasse, corn stalks and husks. Agricultural waste is used as the sole carbon source in media production. Avicel is used as a comparable carbon source. Avicel and CMCase activity are determined based on the amount of the reducing sugars is generated by using the method of Somogy - Nelson. The results showed that all the studied agricultural waste was a potential carbon source better than ethical for avicelase and CMCase production from B. circulans. Agricultural waste bagasse was the best one. The use of 0.5 % bagasse produce CMCase and aviselase at 309.39 and 405.48 U / mL respectively. The resulting system was able to degrade bagasse , corn stalks and husks.Keywords : avicelase , CMCase , agricultural waste , carbon sources , Bacillus circulans


2019 ◽  
Vol 32 (2) ◽  
pp. 213-222
Author(s):  
Wafaa H. Khassaf ◽  
Alaa K. Niamah ◽  
Alaa J. A. Al-Manhel

The present study was aimed to test optimum conditions for the levan production from local isolation Bacillus subtilis subsp. subtilis w36, which was isolated from Basrah city soil by using production medium containing (40 g of sucrose as carbon source 10g pepton, 1g (NH4) 2SO4, 1g KH2PO4, 1g MgSO4.7H2O). The amount of levan produced was 4.9 g.ml-1. Molasses and date juice were used as substitutes for sucrose in growth media and substitute percentages were (25%, 50%, 75% and100%). The results showed the highest production of levan was recorded when sucrose was substituted with 25% molasses, which was 5.2 g.ml-1.Therefore, this medium was used to study optimum conditions included incubation period, inoculation volume, temperature ,initial pH. The highest production of levan was 6.8 g .100 ml-1 within 40 hours' incubation, 1 ml inoculum volume, pH 6.5 and 32 ºC.


1981 ◽  
Vol 27 (12) ◽  
pp. 1298-1305 ◽  
Author(s):  
Michael A. Pickard

Ten strains of Caldariomyces fumago and related fungi were found to produce extracellular chloroperoxidase when grown on a glucose – malt extract medium. High enzyme levels and pigment production were observed for C. fumago ATCC 16373 and C. fumago CMI 89362. Removal of malt extract from the medium and the replacement of glucose by fructose as the carbon source provided a defined medium which, by comparison with the complex medium, produced the following results with both fungal strains. Chloroperoxidase was produced to similar levels, with maximum production after 6 days rather than 12 days of growth; pigmentation of the medium was reduced by 90% and the pH of the medium remained constant, thus stabilizing enzyme activity. Addition of urea or proline as a nitrogen supplement to nitrate enhanced enzyme production by strain CMI 89362. Comparison of the two strains indicated that CMI 89362 produced higher levels of chloroperoxidase than ATCC 16373.


1970 ◽  
Vol 16 (9) ◽  
pp. 841-844 ◽  
Author(s):  
Robert G. Brown

Penicillium funiculosum, Penicillium lilacinum, and Spicaria violacea produced excellent yields of dextranase if ketodextran replaced dextran as a carbon source. Ketodextrans I and II having degrees of substitution of 2 and 20% respectively were used in this study. P. funiculosum grew equally well on dextran and ketodextran I but less well on ketodextran II. Addition of a readily metabolizable carbohydrate such as glucose, sucrose, or galactose stimulated growth on ketodextran II, resulting in better dextranase production. However, excess glucose reversed this increase in enzyme production. Replacement of an inorganic nitrogen source with an organic one further stimulated dextranase production during growth of P. funiculosum on ketodextran II.


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