scholarly journals Xylanase Production by Isolated Fungal Strain, Aspergillus fumigatus RSP-8 (MTCC 12039): Impact of Agro-industrial Material as Substrate

Sugar Tech ◽  
2015 ◽  
Vol 18 (1) ◽  
pp. 29-38 ◽  
Author(s):  
K. Ravichandra ◽  
V. V. N. Yaswanth ◽  
B. Nikhila ◽  
Jamal Ahmad ◽  
P. Srinivasa Rao ◽  
...  
Keyword(s):  
Aspergillus Fumigatus ◽  
Fungal Strain ◽  
Xylanase Production ◽  
Industrial Material

scholarly journals Substract and temperature effect on xylanase production by aspergillus fumigatus using low cost agricultural wastes

2016 ◽  
pp. 915-921 ◽  
Author(s):  
Arthur Filipe Sousa Gomes ◽  
Bruna Silveira Lamanes dos Santos ◽  
Emanuele Giuliani Franciscon ◽  
Milla Alves Baffi
Keyword(s):  
Aspergillus Fumigatus ◽  
Temperature Effect ◽  
Low Cost ◽  
Agricultural Wastes ◽  
Xylanase Production

scholarly journals Banana Peels: A Promising Substrate for the Coproduction of Pectinase and Xylanase from Aspergillus fumigatus MS16

2020 ◽  
Vol 69 (1) ◽  
pp. 19-26
Author(s):  
MAHWISH ZEHRA ◽  
MUHAMMAD NOMAN SYED ◽  
MUHAMMAD SOHAIL
Keyword(s):  
Solid State ◽  
Aspergillus Fumigatus ◽  
Solid State Fermentation ◽  
Enzyme Preparation ◽  
Ph Value ◽  
Sole Source ◽  
Xylanase Production ◽  
Nutritional Factors ◽  
Factors Affecting ◽  
Aspergillus Fumigates

Banana peels (BP), an under-utilized waste material, was studied for the production of xylanase and pectinase by Aspergillus fumigates MS16. The factors affecting the co-production of both the enzymes were separately studied for their influence under submerged (Smf) and solid-state fermentation (SSF) of BP. The strain was cultivated in the presence of mineral salt (MS) solution containing BP powder as a sole source of carbon and physical and nutritional factors varied to observe the change in the enzyme titers. The data revealed that the MS-based medium was appropriate for the production of both the enzymes; therefore, in subsequent experiments, the same medium was used. A temperature of 30–35°C was found better for the production of the two enzymes under Smf; however, the titers of pectinase dropped significantly at 40°C. Contrarily, xylanase production was inhibited at 40°C under SSF but not under Smf. Whereas, supplementation of xylan or pectin to BP induced the production of xylanase and pectinase, respectively. Lowering the pH value favored the production of both the enzymes under Smf; however, the production of pectinase improved significantly when a higher concentration of BP (1%) was used compared to the concentration (0.25%) required for the production of xylanase. Interestingly, the enzyme preparation obtained under SSF exhibited optimal activities of both the enzymes at higher temperatures when compared to those obtained under Smf. The data indicated that the physiology of the fungus differed greatly when the cultivation pattern varied from Smf to SSF and, hence, the enzymes produced were characteristically distinct.

scholarly journals Aspergillus fumigatusNITDGPKA3 Provides for Increased Cellulase Production

2014 ◽  
Vol 2014 ◽  
pp. 1-9 ◽  
Author(s):  
Nibedita Sarkar ◽  
Kaustav Aikat
Keyword(s):  
Aspergillus Fumigatus ◽  
Rice Straw ◽  
Fermentation Broth ◽  
High Titer ◽  
Xylanase Activity ◽  
Cellulase Production ◽  
Reducing Sugar ◽  
Crude Enzyme ◽  
High Concentration ◽  
Xylanase Production

A cellulolytic fungal strain,Aspergillus fumigatusNITDGPKA3, was isolated from straw retting ground. Cellulase and xylanase production byA. fumigatusNITDGPKA3 in submerged fermentation of rice straw was studied. The culture conditions for maximum enzyme production were found to be initial pH 4, 1% substrate concentration, temperature 30°C, incubation time 5 days, 0.2% tryptone as nitrogen source, and inoculum volumes 7% v/v (for cellulase) and 5% v/v (for xylanase). Addition of Tween 80 in fermentation broth improved xylanase production (193.58 IU/ml) much more compared to cellulase production (6.53 IU/ml). Xylanase activity found in the culture broth was approximately 50% higher compared to most of the reported data. The crude enzyme was further applied for reducing sugar production from alkali pretreated rice straw, where a dosage of 40 IU/g CMCase produced 0.522 g reducing sugar/g dry substrate after 36 hours which was higher than that in the reported literature. The high concentration of reducing sugar yield was most probably due to the extraordinarily high titer ofβ-glucosidase (80.1 IU/ml) found in the crude enzyme. The crude enzymes secreted byAspergillus fumigatusNITDGPKA3 efficiently hydrolyzed alkali pretreated rice straw suggesting thatAspergillus fumigatusNITDGPKA3 is a robust microorganism.

scholarly journals A Thermostable Crude Endoglucanase Produced by Aspergillus fumigatus in a Novel Solid State Fermentation Process Using Isolated Free Water

2012 ◽  
Vol 2012 ◽  
pp. 1-6 ◽  
Author(s):  
Abdul A. N. Saqib ◽  
Ansa Farooq ◽  
Maryam Iqbal ◽  
Jalees Ul Hassan ◽  
Umar Hayat ◽  
...  
Keyword(s):  
Free Energy ◽  
Solid State ◽  
Vapor Pressure ◽  
Aspergillus Fumigatus ◽  
Wheat Straw ◽  
Solid State Fermentation ◽  
Fermentation Process ◽  
Free Water ◽  
Fungal Strain ◽  
Ssf Process

Aspergillus fumigatus was grown on chopped wheat straw in a solid state fermentation (SSF) process carried out in constant presence of isolated free water inside the fermentation chamber. The system allowed maintaining a constant vapor pressure inside the fermentor throughout the fermentation process. Crude endoglucanase produced by A. fumigatus under such conditions was more thermostable than previously reported enzymes of the same fungal strain which were produced under different conditions and was also more thermostable than a number of other previously reported endoglucanases as well. Various thermostability parameters were calculated for the crude endoglucanase. Half lives (T1/2) of the enzyme were 6930, 866, and 36 min at 60°C, 70°C, and 80°C, respectively. Enthalpies of activation of denaturation (ΔHD*) were 254.04, 253.96, and 253.88 K J mole−1, at 60°C, 70°C and 80°C, respectively, whereas entropies of activation of denaturation (ΔSD*) and free energy changes of activation of denaturation (ΔGD*) were 406.45, 401.01, and 406.07 J mole−1 K−1 and 118.69, 116.41, and 110.53 K J mole−1 at 60°C, 70°C and 80°C, respectively.

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