scholarly journals Optimal Conditions For Production Acidic D-Xylanase By Aspergillus niger in Submerged Fermentation

2011 ◽  
Vol 5 (3) ◽  
pp. 14-21
Author(s):  
Muhamed Omar Abdulatif ◽  
Hyder H. Assmaeel ◽  
Raghad kadhim Obeid ◽  
Ayat Adnan Abbas

he Xylanase producing strain Aspergillus niger was isolated from soil on potato dextrose agar in the presence of xylan as its first substrate for primary isolation, and then grown under liquid medium fermentation in the presence of crude xylan (rice husk) to produce D-Xylanase. the optimum conditions were determined as follows: the Optimum pH for xylanase production was found pH 5.0, xylanase was induced by xylan (rice husk) 0.1% and the production was (61.221 U/ml) and nitrogen source Yeast extract recorded highest enzyme production( 89.71 U/ml), and repressed by carbon source xylose the highest enzyme production (88.69 U/ml). The optimum temperature was 40°с for xylanase production was (35.15 U/ml), the optimum period after 7 days of incubation was (52.33 U/ml) ,the optimum substrate concentration 0.1% was (45.95 U/ml), and the optimum inoculum size was 1 x 106 (spore /ml) recorded (57.19 U/ml ).

2020 ◽  
Vol 11 (4) ◽  
pp. 11187-11201

This work's objective was the extracellular production, partial characterization, and immobilization of the enzymes fructosyltransferase (Ftase) and β-fructofuranosidadase (Ffase) by filamentous fungi. Aspergillus niger ATCC 9642 and Penicillium brasilianum were evaluated for the production of fructosyltransferase (Ftase) and β-fructofuranosidadase (FASE) enzymes. The A. niger presented the highest activity of FTase (24.86 µmol/min.mL) and FFase (28.68 µmol/min.mL) in medium composed of 20% sucrose, 0.5% yeast extract, 1% NaNO3, 0.05% MgSO4.7 H2O, 0.25% KH2PO4, 0.5% NH4Cl and 0.25% NaCl inoculated using 5x107spores/mL and incubated at 25°C, pH 5.5, 150 rpm for 48 h. Presenting optimum pH and temperature of 2.39 and 60°C. Thermal stability has shown that the enzyme FFase is more thermally stable when compared to FTase. Stability against different pHs showed similar behavior for FTase and FFase; the optimum pH being between 2.0 and 3.0. FTase and FFase showed storage stability in freezing and refrigeration temperature for approximately 400 h. The kinetic parameters, Km and Vmax, for the sucrose substrate were 24.60mM and 104.16 μmol/min.mL for FTase and 3.91mM and 20.24 μmol/min.mL for FFase. The immobilization process displayed a yield of 6744.66% for FFase and 3928.90% for FTase, with enzymatic activities of 364.79 U/g and 220.34 U/g, and 4 and 3 times reuse, respectively.


Author(s):  
Farooq Abubakar Atiku ◽  
Vahid Pirouzfar ◽  
Chia-Hung Su ◽  
Sung-Yen Wei

Abstract Ethylene is one of the most primary and widely used petrochemical products in today’s world and is considered as a chemical building block in the petrochemical industry. In this research, ethylene production from ethane and natural gas is evaluated in terms of cost and optimum conditions. Also, a comprehensive economic and technical comparison is made to achieve the optimal conditions for ethylene production concerning feed diversity. Nowadays most ethylene production units run with ethane feed. If it is possible to implement gas-ethylene processes with an inexpensive natural gas feed, it will be a significant step for technical and economic optimization. Thus, some methods are introduced and compared, and finally an economic review about best condition for ethylene production from ethane and natural gas/investment with regard to cost and economic efficiency of the methods is provided. The investment cost for Gas to Ethylene (GTE) and Ethane to Ethylene (ETE) processes is 363–701 million dollars per year, respectively. Also, rate of return (ROR) of 24 and 19% is calculated for GTE and ETE processes, respectively.


2021 ◽  
Author(s):  
Pfariso Maumela ◽  
Shaunita Rose ◽  
Eugene van Rensburg ◽  
Annie Chimphango ◽  
Johann Gorgens

Abstract Endoinulinases gene was expressed in recombinant Aspergillus niger for selective and high-level expression using an exponential fed-batch fermentation. The effects of the growth rate (µ), glucose feed concentration, nitrogen concentration and fungal morphology, on enzyme production were evaluated. A recombinant endoinulinases with a molecular weight of 66 KDa was secreted. Endoinulinases production was growth associated at µ> 0.04 h -1 , which is characteristic of the constitutive gpd promoter used for the enzyme production. The highest volumetric activity (670 U/ml) was achieved at a growth rate of 93% of µ max (0.07 h -1 ), while enzyme activity (506 U/ml) and biomass substrate yield (0.043 g biomassDW /g glucose ) significantly decreased at low µ (0.04 h -1 ). Increasing the feed concentration resulted in high biomass concentrations and viscosity, which necessitated high agitation for improved mixing and oxygen. However, the high agitation and low DO levels (ca. 8% of saturation) led to pellet disruption and growth in mycelial morphology. Enzyme production profiles, product (Y p/s ) and biomass (Y x/s ) yield coefficients were not affected by feed concentration and morphological change. The gradual increase in the concentration of nitrogen sources showed that, a nitrogen limited culture was not suitable for endoinulinases production in recombinant A. niger. Moreover, the increase in enzyme volumetric activity was still directly related to an increase in biomass concentration. An increase in nitrogen concentration, from 3.8 to 12 g/L, resulted in volumetric activity increase from 393 to 670 U/ml, but the Y p/s (10053 U/g glucose ) and Y x/s (0.049 g biomasDWs /g glucose ) did not significantly change. The data demonstrated the potential of recombinant A. niger and high cell density fermentation for the development of largescale endoinulinases production system.


2016 ◽  
Vol 29 (1) ◽  
pp. 222-233 ◽  
Author(s):  
TAMIRES CARVALHO DOS SANTOS ◽  
GEORGE ABREU FILHO ◽  
AILA RIANY DE BRITO ◽  
AURELIANO JOSÉ VIEIRA PIRES ◽  
RENATA CRISTINA FERREIRA BONOMO ◽  
...  

ABSTRACT: Prickly palm cactus husk was used as a solid-state fermentation support substrate for the production of cellulolytic enzymes using Aspergillus niger and Rhizopus sp. A Box-Behnken design was used to evaluate the effects of water activity, fermentation time and temperature on endoglucanase and total cellulase production. Response Surface Methodology showed that optimum conditions for endoglucanase production were achieved at after 70.35 h of fermentation at 29.56°C and a water activity of 0.875 for Aspergillus niger and after 68.12 h at 30.41°C for Rhizopus sp. Optimum conditions for total cellulase production were achieved after 74.27 h of fermentation at 31.22°C for Aspergillus niger and after 72.48 h and 27.86°C for Rhizopus sp. Water activity had a significant effect on Aspergillus niger endoglucanase production only. In industrial applications, enzymatic characterization is important for optimizing variables such as temperature and pH. In this study we showed that endoglucanase and total cellulase had a high level of thermostability and pH stability in all the enzymatic extracts. Enzymatic deactivation kinetic experiments indicated that the enzymes remained active after the freezing of the crude extract. Based on the results, bioconversion of cactus is an excellent alternative for the production of thermostable enzymes.


2013 ◽  
Vol 48 (1) ◽  
pp. 25-32 ◽  
Author(s):  
S Islam ◽  
B Feroza ◽  
AKMR Alam ◽  
S Begum

Pectinase activity among twelve different fungal strains, Aspergillus niger IM09 was identified as a potential one to produce maximal level 831 U/g at pH 4.0. Media composition, incubation temperature, incubation time, substrate concentration, aeration, inoculum size, assay temperature and nitrogen sources were found to effect pectinase activity. Moisture content did not affect the activity significantly. Media composition was varied to optimize the enzyme production in solid state fermentation. It was observed that the highest pectinase activity of 831.0 U/g was found to produce in presence of yeast extract as a nitrogen source in combination with ammonium sulfate in assay media. Aeration showed positive significant effects on pectinase production 755 U/g at 1000 ml flasks. The highest pectinase production was found at 2 g pectin (521 U/g) used as a substrate. Pectinolytic activity was found to have undergone catabolite repression with higher pectin concentration (205 U/g at 5 g pectin). The incubation period to achieve maximum pectinase activity by the isolated strain Aspergillus niger IM09 was 3 days, which is suitable from the commercial point of view. DOI: http://dx.doi.org/10.3329/bjsir.v48i1.15410 Bangladesh J. Sci. Ind. Res. 48(1), 25-32, 2013


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