scholarly journals Production of polygalacturonase by Aspergillus niger BC23 isolated from Irvingia gabonensis (African mango) fruit

2016 ◽  
Vol 70 (6) ◽  
pp. 717-724
Author(s):  
Nwokoro Ogbonnaya ◽  
Eze Chukwuemeka
Keyword(s):  
Enzyme Activity ◽  
Aspergillus Niger ◽  
Enzyme Production ◽  
Carbon Sources ◽  
Orange Peel ◽  
Relative Activity ◽  
Maximum Activity ◽  
Citrus Pectin ◽  
Enzyme Productivity ◽  
Irvingia Gabonensis

Polygalacturonase was produced from Aspergillus niger BC 23 which was isolated from spoiled Irvingia gabonensis fruit. The influence of carbon substrates on enzyme production showed that the medium containing sucrose produced a maximum enzyme yield of 38.5 U/mg protein after 72 h. Enzyme productivity in this medium was much higher than in the medium that contained only citrus pectin as the sole carbon source. Medium containing yeast extract as a nitrogen source caused the production of specific enzyme activity of 31.2 U/mg protein. Results on the effect of metal ions on enzyme activity showed that Ca2+ gave a percent relative activity of 214% in comparison to the native enzyme activity. The enzyme showed maximum activity in slight acid and neutral pH media with optimal activity at pH 4.0. Temperature activity profile of the enzyme showed best activity at a temperature of 35?C. Dried fruit peels were tested for their abilities to support enzyme production in a media devoid of citrus pectin. The best enzyme productivity of 102.3 U/mg protein was achieved after 72 h in the medium containing orange peel and this level was much higher than that achieved when pure carbon sources or citrus pectin alone were used for enzyme production.

scholarly journals EFFECT OF GROUNDNUT CAKE AND SOYA BEANS ON ENHANCED CITRIC ACID PRODUCTION FROM PAWPAW AND ORANGE PEEL BY MUTANTS OF ASPERGILLUS NIGER

2019 ◽  
Vol 17 (1) ◽  
pp. 147-155
Author(s):  
H. T. BALOGUN-ABIOLA ◽  
S. O. KAREEM ◽  
R. B. AFOLABI ◽  
O. A. AKINLOYE
Keyword(s):  
Citric Acid ◽  
Solid State ◽  
Aspergillus Niger ◽  
Mutant Strain ◽  
Fermentation Process ◽  
Carbon Sources ◽  
Orange Peel ◽  
Nitrogen Sources ◽  
Groundnut Cake ◽  
Mutant Strains

This present study was concerned with the biosynthesis of citric acid (CA) with mutant strain of Aspergillus niger using pawpaw and orange peel as substrates by solid state fermentation process. The A. niger strain isolated from spoilt orange was identified, screened for CA production on Czapek-Dox Agar and subjected to mutation by ethidium bromide. The effect of carbon sources, nitrogen sources and substrates were also determined.  Among the mutant strains, A. niger PJ-02 A120 was found to be the best mutant that produced citric acid (65.00±0.58f) after 48 hours in Vogel’s medium. The effects of carbon sources (sucrose and glucose) on CA production from each substrate (orange and pawpaw peel) using mutant A. niger PJ-02 was determined and sucrose, the best carbon source was combined with two the nitrogen sources (groundnut cake and soyabeans) to determine the most suitable supplement for CA production. Groundnut cake enhances the production of citric acid while soyabeans was inhibitory. Citric acid was further produced in pawpaw peel and orange peel medium containing sucrose (5 %) groundnut cake (2 %), methanol (1.5 %) and the mutant strain. The orange peel substrates yielded 112.07g/kg of CA while 107.17g/kg was recorded for pawpaw peel when fermented for 5 days at 30°C. The Production of citric acid with mutant Aspergillus niger proved better with orange peel than pawpaw peel when optimized with alcohol.      

Synthesis of Pectin Methylesterase from Aspergillus niger in Submerged Fermentation Using as Citrus Pectin and Orange Peel as Inducers

2018 ◽  
Vol 14 (4) ◽  
pp. 212-221
Author(s):  
Jonaina Pili ◽  
Cindy Elena Bustamante Vargas ◽  
Carolina Elisa Demaman Oro ◽  
Geciane Toniazzo Backes ◽  
Eunice Valduga ◽  
...  
Keyword(s):  
Aspergillus Niger ◽  
Submerged Fermentation ◽  
Orange Peel ◽  
Pectin Methylesterase ◽  
Citrus Pectin

scholarly journals Screening of bacterial strains for pectate lyase production and detection of optimal growth conditions for enhanced enzyme activity

2017 ◽  
Vol 9 (1) ◽  
pp. 370-374 ◽  
Author(s):  
Monidipta Saha ◽  
Rajib S. Rana ◽  
Biswanath Adhikary ◽  
Sabyasachi Mitra
Keyword(s):  
Enzyme Production ◽  
Pectate Lyase ◽  
Optimal Growth ◽  
Growth Conditions ◽  
Relative Activity ◽  
Subtilis Strain ◽  
Bacterial Strains ◽  
Apple Pectin ◽  
Citrus Pectin ◽  
Lyase Activity

In the present study, the pectatelyase production by fifty two bacterial strains isolated from ramie grown soils were studied and the strain RDSM01 showed maximum pectate lyase activity. According to sequence homology of Genbank, the strain RDSM01 was identified as Bacillus subtilis (Genbank Accession No. KX035109). Maximum pectate lyase activity of the strain was observed when 1.5% (v/v) inoculum was added to the growth medium and was incubated for 48 hours at 34-370C and at pH 7.0. The relative activity of the strain was 19% higher when apple pectin was used as carbon source compared to citrus pectin. Maximum enzyme production (149.1 – 153.4 IU/ml) was recorded when ammonium chloride or ammonium sulphate at 0.4% concentration was used as nitrogen source. Thus, B. subtilis strain RDSM01 possessing high pectate lyase activity may be effectively utilized for removal of gum from ramie fibre, which is primarily made of pectin and hemicellulose.

scholarly journals Immobilization of Aspergillus niger F7-02 Lipase in Polysaccharide Hydrogel Beads of Irvingia gabonensis Matrix

2014 ◽  
Vol 2014 ◽  
pp. 1-7 ◽  
Author(s):  
Safaradeen Olateju Kareem ◽  
Olayinka Quadri Adio ◽  
Michael Bamitale Osho
Keyword(s):  
Aspergillus Niger ◽  
Specific Activity ◽  
Temperature Stability ◽  
Relative Activity ◽  
Formaldehyde Solution ◽  
Hydrogel Beads ◽  
Bead Size ◽  
Size Number ◽  
Irvingia Gabonensis ◽  
Activity Yield

The potential of polysaccharide Irvingia gabonensis matrix as enzyme immobilization support was investigated. Lipase of Aspergillus niger F7-02 was immobilized by entrapment using glutaraldehyde as the cross-linking agent and stabilized in ethanolic-formaldehyde solution. The pH and temperature stability and activity yield of the immobilized enzyme were determined. Such parameters as enzyme load, bead size, number of beads, and bead reusability were also optimized. Adequate gel strength to form stabilized beads was achieved at 15.52% (w/v) Irvingia gabonensis powder, 15% (v/v) partially purified lipase, 2.5% (v/v) glutaraldehyde, and 3 : 1 (v/v) ethanolic-formaldehyde solution. There was 3.93-fold purification when the crude enzyme was partially purified in two-step purification using Imarsil and activated charcoal. Optimum lipase activity 75.3 Ug−1 was achieved in 50 mL test solution containing 15 beads of 7 mm bead size. Relative activity 80% was retained at eight repeated cycles. The immobilization process gave activity yield of 59.1% with specific activity of 12.3 Umg−1 and stabilized at optimum pH 4.5 and temperature 55°C. Thus the effectiveness and cost-efficiency of I. gabonensis as a polymer matrix for lipase immobilization have been established.

scholarly journals Optimization of Pectinase and Protease Produced from Bacillus subtilis Isolated from Market Waste

2021 ◽  
pp. 48-57
Author(s):  
C. Anab-Atulomah ◽  
E. Nwachukwu
Keyword(s):  
Enzyme Activity ◽  
Bacillus Subtilis ◽  
Large Scale ◽  
Carbon Sources ◽  
Maximum Activity ◽  
Molecular Technique ◽  
Laboratory Unit ◽  
Optimum Activity ◽  
Significant Difference ◽  
Different Temperatures

Aims: The objective of the study was to produce and optimize protease and pectinase from Bacillus subtilis isolated from market waste. Place and Duration of Study: Department of Microbiology (laboratory unit), Michael Okpara University of Agriculture Umudike, Abia State Nigeria. Methodology: The production and optimization of protease and pectinase from bacteria isolated from solid market waste was investigated. Isolated bacteria from the waste were screened for protease and pectinase production using skim milk agar and pectin agar respectively. Using morphological, biochemical and molecular technique the enzymes producing isolate was confirmed as Bacillus subtilis. Protease and Pectinase were produced by Bacillus subtilis using submerged fermentation in gelatin broth and pectin broth respectively. The enzymes were purified using ammonium sulphate precipitation, dialysis and ion-exchange chromatography. Optimization using different temperatures, pH and nutrient sources was done. Enzyme activity was measured. Results: Purified protease exhibited maximum activity of 8.72U/ml at 40oC while pectinase exhibited maximum activity of 8.98U/ml at 50oC. Glucose as a carbon source and peptone as a nitrogen source gave optimum activity for both enzymes. Both pectinase and protease exhibited optimum activity at pH 9. There was significant difference (P=.05) in enzyme activity at different temperatures, pH and nitrogen sources for both protease and pectinase. There was no significant difference in pectinase activity at P=.05 for the different carbon sources while there was significant difference for protease activity for the different carbon sources at P=.05. Conclusion: Production of microbial enzymes such as protease and pectinase from waste material is an eco-friendly process and cheaper option for large scale use of enzymes in industry.

scholarly journals A novel Thermothelomyces heterothallicus PA2S4T fungus isolated from the soil induces chitinase production using orange peel flour

2021 ◽  
Vol 17 (9) ◽  
Author(s):  
Victoria Pommer ◽  
Paula Daniela Helfenstein Rother ◽  
Letícia Mara Rasbold ◽  
José Luis Da Conceição Silva ◽  
Alexandre Maller ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Enzymatic Activity ◽  
Carbon Sources ◽  
Orange Peel ◽  
Biotechnological Application ◽  
Optimum Ph ◽  
Chitinase Production ◽  
Stationary Conditions ◽  
Agricultural Industries ◽  
Optimum Ph And Temperature

Chitinases are enzymes capable of hydrolysing the β-1,4 bonds of chitin releasing chitooligosaccharides and N-acetylglucosamine and are widely used in food, pharmaceutical, and agricultural industries. Microorganisms are potential producers of this enzyme; however, there are no reports in the literature on the production of chitinase by fungi of the genus Thermothelomyces. Thus, this work aimed to investigate the production of extracellular chitinase using alternative carbon sources by the fungus isolated from soil, Thermothelomyces heterothallicus PA2S4T. The fungus was cultivated in a liquid medium supplemented with carbon sources and incubated at 40°C under stationary conditions for seven days. Orange peel flour was the best inducer for extracellular chitinase, with 82.3 U/mL of enzymatic activity. The highest production of chitinase was obtained on the tenth day, and the optimum pH and temperature for enzyme activity were 4.5 and 50ºC, respectively. Therefore, the fungus T. heterothallicus PA2S4T proved to be promising in the production of extracellular chitinase, which presents pH and temperature characteristics favourable to biotechnological application.

scholarly journals PRODUKSI ENZIM LIPASE DARI Aspergillus niger ISOLAT KAPANG KOPRA DENGAN MENGGUNAKAN MEDIUM KELAPA PARUT

KOVALEN ◽  
2017 ◽  
Vol 3 (3) ◽  
pp. 269
Author(s):  
Indah Indah ◽  
Mappiratu Mappiratu ◽  
Musafira Musafira
Keyword(s):  
Enzyme Activity ◽  
Aspergillus Niger ◽  
Water Content ◽  
High Activity ◽  
Incubation Time ◽  
Enzyme Production ◽  
Block Design ◽  
Lipase Enzyme ◽  
Randomized Block Design

The investigation about the lipase enzyme production from Aspergillus niger using grated coconut as a medium has been done. The aim of the study is to determine the best incubation time, pH and water content which produced lipase enzyme with high activity. Randomized Block Design (RBD) with 2 factorial pattern (incubation time and pH of the medium) was used in this research. Each factor consists of three levels and it was done in the triple. The level of incubation time and of pH were 48, 60, 72 hours and pH 5, 6, and 7, respectively. The observed parameter was the obtained lipase enzyme activity. The result showed that the highest activity was achieved at pH 7 for 48 hours of incubation time with 45% of water content. The amount of lipase enzyme activity was 1.70 µmol/ml.minutes.Keywords: mold coconut, Aspergillus niger, lipase

scholarly journals Partial purification and biochemical characterization of a new highly acidic NYSO laccase from Alcaligenes faecalis

2020 ◽  
Vol 18 (1) ◽  
Author(s):  
Soad A. Abdelgalil ◽  
Ahmad R. Attia ◽  
Reyed M. Reyed ◽  
Nadia A. Soliman
Keyword(s):  
Enzyme Activity ◽  
Sodium Dodecyl ◽  
Alcaligenes Faecalis ◽  
Maximum Activity ◽  
Sodium Oxalate ◽  
Partial Purification ◽  
Bromophenol Blue ◽  
Bromocresol Purple ◽  
Laccase Enzyme

Abstract Background Due to the multitude industrial applications of ligninolytic enzymes, their demands are increasing. Partial purification and intensive characterization of contemporary highly acidic laccase enzyme produced by an Egyptian local isolate designated Alcaligenes faecalis NYSO were studied in the present investigation. Results Alcaligenes faecalis NYSO laccase has been partially purified and intensively biochemically characterized. It was noticed that 40–60% ammonium sulfate saturation showed maximum activity. A protein band with an apparent molecular mass of ~ 50 kDa related to NYSO laccase was identified through SDS-PAGE and zymography. The partially purified enzyme exhibited maximum activity at 55 °C and pH suboptimal (2.5–5.0). Remarkable activation for enzyme activity was recognized after 10-min exposure to temperatures (T) 50, 60, and 70 °C; time elongation caused inactivation, where ~ 50% of activity was lost after a 7-h exposure to 60 °C. Some metal ions Cu2+, Zn2+, Co2+, Ni2+, Mn2+, Cd2+, Cr2+, and Mg2+ caused strong stimulation for enzyme activity, but Fe2+ and Hg2+ reduced the activity. One millimolar of chelating agents [ethylenediamine tetraacetic acid (EDTA), sodium citrate, and sodium oxalate] caused strong activation for enzyme activity. Sodium dodecyl sulfate (SDS), cysteine-HCl, dithiothreitol (DTT), β-mercaptoethanol, thioglycolic acid, and sodium azide caused strong inhibition for NYSO laccase activity even at low concentration. One millimolar of urea, imidazole, kojic acid, phenylmethylsulfonyl fluoride (PMSF), H2O2, and Triton X-100 caused activation. The partially purified NYSO laccase had decolorization activity towards different dyes such as congo red, crystal violet, methylene blue, fast green, basic fuchsin, bromophenol blue, malachite green, bromocresol purple eriochrome black T, and Coomassie Brilliant Blue R-250 with various degree of degradation. Also, it had a vast range of substrate specificity including lignin, but with high affinity towards p-anisidine. Conclusion The promising properties of the newly studied laccase enzyme from Alcaligenes faecalis NYSO strain would support several industries such as textile, food, and paper and open the possibility for commercial use in water treatment. It will also open the door to new applications due to its ligninolytic properties in the near future.

Bioprocess optimisation for high cell density endoinulinase production from recombinant Aspergillus niger

2021 ◽  
Author(s):  
Pfariso Maumela ◽  
Shaunita Rose ◽  
Eugene van Rensburg ◽  
Annie Chimphango ◽  
Johann Gorgens
Keyword(s):  
Growth Rate ◽  
Aspergillus Niger ◽  
Cell Density ◽  
Enzyme Production ◽  
High Cell Density ◽  
Nitrogen Concentration ◽  
High Cell ◽  
Feed Concentration ◽  
Volumetric Activity ◽  
Activity Increase

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.

Convenient Partial Purification of Glucose Oxidase from Aspergillus niger A9 Fermentation Broth by Reversed Micelles

2012 ◽  
Vol 554-556 ◽  
pp. 957-961
Author(s):  
Hong An ◽  
Xi Feng He ◽  
Shu Gang Gao
Keyword(s):  
Enzyme Activity ◽  
Aspergillus Niger ◽  
Glucose Oxidase ◽  
Fermentation Broth ◽  
Volume Ratio ◽  
Reversed Micelles ◽  
Partial Purification ◽  
Ammonium Bromide ◽  
Ultrasonic Oscillation ◽  
Protein Activity

Aim of this work was to establish the optimum conditions for the extraction and recovery by cationic reversed micelles of glucose oxidase (GOX) from Aspergillus niger A9, The influence of pH, temperature, solvent/co-solvents ratio on the extraction was investigated by experiment, using the residual enzyme activity to evaluate the results. The best condition for GOX extraction were ensured using iso-octane as solvent and butanol and n-hexanol co-solvent at 76/18/6 volume ratio, pH 4.80, 200mM cetyl-trimethyl ammonium bromide (CTAB) as cationic surfactant, The enzyme activity of GOX is measured by DNS method (3,5-dinitro salicylic acid method). In the extraction process, ultrasonic oscillation was adopted to mix organic solvent and water, ultrasonic oscillation temperature is 45 °C. Protein activity recovery of GOX can reach 88.2% in extraction.

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