Optimization of medium and process parameters for the production of lipase from an oil-tolerant Aspergillus sp. (RBD-01) (original) (raw)
Related papers
Journal of Basic Microbiology, 2010
Under the current assay conditions, lipase production in mineral medium was only detected in the presence of vegetable oils, reaching the highest specific activity with olive oil. In this way, effect of different environmental conditions on fungal morphology and olive oil-induced extracellular lipases production from Aspergillus niger MYA 135 was studied. It was observed that addition of 1.0 g l -1 FeCl 3 to the medium encouraged filamentous growth and increased the specific activity 6.6 fold after 4 days of incubation compared to the control. However, major novelty of this study was the satisfactory production of an acidic lipase at initial pH 3 of the culture medium (1.74 ± 0.06 mU μg -1 ), since its potencial applications in food and pharmaceutical industry are highly promising.
Botanica, 2022
Lipase enzyme-mediated processes have biological significance and tremendous potential in various industrial and technological areas due to the enzymatic properties and broad specificity for a wide spectrum of substrates. This research involved the production of hydrolytic lipase enzyme by Aspergillus terreus extracted from petroleum-contaminated soil and optimising the environmental parameters that may affect lipase production. Hydrolytic lipase enzyme activity of the isolated Aspergillus terreus from petroleum-contaminated soil was undertaken in submerged fermentation. Dry cell weight, lipase enzyme pellets, and lipase enzyme concentration by measuring the percentage transmission by spectrophotometry were measured to determine the effects of various abiotic factors (pH, temperature, carbon and nitrogen sources, lipid substances and vegetable oils) affecting cell growth and lipase enzyme production by Aspergillus terreus on modified lipase production media. The results showed a precipitate on Tween 20 and a bright pink-fluorescent halo on the rhodamine B agar plate. After temperature adjustment to 35 °C, statistical analysis showed that Aspergillus terreus produced a dry cell weight of 3.14 g/L and a lipase enzyme pellet of 0.33 g with a spectrophotometric transmission of 0.03%. The sucrose substrate displayed a dry cell weight of 3.11 g/L and a lipase enzyme pellet of 1.15 g. Spectrophotometric analysis showed that sucrose, glucose and peptone had a similarity in transmission at p = 0.321. The addition of Neem oil improved enzyme yield as a dry cell weight of 3.02 g/L and a lipase enzyme pellet of 0.95 g was obtained. Statistically, sunflower and tributyrin similarly affected enzyme production by showing a spectrophotometric transmission at p = 0.024. This study has indicated that Aspergillus terreus could be employed as a reliable source of lipase enzymes for industrial processes due to its stability across different abiotic factors.
International Journal of Food Science & Technology, 2014
Lipase from Aspergillus sp. obtained by solid-state fermentation (SSF) on wheat bran (LWB), soybean bran (LSB) and soybean bran combined with sugarcane bagasse (LSBBC) were 67.5, 58 and 57.3 U of crude lipase per gram substrate, respectively. The optimum pH of activity and stability of the LWB was between 8 and 9, and the optimum temperature of activity and stability was 50°C and up to 60°C, respectively. The LSB and LSBBC showed two peaks of optimum pH (4 and 6) and optimal values of temperature and stability at 50°C. The LSB was stable in the pH range of 6-7, while LSBBC in the range of pH 4-7. All the enzymes show activities on p-nitrophenyl esters (butyrate, laurate and palmitate). LWB stood out either on the hydrolysis of sunflower oil, presenting 66.1% of the activity over commercial lipase and on the esterification of oleic acid and ethanol, surpassing the activities of the commercial lipases studied. The thin layer chromatography showed that LWB and LSB have produced ethyl esters from corn oil, while LWB produced it from sunflower oil.
2018
Lipases are the enzymes of choice for applications in a large number of industries. Present study describes the isolation of potent lipolytic fungal strains and their subsequent production by using shake flasks fermentation technique. The selected isolate was identified as Aspergillus terreus, based on morphological features and 18s rRNA sequencing. Seven different culture media were analyzed for the extracellular lipase production employing A. terreus as the production organism and it was found that M6 gave maximum lipase production i.e., 5.0 U/mL/min in the medium containing (% w/v) MgSO4, 0.05; NaNO3, 0.05; KCl, 0.05; KH2PO4, 0.2; olive oil, 1.0; pH 6.0. Maximum production of lipase (7.66 U/mL/min) was found at a medium pH of 6.0 and an incubation temperature of 30C after 72 hrs of incubation period. An increase in the lipase production (7.99 U/mL/min) was observed when the production medium was provided with 1.0% peptone, 2.0% glucose and 1.0% olive oil. Ammonium sulphate precip...
Investigation of low-temperature lipase production and enzymatic properties of Aspergillus Niger
Iranian Journal of Chemistry & Chemical Engineering-international English Edition, 2021
To obtain the optimum fermentation medium and circumstances for extracellular lipase construction (as an important biocatalyst and promising industrial enzyme) by Aspergillus Niger, the fermentation conditions of Aspergillus Niger were optimized by single factor and response surface design, the enzymatic properties of the crude enzyme were studied. The results displayed that the optimum fermentation medium was soluble starch 4%, (NH4)2SO4 0.1%, K2HPO4 0.1%, MgSO4·7H2O 0.05%, peptone 3%, olive oil 1.05% and initial pH 7. The optimal fermentation conditions were 30℃, the sample size was 26 mL/250 mL and the shaking speed was 213 r/min. The optimized lipase activity was 1.55 U/mL, which was 7.75 times of the pre-optimized lipase. It was found that when the pH value of lipase was 7.0, the activity of lipase reached its maximum value of 79.3±6.82%. When pH value was between 6.0 and 8.0, the activity of lipase could be kept above 60% and the stability was good. At the same time, through t...
Extracellular lipase produced by Aspergillus japonicus was tested for its activity on sesame, groundnut and sunflower oil substrates. The enzyme showed significant activity in the pH range of 6-8 and a temperature range of 300C-400C but with sunflower oil, the activity is optimum at 500C. This is indicative of the substrate playing a role in the optimization of physico-chemical characteristics affecting the enzyme activity. Of the eleven metal ions tested, only Mg2+ (2mM) enhanced the enzyme activity while others, inhibited. EDTA significantly (P <0.05) enhanced the enzyme activity suggesting that metal ions do not in general affect the lipase isolated from A. japonicus. Organic solvents and acids tested showed significant (P< 0.05) enhancement of the lipase activity at higher concentrations, presumably because of their influence on the interfacial area. Km and Vmax values of the partially purified lipase determined from Lineweaver Burk and Eadie-Hofstee plots were 63.09 (mM/L), 5.33 (mM/L/min) and 71.76 (mM/L), 5.25 (mM/L/min) respectively
Evaluation of lipase activity in some Aspergillus species
Lipase is an enzyme which is able to hydrolyze the esters and breakdown the triglycerides into glycerol and fatty acids. This enzyme is so noteworthy in organic chemistry and industry. Fungi are one of the microorganisms producing this enzyme. In this paper, screening was done between 10 species of fungi, Aspergillus, to determine lipase activity. A specific medium containing minerals and soybean oil was used in order to induce the lipase production. Three days after inoculation, amount of the enzyme was evaluated every other day for 20 days. Evaluation was done using colorimetric method with substrate para-nitrophenyl palmitate in wavelength 410 nm by a spectrophotometer. According to the results, all isolates were able to produce the lipase and degrade the triglyceride; but the most lipase activities were related to Aspergillus caespitosus and A. Ostianus 39.9 U/ml and 36.01 U/ml respectively. The most biomass production was related to A. caespitosus. These native isolates with high lipase production potential can be new candidates to industrially produce lipase.
Biomedicine and Biotechnology, 2014
An enzyme with various commercial purpose, lipase is a carboxy esterase enzyme with many uses in different industries. Multiple isolates of Aspergillus niger were isolated from oil contaminated soil samples and screened for lipase producing ability on tributyrin medium. The isolate showing maximum activity was identified and subjected to growth parameters optimization in attempt to increase the enzyme producing ability of the isolate in larger scale. Different media with varying composition were examined for best lipase production. The activities of the lipase produced by the fungus at various pH were assessed. The enzyme activity was determined by the titration method. Maximum lipase activity of 2.4 U/ml was achieved with organic nitrogen rich media (designated as PM II) at pH 7 on the sixth day of culture. The lipase production was scaled up on a pilot scale in a 5 Liter fermenter maintaining growth parameters of pH 7, temperature at 28°C, stirrer rate at 120 rpm, airflow rate at 30 L/hr, O2 saturation 50% and pressure 0.05 MPa. The crude enzyme was extracted for further assays. Optimization of the parameters can improve the productivity as well as the quality of the enzyme produced.
Production of acidic lipase by Aspergillus niger in solid state fermentation
Among the various fungal strains screened for lipase production, Rhizopus arrhizus NCIM 877, 878, 879 and Aspergillus niger NCIM 1207 produced significant quantities of enzyme when grown in synthetic oil based (SOB) medium under submerged conditions. Rhizopus strains showed major intracellular activity while A. niger NCIM 1207 produced mainly extracellular activity. Lipase production in A. niger NCIM 1207 was studied using both submerged fermentation (SmF) and solid state fermentation (SSF). De novo biosynthesis of lipase occurred only in the presence of lipid substrate and was completely repressed by glucose. The highest yields of enzyme were obtained in SSF using wheat bran as solid substrate in combination with olive oil as lipid substrate. Maximum lipase activity (630 IU/g dry solid substrate) was recovered when fermented wheat bran was extracted with NaCl (1%) supplemented with Triton X-100 (0.5%). The pH and temperature optima for lipase were 2.5 and 45 8C, respectively. The enzyme also exhibited high activity (75%) at extremely acidic pH of 1.5. Lipase activity (63%) was retained when enzyme was incubated in a buffer of 2.5 for 24 h at room temperature. The enzyme retained 63% of its original activity on incubation at 70 8C for 5 h. This organism, being GRAS cleared, can be used for large-scale production of enzyme for commercial purpose.