Application and characterization of crude fungal lipases used to degrade fat and oil wastes (original) (raw)
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New Biotechnology, 2011
Marine fungus BTMFW032, isolated from seawater and identified as Aspergillus awamori, was observed to produce an extracellular lipase, which could reduce 92% fat and oil content in the effluent laden with oil. In this study, medium for lipase production under submerged fermentation was optimized statistically employing response surface method toward maximal enzyme production. Medium with soyabean meal-0.77% (w/v); (NH 4 ) 2 SO 4 -0.1 M; KH 2 PO 4 -0.05 M; rice bran oil-2% (v/v); CaCl 2 -0.05 M; PEG 6000-0.05% (w/v); NaCl-1% (w/v); inoculum-1% (v/v); pH 3.0; incubation temperature 35 8C and incubation period-five days were identified as optimal conditions for maximal lipase production. The time course experiment under optimized condition, after statistical modeling, indicated that enzyme production commenced after 36 hours of incubation and reached a maximum after 96 hours (495.0 U/ml), whereas maximal specific activity of enzyme was recorded at 108 hours (1164.63 U/mg protein). After optimization an overall 4.6fold increase in lipase production was achieved. Partial purification by (NH 4 ) 2 SO 4 precipitation and ion exchange chromatography resulted in 33.7% final yield. The lipase was noted to have a molecular mass of 90 kDa and optimal activity at pH 7 and 40 8C. Results indicated the scope for potential application of this marine fungal lipase in bioremediation.
2015
During this study three Aspergillus species (A.niger, A. paraciticus and A. aculeatus) were screened for lipase production shown with varying lipolytic activities. The most active one was A. niger followed by A. paraciticus. On the other hand, the least lipase productive organism was A. aculeatus. The fermentation was carried out in shake flask culture employing a liquid media than results was compared with control, and found that all three fungal strains were shown lipase production. Effect of various factors (carbon, nitrogen, time period, pH, temperature, activator and inhibitor) on production of fungal lipase, result were shown that carbon source Tween-20, nitrogenous source -yeast extract , temperature 35°C and 55°C, pH 9 and 10 supported the production of lipase activity in fermentation media, whereas glycerol and peptone showed moderate effects. Mostly Co Mg, Zn, Mn & Fe act as enhancer of fungal lipase activity, only in few fungal species they inhibit lipase activity where a...
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.
Journal of Basic Microbiology, 2010
Extracellular lipase production by Aspergillus sp. (RBD-01) was monitored by modulating pH of the growth medium, ambient temperature for growth, source of nitrogen and percentage of carbon (virgin cottonseed oil). This strain was observed to be viable and produces lipase even up to 50% oil as a main carbon source. Maximum lipase activity of 21.8 U/ml was obtained with 50% (v/v) oil acting as the main carbon source and peptone (0.5% w/v) as nitrogen source. The optimum pH and temperature for enzymatic activity were observed to be 7.5 and 35 °C, respectively. The observations are of significance due to limited reports on use of 50% of oil as the main carbon source while obtaining significant lipase activity of 21.8 U/ml.
Bioprocess and biosystems engineering, 2018
In this study, we evaluated the concentration of lipases from Aspergillus niger using efficient and low-cost methods aiming at application in the treatment of waste cooking oils. The change in ionic strength of the medium by the addition of salt and precipitation with ethanol increased the specific activity from 2.90 to 28.50 U/mg, resulting in a purification factor of 9.82-fold. The use of acetone resulted in a specific activity of 33.63 U/mg, resulting in a purification factor of 11.60-fold. After that, the concentrated lipase was used in the hydrolysis of waste cooking oil and 753.07 and 421.60 µmol/mL of free fatty acids were obtained for the enzyme precipitated with ethanol and acetone, respectively. The hydrolysis of waste cooking oil catalyzed by homemade purified lipase in ultrasonic media can be considered a pretreatment of oil by converting a significant amount of triglycerides into free fatty acids.
Catalytic Properties of Lipase Extracts from Aspergillus niger
Screening of lipolytic strains using Rhodamine-B/olive oil plate technique allowed the selection of Aspergillus niger MYA 135. Lipase production in submerged culture containing 2 % olive oil was enhanced by more than 50 % compared to basal cultural conditions. Optimal catalytic conditions for olive oil-induced lipase were pH=6.5 and 30-35°C. These values were shifted to the acid region (4.0-6.5) and 35-37°C when lipase extract was produced under basal conditions. Slight changes of the residual lipase activity against the pH were found. However, preincubation at either 37 or 40°C caused an increase in the olive oil-inducible lipolytic activity. On the contrary, lipase residual activity decreases in the 30-55°C range when it was produced in basal medium. Lipolytic extracts were almost not deactivated in presence of 50 % water-miscible organic solvents. However, water-immiscible aliphatic solvents reduced the lipase activity between 20 and 80 %.
2020
Present scenario demands a more sustainable, ecofriendly and economic measures globally to deal with the growing problems of environmental issues. The main goal of this work is to opt for such ideas and technologies which involve cleaner and greener procedures for utilizing waste materials for deriving value added products. The soil pertaining to the areas of oil mills contains densely population of various microbes’, especially fungal origin. These microbes are rich in lipase content (due to oil source). Thus in this we isolated fungal colonies from this oil rich soil, cultured in laboratory, fermented them under various conditions to extract fungal enzyme i.e. lipase and then used it for further applications. Lipases are highly versatile and industrially important enzymes. Deriving the lipases from waste soil is the main attraction of this work and is a venture strategizing the “best from waste” approach.
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.
Biodegradation activity of Aspergillus niger Lipase isolates from a Tropical Country Garage
Microbial biodegradation of oil pollutants and their derivations has become the most environmental-friendly method in the developing world. Lipolytic enzyme; Aspergillus niger extracted from oil polluted soil has been studied, examined and found to degrade Polyaromatic Hydrocarbons found in petroleum contaminated soil. A. niger can produce Bio-Surfactant at 25 °C and 35 °C that can biodegrade oil hydrocarbons. 24 hours at 35 °C it can reduce surface tension from 55 Nm/m to 25.3 Nm/m at different percentages of crude oil.