scholarly journals Application and characterization of crude fungal lipases used to degrade fat and oil wastes

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Amira Hassan Alabdalall ◽  
Norah A. Al-Anazi ◽  
Lena A. Aldakheel ◽  
Fatma H. I. Amer ◽  
Fatimah A. Aldakheel ◽  
...  
Keyword(s):  
Aspergillus Niger ◽  
Incubation Period ◽  
Lipase Activity ◽  
Tween 80 ◽  
Lipase Production ◽  
Industrial Applications ◽  
Waste Oil ◽  
Liquid Detergent ◽  
Optimal Incubation

AbstractAspergillus niger MH078571.1 and A. niger MH079049.1 were identified previously as the two highest Aspergillus niger strains producing lipase. Biochemical characterizations of lipase activity and stability for these two strains were examined and revealed that the optimal temperature is 45 °C at pH 8for A. niger MH078571.1 and 55 °C for MH079049.1. The lipase production of both strains was studied on medium contains waste oil, as a cheap source to reduce the industrial cost, showed that the optimal incubation period for the enzyme production is 3 days. Moreover, an experiment on lipase activates in organic solvents demonstrated that 50% of acetone is the best solvent for the two strains. In the presence of surfactants, 0.1% of tween 80 surfactant showed the best lipase activities. Furthermore, Mg2+ and Zn2+ ions enhanced the lipase activity of A. niger MH078571.1, while Na2+ and Cu2+ enhanced the enzyme activity of A. niger MH079049.1. Lipase activity was also tested for industrial applications such as integrating it with different detergents. Maximum lipase activity was obtained with 1% of Omo as a powder detergent for both strains. In liquid detergent, 0.1% of Fairy showed maximum lipase activity in A. niger MH078571.1, while the lipase in A. niger MH079049.1 was more effective in 1% of Lux. Moreover, the degradation of natural animal fat with crude enzyme was tested using chicken and sheep fats. The results showed that more than 90% of fats degraded after 5 days of the incubation period.

scholarly journals Rhamnolipid and lipase production by Pseudomonas aeruginosa san-ai: the process comparison analysis by statistical approach

2013 ◽  
Vol 67 (4) ◽  
pp. 677-685 ◽  
Author(s):  
Sonja Jakovetic ◽  
Zorica Knezevic-Jugovic ◽  
Sanja Grbavcic ◽  
Dejan Bezbradica ◽  
Natasa Avramovic ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Lipase Activity ◽  
Sunflower Oil ◽  
Hydrolytic Enzymes ◽  
Tween 80 ◽  
Lipase Production ◽  
Fermentation Time ◽  
Process Comparison ◽  
Central Composite Experimental Design ◽  
Oil Concentration

Pseudomonas aeruginosa was repeatedly reported as powerful producer of rhamnolipid biosurfactants as well as producer of hydrolytic enzymes. In this study effects of four fermentation factors were evaluated using response surface methodology and experiments were performed in accordance with a four-factor and five-level central composite experimental design. Investigated factors were: fermentation temperature, time of fermentation, concentration of sunflower oil and concentration of Tween? 80. The most important finding was that regression coefficients of the highest values were those that describe interactions between factors and that they differ for lipase and rhamnolipid production, which were both investigated in this study. Production of both metabolites was optimized and response equations were obtained, making it possible to predict rhamnolipid concentration or lipase activity from known values of the four factors. The highest achieved rhamnolipid concentration and lipase activity were 138 mg dm-3 (sunflower oil concentration 0.8 %, Tween? 80 concentration 0.05 %, temperature 30?C, and fermentation time 72 h) and 11111 IU dm-3(sunflower concentration of 0.4 %, Tween? 80 concentration of 0.05 %, temperature of 30?C, and fermentation time of 120 h), respectively.

scholarly journals OPTIMIZATION AND CHARACTERIZATION OF EXO-POLYGALACTURONASE BY Aspergillus niger CULTURED VIA SOLID STATE FERMENTATION

2018 ◽  
Vol 81 (1) ◽  
Author(s):  
Halifah Pagarra ◽  
Roshanida A. Rahman ◽  
Nur Izyan Wan Azelee ◽  
Rosli Md Illias
Keyword(s):  
Solid State ◽  
Aspergillus Niger ◽  
Moisture Content ◽  
Solid State Fermentation ◽  
Incubation Time ◽  
Industrial Applications ◽  
Screening Process ◽  
Industrial Sectors ◽  
Polygalacturonase Production

Polygalacturonases represent an important member of pectinases group of enzymes with immense industrial applications. The activity of exo-polygalacturonase produced by Aspergillus niger was studied in solid state fermentation (SSF) using Nephrolepis biserrata leaves as substrate. Central composite design (CCD) was used to optimize four significant variables resulted from the screening process that has been initially analyzed for the production of exo-polygalacturonase which are incubation time, temperature, concentration of pectin and moisture content. The optimum exo-polygalacturonase production obtained was 54.64 U/g at 120 hours of incubation time, temperature at 340C, 5.0 g/L of pectin concentration and 75.26% of moisture content. For partial characterization of exo-polygalacturonase, the optimum temperature and pH were obtained at 50°C and pH 4.0, respectively. SDS-PAGE analysis showed that molecular weight of exo-polygalacturonase were 35 and 71 kDa. This study has revealed a significant production of exo-polygalacturonase by A. niger under SSF using cheap and easily available substrate and thus could found immense potential application in industrial sectors and biotechnology

scholarly journals Production, Purification and Characterization of Extracellular Lipase from a Mutated Strain of Penicillium Citrinum KU613360

2021 ◽  
pp. 111-120
Author(s):  
Lakkakula Bhagya Lakshmi ◽  
M Raghu Ram
Keyword(s):  
Wild Strain ◽  
Strain Improvement ◽  
Lipase Production ◽  
Industrial Applications ◽  
Penicillium Citrinum ◽  
Extracellular Lipase ◽  
Purification And Characterization ◽  
Sds Page ◽  
Guntur District

In the present study lipase production, purification and characterization were carried out with a novel fungal strain of Penicillium citrinum KU613360 isolated from vegetable oil contaminated soil samples collected from oil mills located in and around Guntur District, Andhra Pradesh, India. The strain improvement was carried out by subjecting the strain to both UV and Ethidium Bromide treatments. The wild strain of P. citrinum KU613360 showed maximum lipase activity of 1.053±0.32IUmL-1 on optimized medium and while the mutated strain treated with combination of UV (300 sec) and Et Br (200 µgcm3), recorded the enzyme activity of 4.260±0.011IUmL-1, using the optimised medium at 6.5 pH and 40°C temperature. Thus, a 404% enhancement in the activity was achieved by using induced mutation on wild strain of P. citrinum KU613360. The molecular weight of the purified lipase from the mutated strain was found to be 35 kDa, when analysed on SDS PAGE. From our results it was concluded that the mutated strain has considerable capability and potentiality to be used in various industrial applications.

scholarly journals Molecular, physiological, and biochemical characterization of extracellular lipase production by Aspergillus niger using submerged fermentation

PeerJ ◽  
2020 ◽  
Vol 8 ◽  
pp. e9425
Author(s):  
Amira Hassan Alabdalall ◽  
Norah Ayad ALanazi ◽  
Sumayh A. Aldakeel ◽  
Sayed AbdulAzeez ◽  
J. Francis Borgio
Keyword(s):  
Genetic Diversity ◽  
Carbon Source ◽  
Nitrogen Source ◽  
Lipase Activity ◽  
Submerged Fermentation ◽  
Lipase Production ◽  
Group Method ◽  
Phenol Red ◽  
Optimal Conditions

Background Extracellular production of fungal lipases especially the lipases obtained from the Aspergilli has gained immense interest in recent years due to its diverse biotechnological applications. In this study, we focused on determining the fermentation parameters required for the optimal lipase production. Methods A total of 256 fungal isolates were obtained from oil seeds. From each genus, one isolate was selected to evaluate lipase production using phenol red and tributyrin plate assays. Lipase activity was estimated using the spectrophotometric pNPP hydrolysis assay. The highest lipase producer isolates were identified using 18S ribosomal RNA gene sequencing. The genetic variability was determined by random amplified polymorphic DNA (RAPD) analysis and the dendrogram was constructed using the unweighted pair group method with arithmetic averages method. The isolates were examined in a submerged fermentation culture (Smf) to measure the effect of temperature, pH, incubation time, carbon source, nitrogen source, inoculum volume, and lipid source on lipase production. Results Eleven isolates belonging to the genus Aspergillus were analyzed for lipase production where they were found to be the highest lipase producers among various fungal genera. All the tested isolates were identified as A. niger using 18s rRNA sequencing. Genetic diversity was evaluated among all of the studied A. niger isolates using RAPD primers. The RAPD primers were used to amplify 285 loci, of which five were polymorphic (1.75%) and seven were monomorphic (2.45%). Thus, a high level of genetic diversity was observed among all isolates. The tributyrin test and the lipase activity assay identified five strains of A. niger as high lipase producers, and their optimal enzyme activities were 709.74, 532.54, 735.64, 794.62, and 787.69 U/ml. The optimal conditions for lipase production were as follows: 40 °C, pH 7.5, 1% fructose as the carbon source, 1% yeast extract as the nitrogen source, 2% palm oil, 2.5 × 107 spores/ml suspension, and 3 days of incubation. Conclusions The current study provides a comprehensive characterization of the optimal conditions, which are essential to enhance lipase production in five A. niger isolates.

scholarly journals Characterization of an acidophilic α-amylase from Aspergillus niger RBP7 and study of catalytic potential in response to nutritionally important heterogeneous compound

2018 ◽  
Vol 62 (1) ◽  
pp. 75-82 ◽  
Author(s):  
Riddha Mukherjee ◽  
Tanmay Paul ◽  
Suman Kumar Halder ◽  
Jyoti Prakash Soren ◽  
Amrita Banerjee ◽  
...  
Keyword(s):  
Aspergillus Niger ◽  
Tween 80 ◽  
Potato Peel ◽  
Catalytic Potential ◽  
Nacl Concentration ◽  
Comparable Activity ◽  
Tween 60 ◽  
Ph Range ◽  
Rice Fish

An acidophilic α-amylase from Aspergillus niger RBP7 was purified after solid state fermentation on potato peel substrate. Molecular mass of the purified α-amylase was 37.5 kDa and it exhibited 1.4 mg/ml and 0.992 μ/mol/min Km and Vmax values, respectively. The enzyme was stable in the pH range from 2.0 to 6.0, at high NaCl concentration (3 M) and at temperatures between 40 °C and 70 °C. The enzyme showed an optimal activity at pH 3.0 and at 45 °C. The enzyme was inhibited by Hg2+ and was stable in the presence of different surfactants (Tween 60, Tween 80, and SDS at 1% level) and different inhibitory reagents (β-mercaptoethanol, phenylmethylsulfonyl fluoride, and sodium azide). This acidophilic amylase enzyme can digest heterogeneous food materials, i.e. the mixture of rice, fish, bread and curry with comparable activity to the commercial diastase enzymes available.

scholarly journals Application of Plackett-Burman Experimental Design for Lipase Production by Aspergillus niger Using Shea Butter Cake

2013 ◽  
Vol 2013 ◽  
pp. 1-5 ◽  
Author(s):  
Aliyu Salihu ◽  
Muntari Bala ◽  
Shuaibu M. Bala
Keyword(s):  
Aspergillus Niger ◽  
Statistical Approach ◽  
Tween 80 ◽  
Lipase Production ◽  
Rapid Identification ◽  
Shea Butter ◽  
Medium Components ◽  
Burman Design ◽  
Plackett Burman Design ◽  
Main Substrate

Plackett-Burman design was used to efficiently select important medium components affecting the lipase production by Aspergillus niger using shea butter cake as the main substrate. Out of the eleven medium components screened, six comprising of sucrose, (NH4)2SO4, Na2HPO4, MgSO4, Tween-80, and olive oil were found to contribute positively to the overall lipase production with a maximum production of 3.35 U/g. Influence of tween-80 on lipase production was investigated, and 1.0% (v/w) of tween-80 resulted in maximum lipase production of 6.10 U/g. Thus, the statistical approach employed in this study allows for rapid identification of important medium parameters affecting the lipase production, and further statistical optimization of medium and process parameters can be explored using response surface methodology.

scholarly journals Isolation and Characterization of Xenorhabdus nematophila Transposon Insertion Mutants Defective in Lipase Activity against Tween

2009 ◽  
Vol 191 (16) ◽  
pp. 5325-5331 ◽  
Author(s):  
Gregory R. Richards ◽  
Eugenio I. Vivas ◽  
Aaron W. Andersen ◽  
Delmarie Rivera-Santos ◽  
Sara Gilmore ◽  
...  
Keyword(s):  
Lipase Activity ◽  
Metabolic Pathways ◽  
Lipase Production ◽  
Xenorhabdus Nematophila ◽  
Transposon Insertion ◽  
Isolation And Characterization ◽  
Transposon Mutants ◽  
Conserved Gene ◽  
Insertion Mutants

ABSTRACT We identified Xenorhabdus nematophila transposon mutants with defects in lipase activity. One of the mutations, in yigL, a conserved gene of unknown function, resulted in attenuated virulence against Manduca sexta insects. We discuss possible connections between lipase production, YigL, and specific metabolic pathways.

Isolation and Characterization of a Xylan-Degrading Enzyme from Aspergillus niger van Tieghem LPM 93 with Potential for Industrial Applications

2011 ◽  
Vol 5 (2) ◽  
pp. 363-371 ◽  
Author(s):  
Natália von Gal Milanezi ◽  
Diana Paola Gómez Mendoza ◽  
Félix Gonçalves de Siqueira ◽  
Luciano Paulino Silva ◽  
Carlos André Ornelas Ricart ◽  
...  
Keyword(s):  
Aspergillus Niger ◽  
Industrial Applications ◽  
Degrading Enzyme ◽  
Isolation And Characterization

scholarly journals Effect of inoculum size, inducer and metal ion on lipase production by Rhodococcus strain UCC 0009

2020 ◽  
Vol 211 ◽  
pp. 02012
Author(s):  
Maegala Nallapan Maniyam ◽  
Anupriya Sundarajoo ◽  
Hazeeq Hazwan Azman ◽  
Nor Suhaila Yaacob ◽  
Hasdianty Abdullah
Keyword(s):  
Lipase Activity ◽  
Metal Ion ◽  
Optimization Method ◽  
Enzyme Characterization ◽  
Lipase Production ◽  
Industrial Applications ◽  
Culture Conditions ◽  
Inoculum Size ◽  
Local Resources ◽  
The One

Lipases are critical enzymes for industrial applications such as in the food and pharmaceutical fields. Therefore, the discovery of new lipases with enhanced characteristics are always encouraged. Thus, the present study explored the ability of a novel bacterial strain isolated from a tropical climate for lipase production. The optimization method using the one-variable-at-a-time approach was adopted to obtain increased production of lipase. The strain identified as Rhodococcus strain UCC 0009 was able to generate specific lipase activity of 11.67a ± 0.00 mU/mg at optimized conditions of 8 % (v/v) inoculum concentration, 1 % (v/v) olive oil as the inducer, and the addition of Ca2+ions. The specific lipase activity increased by 162 % when the optimization using a one-variable-ata-time approach was adopted compared to that of the non-optimized counterpart, signifying this experimental phase’s importance. The present study’s findings revealed the potential of utilizing Rhodococcus strain UCC 0009 as a green lipase producer for application in bioremediation and biotransformation at an industrial scale. Further study concentrating on enzyme characterization and improving culture conditions for conducive production of lipase via statistical optimization using response surface methodology (RSM) will be attempted to elucidate further the superiority of lipase obtained from local resources.

scholarly journals Production and characterization of Aspergillus niger GH29 family α-fucosidase and production of a novel non-reducing 1-fucosyllactose

2019 ◽  
Vol 37 (2) ◽  
pp. 221-229 ◽  
Author(s):  
Anne Usvalampi ◽  
Marcela Ruvalcaba Medrano ◽  
Hannu Maaheimo ◽  
Heidi Salminen ◽  
Olli Tossavainen ◽  
...  
Keyword(s):  
Aspergillus Niger ◽  
Glycosyl Hydrolase ◽  
Temperature Stability ◽  
Hydrolytic Activity ◽  
Industrial Applications ◽  
Optimal Temperature ◽  
Anomeric Carbon ◽  
Substrate Concentrations ◽  
Hydrolase Family

AbstractFucosylated oligosaccharides are interesting molecules due to their bioactive properties. In particular, their application as active ingredient in milk powders is attractive for dairy industries. The objective of this study was to characterize the glycosyl hydrolase family 29 α-fucosidase produced by Aspergillus niger and test its ability to transfucosylate lactose with a view towards potential industrial applications such as the valorization of the lactose side stream produced by dairy industry. In order to reduce costs and toxicity the use of free fucose instead of environmentally questionable fucose derivatives was studied. In contrast to earlier studies, a recombinantly produced A. niger α-fucosidase was utilized. Using pNP-fucose as substrate, the optimal pH for hydrolytic activity was determined to be 3.8. The optimal temperature for a 30-min reaction was 60 °C, and considering temperature stability, the optimal temperature for a 24-h reaction was defined as 45 °C For the same hydrolysis reaction, the kinetic values were calculated to be 0.385 mM for the KM and 2.8 mmol/(mg*h) for the Vmax. Transfucosylation of lactose occurred at high substrate concentrations when reaction time was elongated to several days. The structure of the product trisaccharide was defined as 1-fucosyllactose, where fucose is α-linked to the anomeric carbon of the β-glucose moiety of lactose. Furthermore, the enzyme was able to hydrolyze its own transfucosylation product and 2′-fucosyllactose but only poorly 3-fucosyllactose. As a conclusion, α-fucosidase from A. niger can transfucosylate lactose using free fucose as substrate producing a novel non-reducing 1-fucosyllactose.

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