scholarly journals Partial characterization of esterases from Fusarium culmorum grown in media supplemented with di (2-ethyl hexyl phthalate) in solid-state and submerged fermentation

2018 ◽  
Vol 3 (1) ◽  
pp. 82-94 ◽  
Author(s):  
Lorena Ferrer-Parra ◽  
Dolores Itzel López-Nicolás ◽  
Rocío Martínez-Castillo ◽  
Juan Pedro Montiel-Cina ◽  
Ana Rosa Morales-Hernández ◽  
...  
Keyword(s):  
Solid State ◽  
Solid State Fermentation ◽  
Esterase Activity ◽  
Submerged Fermentation ◽  
Polyacrylamide Gel Electrophoresis ◽  
Fusarium Culmorum ◽  
Phytopathogenic Fungus ◽  
Biochemical Tests ◽  
Enzymatic Production ◽  
High Concentrations

Di (2-ethylhexyl) phthalate (DEHP) is a plasticizer used in the polyvinyl chloride (PVC) industry. The indiscriminate use of various products manufactured with PVC, causes this plasticizer to be considered a contaminant. Fusarium culmorum is a phytopathogenic fungus that has the ability to produce esterase enzymes. Esterases are of great importance because they can break the ester bonds present in the plasticizers. In this work, the activity of esterases produced by F. culmorum grown in media supplemented with different concentrations of DEHP (1500 and 2000 mg/L) in solid-state fermentation and submerged fermentation was characterized by biochemical tests and polyacrylamide gel electrophoresis. F. culmorum showed higher esterase activity in media supplemented with 1500 and 2000 mg DEHP/L in solid-state fermentation. A greater number of esterase activity bands were observed in the DEHP-supplemented media, having a molecular weight of about 20, 25, 37, 45, 55, 75 and 150 kDa, in both fermentation systems. 1500 mg of DEHP/L induced a higher production of esterases, demonstrating that high concentrations of DEHP did not inhibit the enzymatic production of the fungus.

scholarly journals Growth and esterase activity of Fusarium culmorum grown in di(2- ethyl hexyl) phthalate in liquid fermentation

2019 ◽  
Vol 4 (1) ◽  
pp. 51-60 ◽  
Author(s):  
Naomi Surellem Ríos-González ◽  
Ángel González-Márquez ◽  
Carmen Sánchez
Keyword(s):  
Esterase Activity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Fusarium Culmorum ◽  
Terrestrial Ecosystems ◽  
Phytopathogenic Fungus ◽  
Biochemical Tests ◽  
Liquid Fermentation ◽  
Endocrine Disrupting Compound ◽  
Ethyl Hexyl ◽  
High Concentrations

Di (2-ethyl hexyl) phthalate (DEHP) is a plasticizer present in various products, mainly those made with PVC. This phthalate has attracted attention due to its important participation in the contamination of the environment. It has been reported as an endocrine-disrupting compound in mammals. Fusarium culmorum is a phytopathogenic fungus able to degrade DEHP, because it produces esterases, which are enzymes capable to break down ester bonds present in the structure of phthalates. In this research, growth, protein content and esterases activity by biochemical tests and polyacrylamide gel electrophoresis were characterized for F. culmorum grown in DEHP-supplemented (100 and 1500 mg/L) media as the only carbon source in liquid fermentation. F. culmorum showed higher biomass production and esterase activity in medium supplemented with 1500 mg of DEHP/L. Zymography revealed that bands with esterase activity were observed after 24 h and 48 h in media supplemented with 1500 and 100 mg of DEHP/L, respectively. It was shown that DEHP is an inducer of esterases and that this compound was used as carbon and energy sources by F. culmorum. This fungus can secrete specific esterase to breakdown high concentrations of DEHP, being a promising organism for bioremediation of DEHP-polluted environments in both aquatic and terrestrial ecosystems.

scholarly journals Production of cutinolytic esterase by Fusarium culmorum grown at different apple cutin concentrations in submerged fermentation

2019 ◽  
Vol 4 (4) ◽  
pp. 50-64
Author(s):  
Angel González-Márquez ◽  
Octavio Loera-Corral ◽  
Gustavo Viniegra-González ◽  
Carmen Sánchez
Keyword(s):  
Protein Content ◽  
Submerged Fermentation ◽  
Food Industry ◽  
Specific Growth ◽  
Polyacrylamide Gel Electrophoresis ◽  
Fusarium Culmorum ◽  
Toxic Substances ◽  
Biochemical Tests ◽  
The Media ◽  
Activity Band

Cutinolytic esterase (i.e., cutinase) is an enzyme that catalyzes the cleavage of ester bonds in cutin and also in diverse soluble and insoluble esters. It has application in several biotechnological areas, acting as biocatalysts in the food industry, in detergents, in biodegradation of polymers and other toxic substances, being important in biorremediation. In this research, specific growth rate, protein content, cutinolytic activity by biochemical tests and polyacrylamide gel electrophoresis, and growth and enzymatic kinetic parameters were determined for F. culmorum grown at different apple cutin concentrations (0.2, 2 and 20 g/L) in submerged fermentation. It was observed that biomass, protein content and enzymatic activity enhanced as cutin concentration increased in the media. A cutinase activity band of around 65 KDa was observed in zymograms of different cutin concentration. An additional cutinase activity band of around 90 KDa was also observed in zymograms of F. culmorum grown in 20 g of apple cutin/L. These studies showed that F. culmorum used apple cutin as the sole carbon source, which acted as a cutinase inducer. The highest-yielding parameters of cutinase were observed in 2 g of apple cutin/L. This research showed promising results in the cutinase induction for F. culmorum using a low concentration of apple cutin.

scholarly journals Characterization of -amylase produced by the endophytic strain of Penicillium digitatum in solid state fermentation (SSF) and submerged fermentation (SMF)

2016 ◽  
Vol 15 (28) ◽  
pp. 1511-1519 ◽  
Author(s):  
Becker Onofre Sideney ◽  
Abatti Dirceu ◽  
Refosco Douglas ◽  
Antonio Tessaro Amarildo ◽  
Alisson Becker Onofre Jean ◽  
...  
Keyword(s):  
Solid State ◽  
Solid State Fermentation ◽  
Submerged Fermentation ◽  
Penicillium Digitatum

Biocatalytic benefits of immobilized Fusarium sp. (GFC) lipase from solid state fermentation on free lipase from submerged fermentation

2020 ◽  
Vol 147 ◽  
pp. 112235 ◽  
Author(s):  
Bruno Henrique de Oliveira ◽  
Gilberto Victor Coradi ◽  
Pedro de Oliva-Neto ◽  
Valeria Marta Gomes do Nascimento
Keyword(s):  
Solid State ◽  
Solid State Fermentation ◽  
Submerged Fermentation ◽  
Fusarium Sp ◽  
Free Lipase

scholarly journals Effect of surfactant Tween 80 on growth and esterase production of Fusarium culmorum in liquid fermentation

2020 ◽  
Vol 5 (4) ◽  
pp. 64-79
Author(s):  
Henry Medina-Flores ◽  
◽  
Angel González-Márquez ◽  
Carmen Sánchez ◽  
◽  
...  
Keyword(s):  
Esterase Activity ◽  
Enzyme Production ◽  
Culture Media ◽  
Fusarium Culmorum ◽  
Tween 80 ◽  
Ionic Surfactant ◽  
Specific Rate ◽  
Biochemical Tests ◽  
Liquid Fermentation ◽  
Esterase Production

Tween 80 is a widely used non-ionic surfactant that is added to culture media to make hydrophobic substrate available to microorganisms. Because of this surfactant widespread use, it is important to understand how it affects microbial growth and enzyme production. In this work, the effect of different concentrations (100, 400 and 600 l/L; v/v) of Tween 80 (as the sole carbon source) on the biomass production, esterase activities (assessed through biochemical tests and zymographic assays) and protein content of Fusarium culmorum grown in liquid fermentation was determined. The specific growth rate (μ), biomass yield (YX/S), esterase yield (YE/X), esterase productivity (P), maximal enzymatic activity (Emax), and specific rate of enzyme production (qp) were also estimated. A control medium added with glucose was used. The highest μ was showed in the medium added with 100 l of Tween 80/L. However, the greatest esterase activity was observed in those media containing the highest concentrations of Tween 80 ( energy source and it also induced the esterase production by F. culmorum. Tween 80 concentration is positively correlated with the number of esterase isoforms produced by this fungus. The higher the Tween 80 concentration (400 μl/L and 600 μl/L, v/v), the more number of esterase isoforms will be induced. However, lower concentration (100 μl/L) of Tween 80/L did not show a significant effect on the induction of the esterase activity.400 l/L and 600 l/L; v/v). These results show that Tween 80 was used as the sole carbon and

scholarly journals Production of Extracellular Protease from Bacterial Co-cultures using Solid State Fermentation

2020 ◽  
Vol 2 (4) ◽  
pp. 13-23
Author(s):  
Nabiha Naeem Sheikhs ◽  
Qurat-ul-ain ◽  
Saba Altaf
Keyword(s):  
Solid State ◽  
Solid State Fermentation ◽  
Bacterial Strain ◽  
Hydrolytic Enzymes ◽  
Skim Milk ◽  
Cost Effective ◽  
Protease Production ◽  
Bacterial Strains ◽  
Biochemical Tests ◽  
Waste Products

Proteases (also known as peptidases or proteinases) are hydrolytic enzymes that cleave proteins into amino acids. They comprise 60% of the total industrial usage of enzymes worldwide and can be obtained from many sources. The current study aims to isolate and screen protease-producing bacterial strains from the soil and to produce protease from the bacterial co-cultures using solid-state fermentation (SSF). Primary screening of the protease-producing bacterial strains was carried out on skim milk agar and they were sub-cultured and preserved on the nutrient agar for further testing. Thirty-two compatibility tests of twenty-seven bacterial isolates were performed and SSF was carried out. Afterward, absorbance was taken at 660 nm against tyrosine as standard. According to the results, the bacterial co-culture 19 showed the highest absorbance with an enzyme activity of 10.2 U/ml. The bacterial strains of the co-culture 19 were identified through morphological and biochemical tests. Bacterial strain 1 was observed as cocci and irregular, while bacterial strain 2 was bacillus and rod-shaped. Both strains were positive for gram staining, catalase test, casein hydrolysis test and methyl red test. As for endospore staining, bacterial strain 1 was spore forming while bacterial strain 2 was a non-spore former. It was concluded that the bacterial co-culture 19 can act as a potent co-culture for protease production. Compatibility test was carried out to enhance the production of protease by utilizing cheap and readily available agro-waste products, which benefit the industry by being cost effective and the environment by being eco-friendly.

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