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1.
Environ Technol ; : 1-17, 2024 May 31.
Artigo em Inglês | MEDLINE | ID: mdl-38820593

RESUMO

This paper aimed to apply filamentous fungi (Penicillium oxalicum and Cunninghamella echinulata), the microalga Tetradesmus obliquus and their co-culture in advanced treatment (tertiary treatment) of cheese whey. The bioremediation process was carried out in agitated flasks and bubble column bioreactors with different concentrations of chemical oxygen demand (COD) (223-1663 mg L-1), total nitrogen (TN) (13-61 mg L-1), and total phosphorus (TP) (3-26 mg L-1). The results obtained in shaken flasks showed a superiority of the consortium compared to the systems with separated species. In this sense, the treatment was carried out in a bubble column reactor, and the consortium formed by the microalga and the fungus C. echinulata showed a greater efficiency (at a light intensity of 100 µmol m-2 s-1), promoting by the symbiosis to reach removal efficiencies of up to 93.7, 78.8 and 93.4% for COD, TN and TP, respectively; meeting Brazilian and European standards for discharge into water bodies. In addition, no pH adjustment was required during the co-culture treatment, demonstrating the buffering effect of using these two types of microorganisms. Therefore, the use of the consortium formed by T. obliquus and C. echinulata as a remediator was highly promising to promote the advanced treatment of cheese whey.


Dairy wastewater needs a polishing treatment stage after secondary treatmentThe microalga-fungus consortium met legislation requirementsCOD, nitrogen and phosphorus were efficiently removed by the consortiumNo pH control was applied during the biological treatment by the consortium.

2.
J Food Biochem ; 45(4): e13654, 2021 04.
Artigo em Inglês | MEDLINE | ID: mdl-33595123

RESUMO

The Cunninghamella echinulata PA3S12MM fungus is a great producer of invertases in a growth medium supplemented by apple peels. The enzyme was purified 4.5 times after two chromatographic processes, and it presented a relative molecular mass of 89.2 kDa. The invertase reached maximum activity at pH of 6 and at 60°C, in addition to presenting stability in alkaline pH and thermal activation at 50°C. The enzymatic activity increased in the presence of Mn2+ and dithiothreitol (DTT), while Cu2+ and Z2+ ions inhibited it. Also, DTT showed to protect enzymatic activity. The apparent values for Km , Vmáx , and Kcat for the sucrose hydrolysis were, respectively, 173.8 mmol/L, 908.7 mmol/L min-1 , and 1,388.79 s-1 . The carbohydrate content was of 83.13%. The invertase presented hydrolytic activity over different types of glycosidic bonds, such as α1 â†” 2ß (sucrose), α1 â†’ 4 (polygalacturonic acid), α1 â†’ 4 and α1 â†’ 2 (pectin), and α1 â†” 1 (trehalose), indicating that the enzyme is multifunctional. Thus, the biochemical properties showed by the C. echinulata PA3S12MM suggest a broad industrial application, such as in the biomass hydrolysis or in the food industry. PRACTICAL APPLICATIONS: Invertases are hydrolytic enzymes employed in several industrial sectors. Given their great importance for the economy and several industrial sectors, there is a growing interest in microorganisms producing this enzyme. The analysis of the biochemical properties of invertase in C. echinulata PA3S12MM suggest applications in the food industry. Due to its increased hydrolytic activity, the hydrolysis process of the sucrose may employ invertase for the production of invert sugar. The stability at alkaline pH suggests an application in the development of enzymatic electrodes for the quantification of sucrose in food and beverage. The multifunctional activity may work in the biomass hydrolysis or saccharification of by-products for the extraction of fermentable sugars. The high level of invertase N-linked glycosylation of invertase grants this enzyme thermal stability at high temperatures, in addition to resistance against the action of proteases, which are desirable characteristics for the application of this enzyme in industrial processes.


Assuntos
Cunninghamella , beta-Frutofuranosidase , Concentração de Íons de Hidrogênio , Temperatura
3.
Anticancer Agents Med Chem ; 20(14): 1688-1694, 2020.
Artigo em Inglês | MEDLINE | ID: mdl-32329702

RESUMO

BACKGROUND: The strategic development of therapeutic agents, capable of being targeted at their active sites, has been a major goal in treatment of cancer. The delivery of drugs for tumors has as its main challenge the development of safe and effective drugs, since the goal of chemotherapy is to eliminate the tumor completely without affecting healthy cells. The aim of present study was to investigate the antioxidant, anticancer activities of zidovudine and its α-O-glycosylated derivative obtained by biosynthesis of a filamentous fungi, Cunninghamela echinulata. METHODS: An evaluation of the cytotoxic potential of zidovudine and its α-O-glycosylated was performed in fibroblasts and melanoma cells by the tetrazolium reduction method (MTT) and the antioxidant activity of this derivative was observed. RESULTS: The antioxidant activity of zidovudine demonstrated an electrochemical oxidation potential of 0.91V, while the α-O-glycosylated derivative did not exhibit any antioxidant activity. The zidovudine exhibited low cytotoxicity for melanoma and fibroblast cells, while the α-O-glycosylated derivative presented better cytotoxicity on melanoma cells at a concentration of 10mg. mL-1. CONCLUSION: This study demonstrates the specific cytotoxicity of the glycoconjugate and suggests that glycosylation by biosynthesis can be a useful strategy for obtaining new anticancer compounds.


Assuntos
Antineoplásicos/farmacologia , Cunninghamella/metabolismo , Zidovudina/farmacologia , Animais , Antineoplásicos/química , Antineoplásicos/metabolismo , Proliferação de Células/efeitos dos fármacos , Sobrevivência Celular/efeitos dos fármacos , Relação Dose-Resposta a Droga , Ensaios de Seleção de Medicamentos Antitumorais , Glicosilação , Camundongos , Estrutura Molecular , Oxirredução , Relação Estrutura-Atividade , Células Tumorais Cultivadas , Zidovudina/química , Zidovudina/metabolismo
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