Mycelium-bound lipase from a locally isolated strain of Aspergillus westerdijkiae

Castro, Fausto Fernandes de; Pinheiro, Ana Beatriz Ponchio; Nassur, Carolina Beatriz; Barbosa-Tessmann, Ione Parra

doi:10.1016/j.bcab.2017.04.009

Cited by 17 publications

(16 citation statements)

References 26 publications

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“…Most of the fungi cell wall proteins are glycosylated and are secreted by the classical pathway . Accordingly, Castro et al have found an esterase with a high activity against p ‐NPB in the A. westerdijkiae lyophilized mycelia, which could be ascribed to the esterase purified in this work in its secretion pathway.…”

Section: Discussionmentioning

confidence: 56%

“…The esterase production by A. westerdijkiae is regulated by oil presence. Similarly, oil was found to modulate lipase secretion by P. restrictum and Candida rugosa and the production of a mycelium‐bound lipase by A. westerdijkiae . Accordingly, the co‐production of extracellular esterase and cell‐bound lipase by C. rugosa was dependent on oil presence in the culture medium.…”

Section: Discussionmentioning

confidence: 93%

“…In fact, the lyophilized mycelium of A. westerdijkiae presented activity against Tween 80. The activity against long fatty acids esters in A. westerdijkiae mycelia is due to the presence of a true lipase .…”

Section: Discussionmentioning

confidence: 99%

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Production, purification, and characterization of a novel serine‐esterase from Aspergillus westerdijkiae

et al. 2017

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Esterases hydrolyze water soluble short chain fatty acids esters and are biotechnologically important. A strain of Aspergillus westerdijkiae isolated from cooking oil for recycling was found to secrete an esterase. The best enzyme production (19-24 U/ml of filtrate) culture conditions were stablished. The protein was purified using ammonium sulphate precipitation, dialysis, and a chromatographic step in Sephacryl S-200 HR. The 32 kDa purified protein presented an optimal temperature of 40°C, with a T of 48.95°C, and an optimal pH of 8.0. K and V were 638.11 µM for p-NPB and 5.47 µmol of released p-NP · min · µg of protein, respectively. The purified enzyme was partially active in the presence of 25% acetone. PMSF inhibited the enzyme, indicating that it is a serine hydrolase. MS enzyme peptides sequences were used to find the protein in the A. westerdijkiae sequenced genome. A structure model demonstrated that the protein is a member of the a/ß -hydrolase fold superfamily.

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Section: Discussionmentioning

confidence: 56%

Section: Discussionmentioning

confidence: 93%

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Production, purification, and characterization of a novel serine‐esterase from Aspergillus westerdijkiae

et al. 2017

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“…Imediatamente após este tempo, o sistema reacional foi centrifugado (14.000 g, 2 min) e coletou-se o sobrenadante. 25 O pNP liberado foi detectado a 410 nm e quantificado a partir de uma curva padrão (R 2 = 0,9988) feita com concentrações conhecidas deste composto. Os brancos foram obtidos pela leitura do sistema reacional sem micélio.…”

Section: Ensaio Enzimáticounclassified

Avaliação Da Biomassa De Fungos Amazônicos Como Fonte De Lipases Para Biocatálise

Romano¹,

Santos²,

Louzada³

et al. 2020

Quím. Nova

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EVALUATION OF AMAZONIAN FUNGI BIOMASS AS A SOURCE OF LIPASES FOR BIOCATALYSIS. We evaluated the biomass of twenty Amazonian fungal isolates as a potential source of mycelium-bound lipases with hydrolytic, synthetic or enantioselective activity for biocatalysis application. We compared the hydrolytic activity of three biomass treatments (delipidated, non-delipidated and cultivated in medium without inducer). Delipidated biomass showed better results in the hydrolysis of p-nitrophenyl palmitate compared to the other two treatments for fifteen isolates. Delipidated biomass of six Aspergillus strains and UEA_115 strain showed a high synthesis activity of ethyl palmitate by transesterification in organic medium. Results were confirmed by spectrophotometry (410 nm) and gas chromatography. In this reaction, the isolate DPUA_1539 A. flavo-furcatis reached a maximum value of 668.5 ± 23.5 mU g-1. Enantioselective activity assays indicated that biomass-bound lipases from UEA_115 isolate (E = 3.58; ee s = 7 ± 0) and in particular from the DPUA_1539 A. flavo-furcatis isolate (E = 24.15; ee s = 91 ± 1) have the ability to discriminate enantiomers of the drug ibuprofen by ester synthesis, preferably with (R)-enantiomer. These results encourage further investigations of these fungi as potential lipase suppliers for biocatalytic processes such as biodiesel production and enantiopure drugs.

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“…Bharti et al(2013) pesquisaram a lipases produzida pelo microrganismo Aspergillus japonicas e identificaram que ela possui uma alta temperatura ótima (40 °C) e ainda apresenta uma alta estabilidade em solventes hidrofóbicos, o que a torna uma alternativa interessante para reações de transesterificação de ésteres em meios orgânicos, como é o caso da produção de biodiesel a partir de óleos vegetais. Castro et al (2017) estudaram uma nova lipase ligada ao micélio de uma cepa isolada local de Aspergillus westerdijkiae e conforme os autores, as propriedades das lipases naturalmente imobilizadas estudadas tornam essas lipases uma alternativa barata e, portanto, vantajosa para a produção de biodiesel. Mahmoud et al(2015) isolaram a partir de um solo contaminado com querosene um fungo filamentoso identificado como Aspergillus terreus e obtiveram uma alta produção de lipases extracelulares via FS.…”

Section: Análise Qualitativaunclassified

Avanços em caracterização bioquímica de lipases microbianas: uma revisão

Zavarise

Pinotti

2020

RSD

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Mycelium-bound lipase from a locally isolated strain of Aspergillus westerdijkiae

Cited by 17 publications

References 26 publications

Production, purification, and characterization of a novel serine‐esterase from Aspergillus westerdijkiae

Production, purification, and characterization of a novel serine‐esterase from Aspergillus westerdijkiae

Avaliação Da Biomassa De Fungos Amazônicos Como Fonte De Lipases Para Biocatálise

Avanços em caracterização bioquímica de lipases microbianas: uma revisão

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