Hydrolytic enzymes production by Aspergillus section Nigri in presence of butylated hydroxyanisole and propyl paraben on peanut meal extract agar
Background In the last years, food grade antioxidants are used safely as an alternative to traditional fungicides to control fungal growth in several food and agricultural products. Aims In this work, the effect of butylated hydroxyanisole (BHA) and propyl paraben (PP) on two hydrolytic enzyme activ...
| Autores: | , , , , , |
|---|---|
| Tipo de recurso: | artículo |
| Estado: | Versión publicada |
| Fecha de publicación: | 2014 |
| País: | Argentina |
| Institución: | Consejo Nacional de Investigaciones Científicas y Técnicas |
| Repositorio: | CONICET Digital (CONICET) |
| Idioma: | inglés |
| OAI Identifier: | oai:ri.conicet.gov.ar:11336/33790 |
| Acceso en línea: | http://hdl.handle.net/11336/33790 |
| Access Level: | acceso abierto |
| Palabra clave: | Butylated Hydroxyanisole Propyl Paraben Aspergillus Carbonarius Aspergillus Niger Hydrolytic Enzymes Water Activities https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
| Sumario: | Background In the last years, food grade antioxidants are used safely as an alternative to traditional fungicides to control fungal growth in several food and agricultural products. Aims In this work, the effect of butylated hydroxyanisole (BHA) and propyl paraben (PP) on two hydrolytic enzyme activity (β-d-glucosidase and α-d-galactosidase) by Aspergillus section Nigri species under different water activity conditions (aW; 0.98, 0.95 and 0.93) and incubation time intervals (24, 48, 72 and 96 h) was evaluated on peanut-based medium. Methods The activity of two glycosidases, β-d-glucosidase and α-d-galactosidase, was assayed using as substrates 4-nitrophenyl-β-d-glucopyranosido and 4-nitrophenyl-α-d-galactopyranosido, respectively. The enzyme activity was determined by the increase in optical density at 405 nm caused by the liberation of p-nitrophenol by enzymatic hydrolysis of the substrate. Enzyme activity was expressed as micromoles of p-nitrophenol released per minute. Results The major inhibition in β-d-glucosidase activity of A. carbonarius and A. niger was found with 20 mmol l−1 of BHA or PP at 0.98 and 0.95 aW, respectively, whereas for α-d-galactosidase activity a significant decrease in enzyme activity with respect to control was observed in A. carbonarius among 5 to 20 mmol l−1 of BHA or PP in all conditions assayed. Regarding A. niger, the highest percentages of enzyme inhibition activity were found with 20 mmol l−1 of BHA or PP at 0.95 aW and 96 h. Conclusions The results of this work provide information about the capacity of BHA and PP to inhibit in vitro conditions two of the most important hydrolytic enzymes produced by A. carbonarius and A. niger species. |
|---|