دورية أكاديمية

Hydrolytic enzymes production by Aspergillus section Nigri in presence of butylated hydroxyanisole and propyl paraben on peanut meal extract agar ; Producción de enzimas hidrolíticas por Aspergillus sección Nigri en presencia de hidroxianisol butilado y propilparabeno en medio de cultivo de agar con extracto de cacahuete

التفاصيل البيبلوغرافية
العنوان: Hydrolytic enzymes production by Aspergillus section Nigri in presence of butylated hydroxyanisole and propyl paraben on peanut meal extract agar ; Producción de enzimas hidrolíticas por Aspergillus sección Nigri en presencia de hidroxianisol butilado y propilparabeno en medio de cultivo de agar con extracto de cacahuete
المؤلفون: Barberis, Carla Lorena, Landa, Maria Florencia, Barberis, Mauricio Gastón, Giaj Merlera, Guillermo, Dalcero, Ana Maria, Magnoli, Carina Elizabeth
بيانات النشر: Asociacion Espanola Micología
المجموعة: CONICET Digital (Consejo Nacional de Investigaciones Científicas y Técnicas)
مصطلحات موضوعية: Butylated Hydroxyanisole, Propyl Paraben, Aspergillus Carbonarius, Aspergillus Niger, Hydrolytic Enzymes, Water Activities, https://purl.org/becyt/ford/1.6Test, https://purl.org/becyt/ford/1Test
الوصف: 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. ; Antecedentes En los últimos años, para controlar el crecimiento fúngico, en lugar de los fungicidas tradicionales, tanto en la industria alimentaria como en los productos agrícolas se utilizan antioxidantes como aditivos alimentarios bien tolerados y sin riesgos de efectos adversos. Objetivos En el presente estudio, en un medio de cultivo con ...
نوع الوثيقة: article in journal/newspaper
وصف الملف: application/pdf
اللغة: English
تدمد: 1130-1406
العلاقة: info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S1130140613000272Test; http://hdl.handle.net/11336/33790Test; Barberis, Carla Lorena; Landa, Maria Florencia; Barberis, Mauricio Gastón; Giaj Merlera, Guillermo; Dalcero, Ana Maria; et al.; Hydrolytic enzymes production by Aspergillus section Nigri in presence of butylated hydroxyanisole and propyl paraben on peanut meal extract agar; Asociacion Espanola Micología; Revista Iberoamericana de Micología; 31; 2; 3-2014; 131-136; CONICET Digital; CONICET
الإتاحة: https://doi.org/10.1016/j.riam.2013.02.005Test
http://hdl.handle.net/11336/33790Test
حقوق: info:eu-repo/semantics/openAccess ; https://creativecommons.org/licenses/by-nc-sa/2.5/arTest/
رقم الانضمام: edsbas.4A748ADE
قاعدة البيانات: BASE