کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10130473 | 1645337 | 2018 | 41 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Peptidase from Aspergillus niger NRRL 3: Optimization of its production by solid-state fermentation, purification and characterization
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
علوم کشاورزی و بیولوژیک
دانش تغذیه
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Orange peels, soybean hulls, Ilex paraguariensis and Platanus x hispanica were evaluated as solid substrates in order to produce peptidases from Aspergillus niger NRRL3 (PAN) under solid-state fermentation. The mixture of soybean hulls and orange peels enabled fungal development and showed the highest peptidase production. The optimal conditions for PAN production were found to be as follows: soybean hulls/orange peels mass ratio, 0.25; initial pH, 7.05; K2HPO4 43.5â¯g/L and 4.03â¯g/L NaNO3; inoculation with 5000 conidia per 3â¯g of solid substrate; incubation conditions, 30â¯Â°C for 5 days. Under these conditions, the peptidase activity was 1000â¯Â±â¯100 AU/mL. PAN concentration was performed by adsorption on a DEAE-cellulose matrix. The subsequent purification was carried out by gel filtration on Sephadex G-100, with a global purification factor of about 9. PAN proved to belong to the serine-type of peptidases, its highest peptidase activity being at 65â¯Â°C. However, proteolysis at 60â¯Â°C proved more suitable due to the differences in the inactivation rate. Besides, PAN showed high stability over a pH range of 4-11. Taking all this into account, we herein describe the production and purification of a serine peptidase from Aspergillus niger NRRL3 for the first time.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: LWT - Volume 98, December 2018, Pages 485-491
Journal: LWT - Volume 98, December 2018, Pages 485-491
نویسندگان
Débora N. López, Micaela Galante, Germán Ruggieri, Julia Piaruchi, MarÃa E. Dib, Natalia Montellano Duran, Julia Lombardi, Mariana de Sanctis, Valeria Boeris, Patricia H. Risso, DarÃo Spelzini,