Production and Properties of a Thermostable, pH-Stable Exo-Polygalacturonase Using Aureobasidium pullulans Isolated from Saharan Soil of Algeria Grown on Tomato Pomace
| Autor: | Zahia Meraihi, Benedetta Turchetti, Fatima-Zohra Kenza Fk Labbani, Tahar Nouadri, P. Buzzini, Leila Bennamoun, Amel A Ait-Kaki, Philippe Thonart, Serge Hiligsmann, Scheherazad Dakhmouche |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2016 |
| Předmět: |
0106 biological sciences
0301 basic medicine Health (social science) Plant Science Polygalacturonase activity lcsh:Chemical technology 01 natural sciences Health Professions (miscellaneous) Microbiology Aureobasidium pullulans Article response surface methodology tomato pomace 03 medical and health sciences chemistry.chemical_compound Hydrolysis 010608 biotechnology Botany Bioreactor characterization exo-polygalacturonase lcsh:TP1-1185 Food science Pectinase Lactose biology Chemistry Substrate (chemistry) Sciences bio-médicales et agricoles biology.organism_classification 030104 developmental biology Tomato pomace Food Science |
| Zdroj: | Foods (Basel, Switzerland), 5 (4 Foods, Vol 5, Iss 4, p 72 (2016) Foods; Volume 5; Issue 4; Pages: 72 Foods |
| Popis: | Polygalacturonase is a valuable biocatalyst for several industrial applications. Production of polygalacturonase using the Aureobasidium pullulans stain isolated from Saharan soil of Algeria was investigated. Its capacity to produce polygalacturonase was assessed under submerged culture using tomato pomace as an abundant agro-industrial substrate. Optimization of the medium components, which enhance polygalacturonase activity of the strain Aureobasidium pullulans, was achieved with the aid of response surface methodology. The composition of the optimized medium was as follows: tomato pomace 40 g/L, lactose 1.84 g/L, CaCl₂0.09 g/L and pH 5.16. Practical validation of the optimum medium provided polygalacturonase activity of 22.05 U/mL, which was 5-fold higher than in unoptimized conditions. Batch cultivation in a 20 L bioreactor performed with the optimal nutrients and conditions resulted in a high polygalacturonase content (25.75 U/mL). The enzyme showed stability over a range of temperature (5-90 °C) with an optimum temperature of 60 °C with pH 5.0, exhibiting 100% residual activity after 1h at 60 °C. This enzyme was stable at a broad pH range (5.0-10). The enzyme proved to be an exo-polygalacturonase, releasing galacturonic acid by hydrolysis of polygalacturonic acid. Moreover, the exo-polygalacturonase was able to enhance the clarification of both apple and citrus juice. As a result, an economical polygalacturonase production process was defined and proposed using an industrial food by-product. info:eu-repo/semantics/published |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|