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Foods 2016, 5(4), 72; doi:10.3390/foods5040072

Production and Properties of a Thermostable, pH—Stable Exo-Polygalacturonase Using Aureobasidium pullulans Isolated from Saharan Soil of Algeria Grown on Tomato Pomace

1
Laboratoire de Génie Microbiologiques et Applications, Faculté des Sciences de la Nature et de la Vie, Département de Biochimie et Biologie Cellulaire & Moléculaire, Université Frères Mentouri Constantine, Route Ain El Bey 25017, Algeria
2
Walloon Center of Industrial Biology, University of Liège, Boulevard du Rectorat 29, B40 Building, 4000 Liège, Belgium
3
Department of Agricultural, Food and Environmental Science, Industrial Yeasts Collection DBVPG, University of Perugia, Borgo XX Giugno 74, I-06121 Perugia, Italy
*
Author to whom correspondence should be addressed.
Academic Editor: Costas Stathopoulos
Received: 8 September 2016 / Revised: 25 October 2016 / Accepted: 25 October 2016 / Published: 29 October 2016
(This article belongs to the Special Issue Utilisation of Plant Food Waste)
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Abstract

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. View Full-Text
Keywords: exo-polygalacturonase; Aureobasidium pullulans; tomato pomace; response surface methodology; characterization exo-polygalacturonase; Aureobasidium pullulans; tomato pomace; response surface methodology; characterization
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Bennamoun, L.; Hiligsmann, S.; Dakhmouche, S.; Ait-Kaki, A.; Labbani, F.-Z.K.; Nouadri, T.; Meraihi, Z.; Turchetti, B.; Buzzini, P.; Thonart, P. Production and Properties of a Thermostable, pH—Stable Exo-Polygalacturonase Using Aureobasidium pullulans Isolated from Saharan Soil of Algeria Grown on Tomato Pomace. Foods 2016, 5, 72.

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