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Fungal multienzyme production on industrial by-products of the citrus-processing industry
National Technical University of Athens.
National Technical University of Athens.
2008 (English)In: Bioresource Technology, ISSN 0960-8524, E-ISSN 1873-2976, Vol. 99, no 7, p. 2373-2383Article in journal (Refereed) Published
Abstract [en]

Orange peels is the principal solid by-product of the citrus processing industry and the disposal of the fresh peels is becoming a major problem to many factories. Dry citrus peels are rich in pectin, cellulose and hemicellulose and may be used as a fermentation substrate. Production of multienzyme preparations containing pectinolytic, cellulolytic and xylanolytic enzymes by the mesophilic fungi Aspergillus niger BTL, Fusarium oxysporum F3, Neurospora crassa DSM 1129 and Penicillium decumbens under solid-state fermentation (SSF) on dry orange peels was enhanced by optimization of initial pH of the culture medium and initial moisture level. Under optimal conditions A. niger BTL was by far the most potent strain in polygalacturonase and pectate lyase, production followed by F. oxysporum F3, N. crassa DSM 1129 and P. decumbens. N. crassa DSM 1129 produced the highest endoglucanase activity and P. decumbens the lowest one. Comparison of xylanase production revealed that A. niger BTL produced the highest activity followed by N. crassa DSM 1129, P. decumbens and F. oxysporum F3. N. crassa DSM 1129 and P. decumbens did not produce any β-xylosidase activity, while A. niger BTL produced approximately 10 times more β-xylosidase than F. oxysporum F3. The highest invertase activity was produced by A. niger BTL while the lowest ones by F. oxysporum F3 and P. decumbens. After SSF of the four fungi, under optimal conditions, the fermented substrate was either directly exposed to autohydrolysis or new material was added, and the in situ produced multienzyme systems were successfully used for the partial degradation of orange peels polysaccharides and the liberation of fermentable sugars.

Place, publisher, year, edition, pages
2008. Vol. 99, no 7, p. 2373-2383
Identifiers
URN: urn:nbn:se:ltu:diva-10193DOI: 10.1016/j.biortech.2007.05.018Local ID: 8f3dc649-32a3-4c78-acf7-75c75d6adceaOAI: oai:DiVA.org:ltu-10193DiVA, id: diva2:983133
Note
Upprättat; 2008; 20130220 (ysko)Available from: 2016-09-29 Created: 2016-09-29 Last updated: 2017-11-24Bibliographically approved

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