Browsing by Author "Del Monaco, G."
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- A novel β-xylosidase from Anoxybacillus sp. 3M towards an improved agro-industrial residues saccharificationPublication . Marcolongo, L.; La Cara, F.; Del Monaco, G.; Paixão, Susana M.; Alves, Luís; Ionata, E.; Marques, Isabel PaulaABSTRACT: An intracellular β-xylosidase (AbXyl), fromthe thermoalkaline Anoxybacillus sp. 3M,was purified and characterized. The homodimeric enzyme (140 kDa) was optimally active at 65 °C and pH 5.5, exhibited half life of 10 h at 60 °C, 78 and 88% residual activity after 24 h, at pH 4.5 and 8.0, respectively. Fe2+, Cu2+, Al3+, Ag+ and Hg2+inhibited the enzyme; the activity was moderately stimulated by SDS and not influenced by β-mercaptoethanol. In the presence of p-nitrophenyl-β-D-xylopyranoside, AbXyl exhibited Km of 0.19 mM, Kcat of 453.29 s−1, KcatKm−1 of 2322 s−1mMandwas moderately influenced by xylose (Ki 21.25mM). The enzyme hydrolyzed xylo-oligomers into xylose and catalyzed transxylosilation reactions also in presence of alcohols as acceptors, producing xylo-oligosaccharides and alkyl-xylosides. Finally AbXyl was applied towards a statistically optimized process of brewery's spent grain bioconversion, highlighting the important role of this biocatalyst in reaching high yields of fermentable sugars.
- Properties of an alkali-thermo stable xylanase from Geobacillus thermodenitrificans A333 and applicability in xylooligosaccharides generationPublication . Marcolongo, L.; La Cara, F.; Morana, A.; Di Salle, A.; Del Monaco, G.; Paixão, Susana M.; Alves, Luís; Ionata, E.An extracellular thermo-alkali-stable and cellulase-free xylanase from Geobacillus thermodenitrificans A333 was purified to homogeneity by ion exchange and size exclusion chromatography. Its molecular mass was 44 kDa as estimated in native and denaturing conditions by gel filtration and SDS-PAGE analysis, respectively. The xylanase (GtXyn) exhibited maximum activity at 70 °C and pH 7.5. It was stable over broad ranges of temperature and pH retaining 88 % of activity at 60 °C and up to 97 % in the pH range 7.5–10.0 after 24 h. Moreover, the enzyme was active up to 3.0 M sodium chloride concentration, exhibiting at that value 70 % residual activity after 1 h. The presence of other metal ions did not affect the activity with the sole exceptions of K+ that showed a stimulating effect, and Fe2+, Co2+ and Hg2+, which inhibited the enzyme. The xylanase was activated by non-ionic surfactants and was stable in organic solvents remaining fully active over 24 h of incubation in 40 % ethanol at 25 °C. Furthermore, the enzyme was resistant to most of the neutral and alkaline proteases tested. The enzyme was active only on xylan, showing no marked preference towards xylans from different origins. The hydrolysis of beechwood xylan and agriculture-based biomass materials yielded xylooligosaccharides with a polymerization degree ranging from 2 to 6 units and xylobiose and xylotriose as main products. These properties indicate G. thermodenitrificans A333 xylanase as a promising candidate for several biotechnological applications, such as xylooligosaccharides preparation.
- Valorization of chestnut manufacture process residues [Poster]Publication . Morana, A.; Laratta, B.; Vella, F. M.; Santos, Carla A.; Del Monaco, G.; La Cara, F.; Marques, Isabel Paula
- Vegetable wastes to phenolic compounds by anaerobic digestion [Poster]Publication . La Cara, F.; Ionata, E.; Del Monaco, G.; Marques, Isabel PaulaThe present work intends to assess whether anaerobic digestion could be additionally used as a valorisation method of fresh-cut fruit and vegetables by-products, producing different valuable molecules for industrial applications.