Food Engineering / Gıda Mühendisliği
Permanent URI for this collectionhttps://hdl.handle.net/11147/12
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Article Citation - WoS: 1Citation - Scopus: 2Partial Purification of a Polygalacturonase From a New Aspergillus Sojae Mutant and Its Application in Grape Mash Maceration(John Wiley and Sons Inc., 2017) Yıldız, Semanur; Mata-Gomez, Marco A.; Tarı, Canan; Rito-Palomares, Marco; 03.08. Department of Food Engineering; 03. Faculty of Engineering; 01. Izmir Institute of TechnologyThe use of polygalacturonase (PG) preparations in winemaking promotes the release of phenolic compounds. A PG from a new source, Aspergillus sojae mutant, was semi-purified and tested for grape mash maceration. Crude extract (CE), a commercial pectinase, and two high PG activity semi-purified preparations, FI and FII , were applied for maceration at PG activity of 3.5 U g−1 of grape for 46 h. Enzyme-assisted maceration significantly (P < 0.05) increased the total phenolic content from 255.8 to 916.3 ± 5.2, 5732.9 ± 9.9, 563.4 ± 6.7 and 620.6 ± 18.4 mg L−1 for CE, commercial pectinase, FI and FII, respectively. The content of individual phenolics such as gallic, protocatechuic, chlorogenic and p-coumaric acids was improved. Principal component and hierarchical clustering analyses suggested that CE has a better performance upon the release of phenols. Semi-purified preparations acted similar to commercial pectinase. These findings open an opportunity for the potential use of PG from the mutant strain as an alternative macerating enzyme.Article Citation - WoS: 13Citation - Scopus: 18Effect of Physicochemical Parameters on the Polygalacturonase of an Aspergillus Sojae Mutant Using Wheat Bran, an Agro-Industrial Waste, Via Solid-State Fermentation(John Wiley and Sons Inc., 2016) Demir, Hande; Tarı, Canan; 03.08. Department of Food Engineering; 03. Faculty of Engineering; 01. Izmir Institute of TechnologyBACKGROUND: Polygalacturonases (PGs) are valuable enzymes of the food industry; therefore it is of great importance to discover new and GRAS PG-producing microbial strains. In this study, PG enzyme produced from a high PG activity producer mutant Aspergillus sojae using wheat bran at the flask scale under pre-optimized conditions of solid-state fermentation (SSF) was biochemically characterized. RESULTS: The crude PG enzyme showed optimum activity in the pH range 4.0–5.0 and was stable in the pH range 3.0–7.0. The optimum temperature for the PG was 40 °C and it retained 99% of its activity at 50 °C. The mutant A. sojae PG could preserve more than 50% of its stability between 25 and 50 °C, both for 30 and 60 min, and was found to be stable in the presence of most of the tested compounds and metal ions. The inactivation energy (Ed) was determined as 125.3 kJ mol−1. The enthalpy (ΔH*), free energy (ΔG*) and entropy (ΔS*) of inactivation were found to be stable with increasing temperature. CONCLUSION: The mutant A. sojae PG could be suitable for the clarification (depectinization) of orange and grape juices and wine. © 2015 Society of Chemical Industry.
