TY  - JOUR
AU  - Pavlović, Marija
AU  - Margetić, Aleksandra
AU  - Leonardi, Adrijana
AU  - Križaj, Igor
AU  - Kojić, Milan
AU  - Vujčić, Zoran
AU  - Šokarda Slavić, Marinela
PY  - 2024
UR  - http://intor.torlakinstitut.com/handle/123456789/863
AB  - This study focuses on the isolation, purification, and characterisation of endo-polygalacturonase II from Aspergillus tubingensis FAT43, particularly emphasising its potential applications in the fruit juice industry. A comprehensive screening test revealed the temporal dynamics of endo-polygalacturonase production during a 96-hour fermentation process. The purification process, involving ammonium sulfate and ethanol precipitation followed by ion-exchange chromatography, resulted in a 3.3-fold purification of PG II with a yield of 16% and a specific activity of 6001.67 U mg−1. Molecular analysis confirmed the identity of PG II, its gene (pgaII), and a high degree of sequence identity with Aspergillus tubingensis in the SWISS-PROT database. The optimal pH for PG II activity was 3.5–4.5, with robust stability across a broad pH spectrum (3–7). The enzyme exhibited optimal temperature activity at 45 °C, with a retention of 90% activity at 50 °C. The calculated activation energy for PG II was 62.1 kJ mol−1, indicating good stability. Inactivation kinetics revealed a half-life of 13.7 h at 40 °C, 5.4 h at 50 °C, and 0.85 h at 60 °C, with an activation energy of denaturation of 32.8 kJ mol−1. Compared to literature-reported PGs, PG II from A. tubingensis FAT43 demonstrated superior thermal stability. Hydrolysis experiments on different pectins revealed the highest specificity for non-methylated substrates (polygalacturonic acid). In fruit juice processing, PG II significantly increased juice yield and clarity, with the highest impact observed in strawberry juice. Antioxidant activity assays indicated enhanced antioxidant potential in enzyme-treated juices, especially strawberry, quince, and apple juices. The study highlights PG II's potential as an industrially valuable enzyme for fruit juice processing, offering improved thermostability and versatility across various fruit types.
PB  - Royal Society of Chemistry
T2  - Food & Function
T1  - Improvement of fruit juice quality: novel endo-polygalacturonase II from Aspergillus tubingensis FAT 43 for enhanced liquefaction, clarification, and antioxidant potential
DO  - 10.1039/D3FO05297D
ER  - 

@article{
author = "Pavlović, Marija and Margetić, Aleksandra and Leonardi, Adrijana and Križaj, Igor and Kojić, Milan and Vujčić, Zoran and Šokarda Slavić, Marinela",
year = "2024",
abstract = "This study focuses on the isolation, purification, and characterisation of endo-polygalacturonase II from Aspergillus tubingensis FAT43, particularly emphasising its potential applications in the fruit juice industry. A comprehensive screening test revealed the temporal dynamics of endo-polygalacturonase production during a 96-hour fermentation process. The purification process, involving ammonium sulfate and ethanol precipitation followed by ion-exchange chromatography, resulted in a 3.3-fold purification of PG II with a yield of 16% and a specific activity of 6001.67 U mg−1. Molecular analysis confirmed the identity of PG II, its gene (pgaII), and a high degree of sequence identity with Aspergillus tubingensis in the SWISS-PROT database. The optimal pH for PG II activity was 3.5–4.5, with robust stability across a broad pH spectrum (3–7). The enzyme exhibited optimal temperature activity at 45 °C, with a retention of 90% activity at 50 °C. The calculated activation energy for PG II was 62.1 kJ mol−1, indicating good stability. Inactivation kinetics revealed a half-life of 13.7 h at 40 °C, 5.4 h at 50 °C, and 0.85 h at 60 °C, with an activation energy of denaturation of 32.8 kJ mol−1. Compared to literature-reported PGs, PG II from A. tubingensis FAT43 demonstrated superior thermal stability. Hydrolysis experiments on different pectins revealed the highest specificity for non-methylated substrates (polygalacturonic acid). In fruit juice processing, PG II significantly increased juice yield and clarity, with the highest impact observed in strawberry juice. Antioxidant activity assays indicated enhanced antioxidant potential in enzyme-treated juices, especially strawberry, quince, and apple juices. The study highlights PG II's potential as an industrially valuable enzyme for fruit juice processing, offering improved thermostability and versatility across various fruit types.",
publisher = "Royal Society of Chemistry",
journal = "Food & Function",
title = "Improvement of fruit juice quality: novel endo-polygalacturonase II from Aspergillus tubingensis FAT 43 for enhanced liquefaction, clarification, and antioxidant potential",
doi = "10.1039/D3FO05297D"
}

Pavlović, M., Margetić, A., Leonardi, A., Križaj, I., Kojić, M., Vujčić, Z.,& Šokarda Slavić, M.. (2024). Improvement of fruit juice quality: novel endo-polygalacturonase II from Aspergillus tubingensis FAT 43 for enhanced liquefaction, clarification, and antioxidant potential. in Food & Function
Royal Society of Chemistry..
https://doi.org/10.1039/D3FO05297D

Pavlović M, Margetić A, Leonardi A, Križaj I, Kojić M, Vujčić Z, Šokarda Slavić M. Improvement of fruit juice quality: novel endo-polygalacturonase II from Aspergillus tubingensis FAT 43 for enhanced liquefaction, clarification, and antioxidant potential. in Food & Function. 2024;.
doi:10.1039/D3FO05297D .

Pavlović, Marija, Margetić, Aleksandra, Leonardi, Adrijana, Križaj, Igor, Kojić, Milan, Vujčić, Zoran, Šokarda Slavić, Marinela, "Improvement of fruit juice quality: novel endo-polygalacturonase II from Aspergillus tubingensis FAT 43 for enhanced liquefaction, clarification, and antioxidant potential" in Food & Function (2024),
https://doi.org/10.1039/D3FO05297D . .