2026-06-21T23:23:17Zhttps://riubu.ubu.es/oai/requestoai:riubu.ubu.es:10259/51602021-11-10T09:38:20Zcom_10259_4244com_10259_5086com_10259_2604col_10259_4245
Repositorio Institucional de la Universidad de Burgos
author
Illera Gigante, Alba Ester
author
Beltrán Calvo, Sagrario
author
Sanz Díez, Mª Teresa
2019-11-07T12:55:04Z
2019-11-07T12:55:04Z
2019-09
http://hdl.handle.net/10259/5160
10.1038/s41598-019-50209-w
2045-2322
Polyphenoloxidase from apple was extracted and further concentrated by cationic reversed micellar extraction. Previous to reversed micellar extraction a crude protein extract was obtained using AG2-X8 as adsorbent of phenolic compounds and the detergent Triton X-100. Forward and backward extraction conditions were optimized by using dodecyl trimethyl ammonium bromide as surfactant in the organic phase. Optimization was carried out to obtain the highest value of PPO activity recovery and the purification fold at the different experimental conditions. Under the optimum extraction conditions, PPO activity recovery was 99% and purification fold reached a value of 17, showing that reversed micellar extraction was a good technique as a first step to concentrate on a targeted enzyme. After removing some impurities by centrifuge ultrafiltration, the protein extract with PPO activity was treated by pressurized carbon dioxide and thermosonication achieving residual PPO activity values of 16 ± 3 and 9 ± 1%, respectively. Quenching experiments by iodide performed in the non-treated extract and in the treated extracts revealed conformational changes of this protein fraction reflected in the greater exposure of the fluorophore to the quencher.
eng
Structural changes of a protein extract from apple with polyphenoloxidase activity obtained by cationic reversed micellar extraction induced by high-pressure carbon dioxide and thermosonication
info:eu-repo/semantics/article
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URL
https://riubu.ubu.es/bitstream/10259/5160/1/Illera-sr_2019.pdf
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Illera-sr_2019.pdf.txt