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Investigation of Consequences of High-Voltage Pulsed Electric Field and TGase Cross-Linking on the Physicochemical and Rheological Properties of Pleurotus eryngii Protein
This study aimed to evaluate the effects of high-voltage pulsed electric fields (HPEF) and transglutaminase (TGase) cross-clinking on the physicochemical and rheological properties of Pleurotus eryngii protein (PEP). The results showed that HPEF increased α-helixes and β-turns but decreased β-folds....
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9914717/ https://www.ncbi.nlm.nih.gov/pubmed/36766175 http://dx.doi.org/10.3390/foods12030647 |
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author | Li, Jiaxin Feng, Yan Cheng, Qianying Liu, Jingyu Yun, Shaojun Cheng, Yanfen Cheng, Feier Cao, Jinling Feng, Cuiping |
author_facet | Li, Jiaxin Feng, Yan Cheng, Qianying Liu, Jingyu Yun, Shaojun Cheng, Yanfen Cheng, Feier Cao, Jinling Feng, Cuiping |
author_sort | Li, Jiaxin |
collection | PubMed |
description | This study aimed to evaluate the effects of high-voltage pulsed electric fields (HPEF) and transglutaminase (TGase) cross-clinking on the physicochemical and rheological properties of Pleurotus eryngii protein (PEP). The results showed that HPEF increased α-helixes and β-turns but decreased β-folds. A HPEF at 1500 V/cm maximized the free sulfhydryl content and solubility of PEP. TGase formed high-molecular-weight polymers in PEP. TGase at 0.25% maximized the free sulfhydryl groups, particle size, and solubility; shifted the maximum absorption wavelength from 343 nm to 339 nm and 341 nm; increased α-helixes and β-turns and decreased β-folds; and showed better rheological properties. Compared with TGase cross-linking, HPEF-1500 V/cm and 1% TGase significantly reduced the free sulfhydryl groups, particle size, and solubility, produced more uniform network structures, and improved the rheological properties. These results suggest that HPEF can increase the cross-linking of TGase and improve rheological properties of TGase-cross-linked PEP by affecting the physicochemical properties. |
format | Online Article Text |
id | pubmed-9914717 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-99147172023-02-11 Investigation of Consequences of High-Voltage Pulsed Electric Field and TGase Cross-Linking on the Physicochemical and Rheological Properties of Pleurotus eryngii Protein Li, Jiaxin Feng, Yan Cheng, Qianying Liu, Jingyu Yun, Shaojun Cheng, Yanfen Cheng, Feier Cao, Jinling Feng, Cuiping Foods Article This study aimed to evaluate the effects of high-voltage pulsed electric fields (HPEF) and transglutaminase (TGase) cross-clinking on the physicochemical and rheological properties of Pleurotus eryngii protein (PEP). The results showed that HPEF increased α-helixes and β-turns but decreased β-folds. A HPEF at 1500 V/cm maximized the free sulfhydryl content and solubility of PEP. TGase formed high-molecular-weight polymers in PEP. TGase at 0.25% maximized the free sulfhydryl groups, particle size, and solubility; shifted the maximum absorption wavelength from 343 nm to 339 nm and 341 nm; increased α-helixes and β-turns and decreased β-folds; and showed better rheological properties. Compared with TGase cross-linking, HPEF-1500 V/cm and 1% TGase significantly reduced the free sulfhydryl groups, particle size, and solubility, produced more uniform network structures, and improved the rheological properties. These results suggest that HPEF can increase the cross-linking of TGase and improve rheological properties of TGase-cross-linked PEP by affecting the physicochemical properties. MDPI 2023-02-02 /pmc/articles/PMC9914717/ /pubmed/36766175 http://dx.doi.org/10.3390/foods12030647 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Li, Jiaxin Feng, Yan Cheng, Qianying Liu, Jingyu Yun, Shaojun Cheng, Yanfen Cheng, Feier Cao, Jinling Feng, Cuiping Investigation of Consequences of High-Voltage Pulsed Electric Field and TGase Cross-Linking on the Physicochemical and Rheological Properties of Pleurotus eryngii Protein |
title | Investigation of Consequences of High-Voltage Pulsed Electric Field and TGase Cross-Linking on the Physicochemical and Rheological Properties of Pleurotus eryngii Protein |
title_full | Investigation of Consequences of High-Voltage Pulsed Electric Field and TGase Cross-Linking on the Physicochemical and Rheological Properties of Pleurotus eryngii Protein |
title_fullStr | Investigation of Consequences of High-Voltage Pulsed Electric Field and TGase Cross-Linking on the Physicochemical and Rheological Properties of Pleurotus eryngii Protein |
title_full_unstemmed | Investigation of Consequences of High-Voltage Pulsed Electric Field and TGase Cross-Linking on the Physicochemical and Rheological Properties of Pleurotus eryngii Protein |
title_short | Investigation of Consequences of High-Voltage Pulsed Electric Field and TGase Cross-Linking on the Physicochemical and Rheological Properties of Pleurotus eryngii Protein |
title_sort | investigation of consequences of high-voltage pulsed electric field and tgase cross-linking on the physicochemical and rheological properties of pleurotus eryngii protein |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9914717/ https://www.ncbi.nlm.nih.gov/pubmed/36766175 http://dx.doi.org/10.3390/foods12030647 |
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