Enhancing Solubility and Reducing Thermal Aggregation in Pea Proteins through Protein Glutaminase-Mediated Deamidation
The limited solubility and stability of pea proteins hinder their utilization in liquid formulations. In this study, protein glutaminase (PG) was employed to modify pea protein isolates (PPIs) and obtain deamidated PPI with varying degrees of deamidation (DD, 10–25%). The solubility and thermal stab...
| Main Authors: | , , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2023-11-01
|
| Series: | Foods |
| Subjects: | |
| Online Access: | https://www.mdpi.com/2304-8158/12/22/4130 |
| _version_ | 1797459359111839744 |
|---|---|
| author | Lijuan Luo Yuanyuan Deng Guang Liu Pengfei Zhou Zhihao Zhao Ping Li Mingwei Zhang |
| author_facet | Lijuan Luo Yuanyuan Deng Guang Liu Pengfei Zhou Zhihao Zhao Ping Li Mingwei Zhang |
| author_sort | Lijuan Luo |
| collection | DOAJ |
| description | The limited solubility and stability of pea proteins hinder their utilization in liquid formulations. In this study, protein glutaminase (PG) was employed to modify pea protein isolates (PPIs) and obtain deamidated PPI with varying degrees of deamidation (DD, 10–25%). The solubility and thermal stability of these deamidated PPI samples were assessed, and a comprehensive analysis, including SDS-PAGE, zeta potential, FTIR, surface hydrophobicity, and intrinsic fluorescence, was conducted to elucidate the mechanism behind the improvement in their functional properties. The results reveal that PG modification greatly enhances the solubility and heat stability of PPI, with the most notable improvements observed at higher DD (>20%). PG modification increases the net charge of PPI, leading to the unfolding and extension of the protein structures, thus exposing more hydrophobic groups. These structural changes are particularly pronounced when DD exceeds 20%. This increased electrostatic repulsion between carboxyl groups would promote protein unfolding, enhancing interactions with water and hindering the aggregation of unfolded protein in the presence of salts at elevated temperatures (supported by high-performance size exclusion chromatography and transmission electron microscopy). Accordingly, PG-mediated deamidation shows promise in enhancing the functional properties of PPI. |
| first_indexed | 2024-03-09T16:50:18Z |
| format | Article |
| id | doaj.art-e3839a9988e84607b6baaea4fd2014a5 |
| institution | Directory Open Access Journal |
| issn | 2304-8158 |
| language | English |
| last_indexed | 2024-03-09T16:50:18Z |
| publishDate | 2023-11-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Foods |
| spelling | doaj.art-e3839a9988e84607b6baaea4fd2014a52023-11-24T14:42:09ZengMDPI AGFoods2304-81582023-11-011222413010.3390/foods12224130Enhancing Solubility and Reducing Thermal Aggregation in Pea Proteins through Protein Glutaminase-Mediated DeamidationLijuan Luo0Yuanyuan Deng1Guang Liu2Pengfei Zhou3Zhihao Zhao4Ping Li5Mingwei Zhang6Sericultural & Agri-Food Research Institute Guangdong Academy of Agricultural Sciences, Key Laboratory of Functional Foods, Ministry of Agriculture and Rural Affairs, Guangdong Key Laboratory of Agricultural Products Processing, Guangzhou 510610, ChinaSericultural & Agri-Food Research Institute Guangdong Academy of Agricultural Sciences, Key Laboratory of Functional Foods, Ministry of Agriculture and Rural Affairs, Guangdong Key Laboratory of Agricultural Products Processing, Guangzhou 510610, ChinaSericultural & Agri-Food Research Institute Guangdong Academy of Agricultural Sciences, Key Laboratory of Functional Foods, Ministry of Agriculture and Rural Affairs, Guangdong Key Laboratory of Agricultural Products Processing, Guangzhou 510610, ChinaSericultural & Agri-Food Research Institute Guangdong Academy of Agricultural Sciences, Key Laboratory of Functional Foods, Ministry of Agriculture and Rural Affairs, Guangdong Key Laboratory of Agricultural Products Processing, Guangzhou 510610, ChinaSericultural & Agri-Food Research Institute Guangdong Academy of Agricultural Sciences, Key Laboratory of Functional Foods, Ministry of Agriculture and Rural Affairs, Guangdong Key Laboratory of Agricultural Products Processing, Guangzhou 510610, ChinaSericultural & Agri-Food Research Institute Guangdong Academy of Agricultural Sciences, Key Laboratory of Functional Foods, Ministry of Agriculture and Rural Affairs, Guangdong Key Laboratory of Agricultural Products Processing, Guangzhou 510610, ChinaSericultural & Agri-Food Research Institute Guangdong Academy of Agricultural Sciences, Key Laboratory of Functional Foods, Ministry of Agriculture and Rural Affairs, Guangdong Key Laboratory of Agricultural Products Processing, Guangzhou 510610, ChinaThe limited solubility and stability of pea proteins hinder their utilization in liquid formulations. In this study, protein glutaminase (PG) was employed to modify pea protein isolates (PPIs) and obtain deamidated PPI with varying degrees of deamidation (DD, 10–25%). The solubility and thermal stability of these deamidated PPI samples were assessed, and a comprehensive analysis, including SDS-PAGE, zeta potential, FTIR, surface hydrophobicity, and intrinsic fluorescence, was conducted to elucidate the mechanism behind the improvement in their functional properties. The results reveal that PG modification greatly enhances the solubility and heat stability of PPI, with the most notable improvements observed at higher DD (>20%). PG modification increases the net charge of PPI, leading to the unfolding and extension of the protein structures, thus exposing more hydrophobic groups. These structural changes are particularly pronounced when DD exceeds 20%. This increased electrostatic repulsion between carboxyl groups would promote protein unfolding, enhancing interactions with water and hindering the aggregation of unfolded protein in the presence of salts at elevated temperatures (supported by high-performance size exclusion chromatography and transmission electron microscopy). Accordingly, PG-mediated deamidation shows promise in enhancing the functional properties of PPI.https://www.mdpi.com/2304-8158/12/22/4130enzymatic deamidationsecondary structuretertiary structuresolubilitythermal stability |
| spellingShingle | Lijuan Luo Yuanyuan Deng Guang Liu Pengfei Zhou Zhihao Zhao Ping Li Mingwei Zhang Enhancing Solubility and Reducing Thermal Aggregation in Pea Proteins through Protein Glutaminase-Mediated Deamidation Foods enzymatic deamidation secondary structure tertiary structure solubility thermal stability |
| title | Enhancing Solubility and Reducing Thermal Aggregation in Pea Proteins through Protein Glutaminase-Mediated Deamidation |
| title_full | Enhancing Solubility and Reducing Thermal Aggregation in Pea Proteins through Protein Glutaminase-Mediated Deamidation |
| title_fullStr | Enhancing Solubility and Reducing Thermal Aggregation in Pea Proteins through Protein Glutaminase-Mediated Deamidation |
| title_full_unstemmed | Enhancing Solubility and Reducing Thermal Aggregation in Pea Proteins through Protein Glutaminase-Mediated Deamidation |
| title_short | Enhancing Solubility and Reducing Thermal Aggregation in Pea Proteins through Protein Glutaminase-Mediated Deamidation |
| title_sort | enhancing solubility and reducing thermal aggregation in pea proteins through protein glutaminase mediated deamidation |
| topic | enzymatic deamidation secondary structure tertiary structure solubility thermal stability |
| url | https://www.mdpi.com/2304-8158/12/22/4130 |
| work_keys_str_mv | AT lijuanluo enhancingsolubilityandreducingthermalaggregationinpeaproteinsthroughproteinglutaminasemediateddeamidation AT yuanyuandeng enhancingsolubilityandreducingthermalaggregationinpeaproteinsthroughproteinglutaminasemediateddeamidation AT guangliu enhancingsolubilityandreducingthermalaggregationinpeaproteinsthroughproteinglutaminasemediateddeamidation AT pengfeizhou enhancingsolubilityandreducingthermalaggregationinpeaproteinsthroughproteinglutaminasemediateddeamidation AT zhihaozhao enhancingsolubilityandreducingthermalaggregationinpeaproteinsthroughproteinglutaminasemediateddeamidation AT pingli enhancingsolubilityandreducingthermalaggregationinpeaproteinsthroughproteinglutaminasemediateddeamidation AT mingweizhang enhancingsolubilityandreducingthermalaggregationinpeaproteinsthroughproteinglutaminasemediateddeamidation |