Effect of TGase Crosslinking on the Structure, Emulsification, and Gelling Properties of Soy Isolate Proteins
Soy isolate protein (SPI), as a high-quality plant protein source, is often processed into various soy products. In this study, the physicochemical properties of SPI treated with transglutaminase (TGase) were investigated in correlation with emulsification characteristics and rheological behavior. T...
Saved in:
| Main Authors: | , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2025-06-01
|
| Series: | Foods |
| Subjects: | |
| Online Access: | https://www.mdpi.com/2304-8158/14/12/2130 |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| _version_ | 1849431863784898560 |
|---|---|
| author | Ziqi Peng Kunlun Liu Ning Liao |
| author_facet | Ziqi Peng Kunlun Liu Ning Liao |
| author_sort | Ziqi Peng |
| collection | DOAJ |
| description | Soy isolate protein (SPI), as a high-quality plant protein source, is often processed into various soy products. In this study, the physicochemical properties of SPI treated with transglutaminase (TGase) were investigated in correlation with emulsification characteristics and rheological behavior. The polyacrylamide gel electrophoresis with sodium dodecyl sulfate (SDS-PAGE) and Fourier-transform infrared spectroscopy (FTIR) and endogenous fluorescence spectrum analysis results showed that TGase was able to promote the covalent binding of lysine and glutamine residues in SPI. The moderate pre-crosslinking treatment of TGase (5–7.5 U/g TGase pre-crosslinked for 2 h or 5 U/g TGase pre-crosslinked for 2–3 h) improved the emulsification and gel properties to varying degrees: the nanoparticle and emulsification performance increased by 24.35% and the storage modulus of the gel increased by 288%. Furthermore, the surface charge of SPI increased due to the crosslinking impact of TGase, indicating a considerable rise in the surface electrostatic potential. Simultaneously, the protein surface exhibited a substantial increase in hydrophobicity, while the level of free sulfhydryl groups reduced. These changes indicate that TGase enzymatic crosslinking could significantly improve the structural stability of nanoparticles by enhancing the generation efficiency of covalent bonds between protein molecules. |
| format | Article |
| id | doaj-art-cf65d26613974b8e8d199d4d674a78ba |
| institution | Kabale University |
| issn | 2304-8158 |
| language | English |
| publishDate | 2025-06-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Foods |
| spelling | doaj-art-cf65d26613974b8e8d199d4d674a78ba2025-08-20T03:27:29ZengMDPI AGFoods2304-81582025-06-011412213010.3390/foods14122130Effect of TGase Crosslinking on the Structure, Emulsification, and Gelling Properties of Soy Isolate ProteinsZiqi Peng0Kunlun Liu1Ning Liao2College of Food Science and Engineering, Henan University of Technology, Zhengzhou 450001, ChinaCollege of Food Science and Engineering, Henan University of Technology, Zhengzhou 450001, ChinaCollege of Food Science and Engineering, Henan University of Technology, Zhengzhou 450001, ChinaSoy isolate protein (SPI), as a high-quality plant protein source, is often processed into various soy products. In this study, the physicochemical properties of SPI treated with transglutaminase (TGase) were investigated in correlation with emulsification characteristics and rheological behavior. The polyacrylamide gel electrophoresis with sodium dodecyl sulfate (SDS-PAGE) and Fourier-transform infrared spectroscopy (FTIR) and endogenous fluorescence spectrum analysis results showed that TGase was able to promote the covalent binding of lysine and glutamine residues in SPI. The moderate pre-crosslinking treatment of TGase (5–7.5 U/g TGase pre-crosslinked for 2 h or 5 U/g TGase pre-crosslinked for 2–3 h) improved the emulsification and gel properties to varying degrees: the nanoparticle and emulsification performance increased by 24.35% and the storage modulus of the gel increased by 288%. Furthermore, the surface charge of SPI increased due to the crosslinking impact of TGase, indicating a considerable rise in the surface electrostatic potential. Simultaneously, the protein surface exhibited a substantial increase in hydrophobicity, while the level of free sulfhydryl groups reduced. These changes indicate that TGase enzymatic crosslinking could significantly improve the structural stability of nanoparticles by enhancing the generation efficiency of covalent bonds between protein molecules.https://www.mdpi.com/2304-8158/14/12/2130protein nanoparticlestransglutaminasecrosslinkingconformational changesproperties |
| spellingShingle | Ziqi Peng Kunlun Liu Ning Liao Effect of TGase Crosslinking on the Structure, Emulsification, and Gelling Properties of Soy Isolate Proteins Foods protein nanoparticles transglutaminase crosslinking conformational changes properties |
| title | Effect of TGase Crosslinking on the Structure, Emulsification, and Gelling Properties of Soy Isolate Proteins |
| title_full | Effect of TGase Crosslinking on the Structure, Emulsification, and Gelling Properties of Soy Isolate Proteins |
| title_fullStr | Effect of TGase Crosslinking on the Structure, Emulsification, and Gelling Properties of Soy Isolate Proteins |
| title_full_unstemmed | Effect of TGase Crosslinking on the Structure, Emulsification, and Gelling Properties of Soy Isolate Proteins |
| title_short | Effect of TGase Crosslinking on the Structure, Emulsification, and Gelling Properties of Soy Isolate Proteins |
| title_sort | effect of tgase crosslinking on the structure emulsification and gelling properties of soy isolate proteins |
| topic | protein nanoparticles transglutaminase crosslinking conformational changes properties |
| url | https://www.mdpi.com/2304-8158/14/12/2130 |
| work_keys_str_mv | AT ziqipeng effectoftgasecrosslinkingonthestructureemulsificationandgellingpropertiesofsoyisolateproteins AT kunlunliu effectoftgasecrosslinkingonthestructureemulsificationandgellingpropertiesofsoyisolateproteins AT ningliao effectoftgasecrosslinkingonthestructureemulsificationandgellingpropertiesofsoyisolateproteins |