Freeze-thaw stability of transglutaminase-induced soy protein-maltose emulsion gel : Focusing on morphology, texture properties, and rheological characteristics
Copyright © 2024 Elsevier B.V. All rights reserved..
In this study, soy protein isolate (SPI) and maltose (M) were employed as materials for the synthesis of a covalent compound denoted as SPI-M. The emulsion gel was prepared by transglutaminase (TGase) as catalyst, and its freeze-thaw stability was investigated. The occurrence of Maillard reaction was substantiated through SDS-PAGE. The analysis of spectroscopy showed that the structure of the modified protein was more stretched, changed in the direction of freeze-thaw stability. After three freeze-thaw cycles (FTC), it was observed that the water holding capacity of SPI-M, SPI/M mixture (SPI+M) and SPI emulsion gels exhibited reductions of 8.49 %, 16.85 %, and 20.26 %, respectively. Moreover, the soluble protein content also diminished by 13.92 %, 23.43 %, and 35.31 %, respectively. In comparison to unmodified SPI, SPI-M exhibited increase in gel hardness by 160 %, while elasticity, viscosity, chewability, and cohesion demonstrated reductions of 17.7 %, 23.3 %, 33.3 %, and 6.76 %, respectively. Concurrently, the SPI-M emulsion gel exhibited the most rapid gel formation kinetics. After FTCs, the gel elastic modulus (G') and viscosity modulus (G″) of SPI-M emulsion were the largest. DSC analysis underscored the more compact structure and heightened thermal stability of the SPI-M emulsion gel. SEM demonstrated that the SPI-M emulsion gel suffered the least damage following FTCs.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2024 |
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| Erschienen: |
2024 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:261 |
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| Enthalten in: |
International journal of biological macromolecules - 261(2024), Pt 1 vom: 01. März, Seite 129716 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Zhang, Mengyue [VerfasserIn] |
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| Links: |
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| Themen: |
69-79-4 |
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| Anmerkungen: |
Date Completed 11.03.2024 Date Revised 11.03.2024 published: Print-Electronic Citation Status MEDLINE |
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| doi: |
10.1016/j.ijbiomac.2024.129716 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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| 520 | |a Copyright © 2024 Elsevier B.V. All rights reserved. | ||
| 520 | |a In this study, soy protein isolate (SPI) and maltose (M) were employed as materials for the synthesis of a covalent compound denoted as SPI-M. The emulsion gel was prepared by transglutaminase (TGase) as catalyst, and its freeze-thaw stability was investigated. The occurrence of Maillard reaction was substantiated through SDS-PAGE. The analysis of spectroscopy showed that the structure of the modified protein was more stretched, changed in the direction of freeze-thaw stability. After three freeze-thaw cycles (FTC), it was observed that the water holding capacity of SPI-M, SPI/M mixture (SPI+M) and SPI emulsion gels exhibited reductions of 8.49 %, 16.85 %, and 20.26 %, respectively. Moreover, the soluble protein content also diminished by 13.92 %, 23.43 %, and 35.31 %, respectively. In comparison to unmodified SPI, SPI-M exhibited increase in gel hardness by 160 %, while elasticity, viscosity, chewability, and cohesion demonstrated reductions of 17.7 %, 23.3 %, 33.3 %, and 6.76 %, respectively. Concurrently, the SPI-M emulsion gel exhibited the most rapid gel formation kinetics. After FTCs, the gel elastic modulus (G') and viscosity modulus (G″) of SPI-M emulsion were the largest. DSC analysis underscored the more compact structure and heightened thermal stability of the SPI-M emulsion gel. SEM demonstrated that the SPI-M emulsion gel suffered the least damage following FTCs | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Emulsion gel | |
| 650 | 4 | |a Freeze-thaw stability | |
| 650 | 4 | |a Maillard reaction | |
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| 650 | 7 | |a Soybean Proteins |2 NLM | |
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| 700 | 1 | |a Zhang, Bo-Ya |e verfasserin |4 aut | |
| 700 | 1 | |a Sun, Xiaotong |e verfasserin |4 aut | |
| 700 | 1 | |a Liu, Yi-An |e verfasserin |4 aut | |
| 700 | 1 | |a Yu, Zhichao |e verfasserin |4 aut | |
| 700 | 1 | |a Wang, Xibo |e verfasserin |4 aut | |
| 700 | 1 | |a Xu, Ning |e verfasserin |4 aut | |
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