The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Effect of pH-shifting treatment on structural and heat induced gel properties of peanut protein isolate
Abstract
Modifying proteins with new methods to improve their functional properties is essential to extend their application in food related field. In this study, the effect of pH-shifting treatment on structural and heat induced gel properties of peanut protein isolate (PPI) were investigated. PPI was subject to different pH conditions (pH 2, pH 4, pH 10, and pH 12) for 1 h, then adjusted back to pH 7 and they were marked as PPI2, PPI4, PPI10, and PPI12, respectively. It was found that the breaking force (BF) and water holding capacity (WHC) of PPI10 gel were significantly improved due to the decreased particle size, increased solubility, free sulfhydryl group content and surface hydrophobicity of PPI10. While PPI2 or PPI12 lost their gel ability due to the formation of large protein aggregates. These results indicated that pH-shifting treatment might be a convenient and economical method to prepare PPI with different gel and structural properties.
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Cites
Improved enzymatic accessibility of peanut protein isolate pre-treated using thermosonication
Chen, L., Ettelaie, R., & Akhtar, M. (2019) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2019.02.050 · Cited by 62
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Figueroa-González, J. J., Lobato-Calleros, C., Vernon-Carter, E. J., Aguirre-Mandujano, E., Alvarez-Ramirez, J., & Martínez-Velasco, A. (2022) · LWT · doi:10.1016/j.lwt.2021.112561 · Cited by 144
Effect of pH-shifting and ultrasound on soy/potato protein structure and gelation
Sun, Y., Wang, L., Wang, H., Zhou, B., Jiang, L., & Zhu, X. (2025) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2024.110672 · Cited by 106
Guo, R., Liu, L., Huang, Y., Lv, M., Zhu, Y., Wang, Z., Zhu, X., & Sun, B. (2023) · Food Research International · doi:10.1016/j.foodres.2023.113124 · Cited by 96
Zhang, S., Huang, W., Roopesh, M. S., & Chen, L. (2022) · Food Research International · doi:10.1016/j.foodres.2022.111028 · Cited by 96
Zhao, C., Wang, F., Yang, X., Mao, Y., Qi, Q., Zheng, M., Xu, X., Cao, Y., Wu, Y., & Liu, J. (2023) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2022.108374 · Cited by 84
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Guidi, S., Formica, F. A., & Denkel, C. (2022) · Food Research International · doi:10.1016/j.foodres.2022.111752 · Cited by 83
Liu, Z., Li, X., Guan, Z., Jia, Z., Zhang, Z., Yang, C., & Wang, J. (2024) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2024.110158 · Cited by 50
Li, N., Yang, M., Guo, Y., Tong, L.-T., Wang, Y., Zhang, S., Wang, L., Fan, B., Wang, F., & Liu, L. (2022) · LWT · doi:10.1016/j.lwt.2022.113381 · Cited by 45
Self-citationAllergenicity of Peanut Allergens and Its Dependence on the Structure
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Lei, Y., Yue, J., Min, T., Cheng, C., Weng, S., Long, Y., Luo, Y., Zheng, Y., & Wan, Y. (2025) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2024.110988 · Cited by 24
Metadata
- Authors
- Li, J., Wu, M., Wang, Y., Li, K., Du, J., & Bai, Y.
- Venue
- Food Chemistry
- Publisher
- Elsevier BV
- Published
- 2020-09
- Volume
- 325
- Pages
- 126921
- ISSN
- 0308-8146 (ISSN-L)
- OpenAlex
- W3023097777
- Cited by
- 293
- References
- 1
- FWCI
- 17.25
- Type
- journal article
- Language
- en
- Open access
- closed
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