Evidence map›Paper›PMID 41683085›Full record

ArticleFoods (Basel, Switzerland)2026

Structural Characterization and Emulsifying Properties of Highly Soluble Macadamia-Soybean Protein Composites Fabricated by Alkaline-Thermal Treatment.

Xiaohong He, Xixiang Shuai, Ming Zhang, Mingfeng Fang, Lei Zhao, Yunhui Cheng, Liqing Du

Abstract read
In one paragraph

Article in Foods (Basel, Switzerland), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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1 · What the graph read from it

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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

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3 · Its place in the literature

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4 · The record

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5 · Who and what money

Authors and funding

7 authors.

Xiaohong HeSouth Subtropical Crops Research Institute, Chinese Academy of Tropical Agricultural Sciences, Key Laboratory of Tropical Fruit Biology, Ministry of Agriculture & Rural Affairs, Key Laboratory of Postharvest Physiology and Technology of Tropical Horticultural Products of Hainan Province, Zhanjiang 524091, China.
Xixiang ShuaiSouth Subtropical Crops Research Institute, Chinese Academy of Tropical Agricultural Sciences, Key Laboratory of Tropical Fruit Biology, Ministry of Agriculture & Rural Affairs, Key Laboratory of Postharvest Physiology and Technology of Tropical Horticultural Products of Hainan Province, Zhanjiang 524091, China.
Ming ZhangSouth Subtropical Crops Research Institute, Chinese Academy of Tropical Agricultural Sciences, Key Laboratory of Tropical Fruit Biology, Ministry of Agriculture & Rural Affairs, Key Laboratory of Postharvest Physiology and Technology of Tropical Horticultural Products of Hainan Province, Zhanjiang 524091, China.
Mingfeng FangSouth Subtropical Crops Research Institute, Chinese Academy of Tropical Agricultural Sciences, Key Laboratory of Tropical Fruit Biology, Ministry of Agriculture & Rural Affairs, Key Laboratory of Postharvest Physiology and Technology of Tropical Horticultural Products of Hainan Province, Zhanjiang 524091, China.
Lei ZhaoCollege of Food Science, South China Agricultural University, Guangzhou 510642, China.ORCID 0000-0001-9928-3861
Yunhui ChengSchool of Food Science and Bioengineering, Changsha University of Science & Technology, Changsha 410114, China.
Liqing DuSouth Subtropical Crops Research Institute, Chinese Academy of Tropical Agricultural Sciences, Key Laboratory of Tropical Fruit Biology, Ministry of Agriculture & Rural Affairs, Key Laboratory of Postharvest Physiology and Technology of Tropical Horticultural Products of Hainan Province, Zhanjiang 524091, China.

Funding

Hainan Province Natural Science Foundation of China 325QN429the Central Public-interest Scientific Institution Basal Research Fund for China Academy of Tropical Agricultural Sciences 1630062025001the National Natural Science Foundation of China 32402150
6 · The paper itself

Abstract

The complementarity of plant proteins from various sources could achieve higher nutritional value to satisfy the requirement of replacing animal proteins. Therefore, it is very important to seek efficient and convenient approaches to fabricate highly soluble protein composites. In this study, macadamia protein-soybean protein (SP-MP') composites were fabricated by alkaline-thermal treating at different ratios of 1:0.5, 1:1, and 1:2; then, the nitrogen solubility index, particle characteristics, and structure and emulsifying properties of SP-MP' composites were investigated. The nitrogen solubility indexes of SP-MP' composites were higher than 80%, and less small insoluble aggregates were observed by scanning electron microscopy. SP-MP' composites exhibited high ζ-potential values, which were higher than -50 mV. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) analysis found that both subunits of individually alkaline-thermal-treated macadamia protein (MP') and soybean protein (SP') were presented in SP-MP' composites. The results of fluorescence, sulfhydryl group, and secondary structure illustrated that the SP interacted with MP to form SP-MP' composites by the co-folding of proteins during neutralization. Compared to the individual proteins, SP-MP' composites exhibited stronger emulsification ability and stability indexes (EAI and ESI) as the proportion of MP increased, and the EAI and ESI of SP-MP

Indexed as

alkaline-thermal treatmentemulsifying propertiesprotein interactionssolubilitystructural analysis

Identifiers

PMID41683085
PMCPMC12896509

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