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Relationship between Calcium-binding Ability and Structure of Soybean Protein Based on the Change of Preparation

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Bibliographic Details
Title: Relationship between Calcium-binding Ability and Structure of Soybean Protein Based on the Change of Preparation
Authors: Huilin LUAN, Xiaohan HUA, Wenhua YU, Xin JIA, Lijun YIN
Source: Shipin gongye ke-ji, Vol 46, Iss 2, Pp 45-54 (2025)
Publisher Information: The editorial department of Science and Technology of Food Industry, 2025.
Publication Year: 2025
Collection: LCC:Food processing and manufacture
Subject Terms: soybean protein, extraction condition, alkali-soluble acid precipitation, heat treatment, enzymatic hydrolysis, calcium-binding ability, structure, Food processing and manufacture, TP368-456
Description: Soybean protein was a high-quality plant-based alternative protein, yet its calcium content was lower than animal protein. This study measured the calcium-binding ability of soybean protein under different extraction, heat treatment, and enzymatic hydrolysis conditions. The differences in calcium-binding ability, subunit composition, secondary structure, tertiary structure and hydrophobicity of soybean protein under four different preparation methods were compared. The relationship between the calcium-binding ability and the structure of soybean protein were discussed. The results showed that the binding of soybean protein and calcium ions was related to both the protein's secondary structure composition and its hydrophobicity. Heat treatment and enzymatic hydrolysis unfolded the secondary structure, leading to the enhancement of hydrophobicity and the exposure of the calcium-binding sites. Enzymolysis led to the aggregation of small molecular weight proteins, causing a spatial restructuring of the protein. These changes resulted in a 53% increase in bound calcium compared to heat treatment. The heat-enzyme combined treatment was the most effective among various treatments, which could increase the Ca2+ of the protein by about 2 folds and decrease the precipitation rate by 43%. Optimal soybean protein with high calcium-binding ability preparation involved dissolution at pH8 and 25 ℃, with acid-precipitated proteins dissolved in four times water at pH8. Subsequent steps included heating at 100 ℃ for 30 minutes, and enzymatic treatment using 1000 U/g flavor protease for three hours.
Document Type: article
File Description: electronic resource
Language: Chinese
ISSN: 1002-0306
Relation: https://doaj.org/toc/1002-0306
DOI: 10.13386/j.issn1002-0306.2023120282
Access URL: https://doaj.org/article/dd82693582c04d17bc4b690c131910b8
Accession Number: edsdoj.82693582c04d17bc4b690c131910b8
Database: Directory of Open Access Journals
Description
Abstract:Soybean protein was a high-quality plant-based alternative protein, yet its calcium content was lower than animal protein. This study measured the calcium-binding ability of soybean protein under different extraction, heat treatment, and enzymatic hydrolysis conditions. The differences in calcium-binding ability, subunit composition, secondary structure, tertiary structure and hydrophobicity of soybean protein under four different preparation methods were compared. The relationship between the calcium-binding ability and the structure of soybean protein were discussed. The results showed that the binding of soybean protein and calcium ions was related to both the protein's secondary structure composition and its hydrophobicity. Heat treatment and enzymatic hydrolysis unfolded the secondary structure, leading to the enhancement of hydrophobicity and the exposure of the calcium-binding sites. Enzymolysis led to the aggregation of small molecular weight proteins, causing a spatial restructuring of the protein. These changes resulted in a 53% increase in bound calcium compared to heat treatment. The heat-enzyme combined treatment was the most effective among various treatments, which could increase the Ca2+ of the protein by about 2 folds and decrease the precipitation rate by 43%. Optimal soybean protein with high calcium-binding ability preparation involved dissolution at pH8 and 25 ℃, with acid-precipitated proteins dissolved in four times water at pH8. Subsequent steps included heating at 100 ℃ for 30 minutes, and enzymatic treatment using 1000 U/g flavor protease for three hours.
ISSN:10020306
DOI:10.13386/j.issn1002-0306.2023120282