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Preparation, physicochemical properties, and formation mechanism of quinoa self-assembled peptide-based hydrogel

文献类型： 外文期刊

作者： Fan, Xin 1 ; Guo, Huimin 1 ; Richel, Aurore 5 ; Zhang, Lizhen 3 ; Liu, Chenghong 4 ; Qin, Peiyou 1 ; Blecker, Christophe 6 ; Ren, Guixing 1 ;

作者机构： 1.Chinese Acad Agr Sci, Inst Crop Sci, Key Lab Qual Evaluat & Nutr Hlth Agroprod, Minist Agr & Rural Affairs, Beijing 100081, Peoples R China

2.Chengdu Univ, Sch Food & Biol Engn, Key Lab Coarse Cereal Proc, Minist Agr & Rural Affairs, Chengdu 610106, Peoples R China

3.Shanxi Univ, Sch Life Sci, Key Lab Chem Biol & Mol Engn, Minist Educ, Taiyuan 030006, Peoples R China

4.Shanghai Acad Agr Sci, Shanghai Key Lab Agr Genet & Breeding, Biotechnol Res Inst, Shanghai 201106, Peoples R China

5.Univ Liege, Lab Biomass & Green Technol, Gembloux Agrobio Tech, Gembloux, Belgium

6.Univ Liege, Dept Food Sci & Formulat, Gembloux Agrobio Tech, Gembloux, Belgium

7.Chinese Acad Agr Sci, Inst Crop Sci, Beijing 100081, Peoples R China

关键词： Quinoa protein; Enzymatic hydrolysis; Gelation; Rheological property; Microstructure; Molecular characteristics

期刊名称：FOOD HYDROCOLLOIDS （ 影响因子：10.7； 五年影响因子：10.9 ）

ISSN： 0268-005X

年卷期： 2023 年 145 卷

页码：

收录情况： SCI

摘要： Currently, self-assembly peptides with hydrogel properties that are used in various applications are being chemically synthesized. These peptides not only have safety and environmental problems but are also expensive and cumbersome to prepare. The present study established a convenient and efficient method for producing plant-based peptides with decent gel-forming ability from quinoa proteins. After alkaline protease treatment, hydrogels made with quinoa protein hydrolysis exhibited potent self-assembly capacity, enhanced gel hardness, and improved rheological properties. Moreover, the microstructure results revealed that the quinoa peptide hydrogels had regular, uniform, and interconnected porous structures. These observations were primarily attributed to the hydrogen bonding force and hydrophobic aggregation caused by hydrophobic group exposure. Amino acid and proteomics analysis suggested that the amino acid composition and sequence of quinoa peptides significantly influenced the formation of self-assembled hydrogels. Overall, this study provided a cost-effective approach to improve the gelling ability of quinoa protein and could potentially replace the use of chemically synthesized peptides in various applications, laying the theoretical basis for the development of novel natural plant-based foods.

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