Dual modification of soy protein isolate by phlorotannins and enzymatic hydrolysis: Stability and digestive properties

IF 11 1区农林科学 Q1 CHEMISTRY, APPLIED

Food Hydrocolloids Pub Date : 2025-02-25 DOI:10.1016/j.foodhyd.2025.111276

Ziteng Lian, Ruihan Su, Qianqian Zhang, Yaqi Tang, Sai Yang, Xiuying Liu, Lin Cheng, Huan Wang, Lianzhou Jiang

{"title":"Dual modification of soy protein isolate by phlorotannins and enzymatic hydrolysis: Stability and digestive properties","authors":"Ziteng Lian, Ruihan Su, Qianqian Zhang, Yaqi Tang, Sai Yang, Xiuying Liu, Lin Cheng, Huan Wang, Lianzhou Jiang","doi":"10.1016/j.foodhyd.2025.111276","DOIUrl":null,"url":null,"abstract":"<div><div>The dense structure of soy protein isolate (SPI) usually leads to reduced stability and digestibility, limiting its practical application. Protease hydrolysis and polyphenol complexation are considered green means to modify the protein to improve its properties. The study aimed to address the persistent challenges associated with the stability and digestibility of SPI through dual modification of enzymatic hydrolysis and polyphenol. Complexes of varying concentrations of phlorotannins (0, 0.2, 0.5, 1.0, 2.0 mg/mL) with SPI and SPI hydrolysate (SPIH) were prepared through both covalent and noncovalent interactions, and the complex structure, stability, and digestive properties were further investigated. Raman spectroscopy, UV spectroscopy, 3D fluorescence spectroscopy, free sulfhydryl groups, and SEM were employed, and the results showed a synergistic transformation in the SPI structure upon enzymatic hydrolysis and PT addition, which was manifested by the exposure of aromatic amino acids, the formation of intermolecular disulfide bonds, the decrease in surface free sulfhydryl groups (1.04 μmol/g) and an increased in microscopic network structure. The SPIH-PT covalent complexes (CHP) displayed excellent stability in pH, ionic, thermal (73.79 °C), storage (0.55) and freeze-thaw outperforming non-covalent complexes. In vitro gastrointestinal simulated digestion reduced the complexes particle size. The particle size of the digested product increased with increasing PT concentration (increased to 359.70 nm). FTIR of the digested products revealed gradual increase in β-turn and β-sheet content to 34.50% and 19.80%. Enzymatic hydrolysis and polyphenol covalent complexation effectively enhanced the antidigestive properties of the complexes (as low as 19.03%), increased the free amino acid content, improved the antioxidant capacity, and elevated the polyphenol bioaccessibility (up to 88.87%). This work will offer theoretical references to research on the stability and digestion mechanisms of protein hydrolysate-PT complexes, and provide data support for its application in functional foods.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"166 ","pages":"Article 111276"},"PeriodicalIF":11.0000,"publicationDate":"2025-02-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Food Hydrocolloids","FirstCategoryId":"97","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0268005X2500236X","RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"CHEMISTRY, APPLIED","Score":null,"Total":0}

引用次数: 0

Abstract

The dense structure of soy protein isolate (SPI) usually leads to reduced stability and digestibility, limiting its practical application. Protease hydrolysis and polyphenol complexation are considered green means to modify the protein to improve its properties. The study aimed to address the persistent challenges associated with the stability and digestibility of SPI through dual modification of enzymatic hydrolysis and polyphenol. Complexes of varying concentrations of phlorotannins (0, 0.2, 0.5, 1.0, 2.0 mg/mL) with SPI and SPI hydrolysate (SPIH) were prepared through both covalent and noncovalent interactions, and the complex structure, stability, and digestive properties were further investigated. Raman spectroscopy, UV spectroscopy, 3D fluorescence spectroscopy, free sulfhydryl groups, and SEM were employed, and the results showed a synergistic transformation in the SPI structure upon enzymatic hydrolysis and PT addition, which was manifested by the exposure of aromatic amino acids, the formation of intermolecular disulfide bonds, the decrease in surface free sulfhydryl groups (1.04 μmol/g) and an increased in microscopic network structure. The SPIH-PT covalent complexes (CHP) displayed excellent stability in pH, ionic, thermal (73.79 °C), storage (0.55) and freeze-thaw outperforming non-covalent complexes. In vitro gastrointestinal simulated digestion reduced the complexes particle size. The particle size of the digested product increased with increasing PT concentration (increased to 359.70 nm). FTIR of the digested products revealed gradual increase in β-turn and β-sheet content to 34.50% and 19.80%. Enzymatic hydrolysis and polyphenol covalent complexation effectively enhanced the antidigestive properties of the complexes (as low as 19.03%), increased the free amino acid content, improved the antioxidant capacity, and elevated the polyphenol bioaccessibility (up to 88.87%). This work will offer theoretical references to research on the stability and digestion mechanisms of protein hydrolysate-PT complexes, and provide data support for its application in functional foods.

Abstract Image

查看原文本刊更多论文

求助全文

约1分钟内获得全文求助全文

来源期刊

Food Hydrocolloids 工程技术-食品科技

CiteScore

19.90

自引率

14.00%

发文量

871

审稿时长

37 days

期刊介绍： Food Hydrocolloids publishes original and innovative research focused on the characterization, functional properties, and applications of hydrocolloid materials used in food products. These hydrocolloids, defined as polysaccharides and proteins of commercial importance, are added to control aspects such as texture, stability, rheology, and sensory properties. The research's primary emphasis should be on the hydrocolloids themselves, with thorough descriptions of their source, nature, and physicochemical characteristics. Manuscripts are expected to clearly outline specific aims and objectives, include a fundamental discussion of research findings at the molecular level, and address the significance of the results. Studies on hydrocolloids in complex formulations should concentrate on their overall properties and mechanisms of action, while simple formulation development studies may not be considered for publication. The main areas of interest are: -Chemical and physicochemical characterisation Thermal properties including glass transitions and conformational changes- Rheological properties including viscosity, viscoelastic properties and gelation behaviour- The influence on organoleptic properties- Interfacial properties including stabilisation of dispersions, emulsions and foams- Film forming properties with application to edible films and active packaging- Encapsulation and controlled release of active compounds- The influence on health including their role as dietary fibre- Manipulation of hydrocolloid structure and functionality through chemical, biochemical and physical processes- New hydrocolloids and hydrocolloid sources of commercial potential. The Journal also publishes Review articles that provide an overview of the latest developments in topics of specific interest to researchers in this field of activity.