Phosphate salt-induced structure formation in casein suspensions

IF 11 1区农林科学 Q1 CHEMISTRY, APPLIED

Food Hydrocolloids Pub Date : 2025-04-25 DOI:10.1016/j.foodhyd.2025.111488

Ipek Altay , Liesbeth van der Meulen , Paul J. Kempen , Jens J. Sloth , Mohammad Amin Mohammadifar , Thom Huppertz

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Abstract

The influence of 0.6–1.0 mEq/g casein of the phosphate-based calcium sequestering salts (CSS) pyrophosphate (PP), orthophosphate, and polyphosphates, on the properties of micellar casein isolate (MCI) and sodium (NaCas) and calcium (CaCas) caseinate suspensions containing 5–10 % casein was evaluated at 20 and 40 °C at pH 6.0–7.4. Structural characterizations included measurement of viscosity measurements and NMR transverse relaxation time (T₂) and cryo-TEM. Overall, viscosity increased with increasing casein concentration, PP level, and pH. The highest viscosity for MCI was observed at 1.0 mEq PP/g casein. The polyphosphates sodium tripolyphosphate and sodium hexametaphosphate had far less effect on MCI viscosity. PP addition did not notably affect the viscosity of NaCas suspensions, indicating that calcium may contribute strongly to PP-induced increases in the viscosity of casein systems. The combined effect of temperature and pH significantly influenced the viscosity of MCI-5 % and CaCas suspensions, especially at higher CSS concentrations. NMRand cryo-TEM analyses supported these findings, revealing weaker structures in NaCas and PP-induced crosslinks or dense networks depending on pH, correlating with viscosity changes. This investigation provides valuable insights into casein-CSS interactions, with potential benefits for dairy processing and optimization.

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磷酸盐诱导酪蛋白悬浮液的结构形成

在20°C和40°C、pH 6.0-7.4条件下，考察了磷酸基钙螯合盐（CSS）焦磷酸盐（PP）、正磷酸盐和多磷酸盐中0.6-1.0 mEq/g酪蛋白对胶束酪蛋白分离物（MCI）和含有5 - 10%酪蛋白的酪蛋白酸钠（NaCas）和钙（CaCas）酪蛋白酸悬浮液性能的影响。结构表征包括粘度测量、核磁共振横向弛豫时间（T2）和低温透射电镜。总体而言，黏度随着酪蛋白浓度、PP水平和ph的增加而增加。在1.0 mEq PP/g酪蛋白时，MCI的黏度最高。三聚磷酸钠和六偏磷酸钠对MCI粘度的影响较小。PP的加入对NaCas悬浮液的粘度没有显著影响，这表明钙可能对PP诱导的酪蛋白体系粘度的增加有很大的影响。温度和pH的联合作用显著影响mci - 5%和CaCas悬浮液的粘度，特别是在较高的CSS浓度下。核磁共振和低温透射电镜分析支持了这些发现，揭示了NaCas和pp诱导的交联或致密网络中较弱的结构取决于pH值，与粘度变化相关。这项研究为酪蛋白- css相互作用提供了有价值的见解，对乳制品加工和优化具有潜在的好处。

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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.