Impacts of N-(n-Butyl)thiophosphoric triamide (NBPT) on the physicochemical properties of milk protein isolate (MPI) dispersions: A study on micelle integrity

IF 5.6 3区农林科学 Q1 FOOD SCIENCE & TECHNOLOGY

Food Structure-Netherlands Pub Date : 2025-04-01 DOI:10.1016/j.foostr.2025.100423

Maria P. Byrne , Patrick J. Forrestal , Tom F. O’ Callaghan , Niharika Rahman , Aishwarya Ray , Martin Danaher , Bernard M. Corrigan , Noel A. McCarthy , Chikere G. Nkwonta , Karl Richards , Farhad Garavand , Enda Cummins , Sean A. Hogan

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Abstract

This study investigated the effects of the urease inhibitor N-(n-Butyl)thiophosphoric triamide (NBPT) on milk protein isolate (MPI) dispersions. The addition of NBPT to MPI led to significant (p < 0.05) reductions in particle size (from 154 to 119 nm) and significant (p < 0.05) increases in sample polydispersity index for the MPI control and MPI containing 3 mg/mL NBPT respectively, which is suggestive of micelle dissociation presumably due to the release of calcium sensitive caseins and the subsequent generation of small protein aggregates. Zeta potential values of MPI became more negative and increased from −26.4 in the MPI control to −44.7 Mv in the presence of 3 mg/mL NBPT. Increased calcium (Ca^2 +) ions in the serum phase of MPI containing NBPT delayed rennet gelation due to slower hydrolysis of kappa-casein, these gels also exhibited increased strength which could be attributed to enhanced Ca²⁺ crosslinking. Acid-induced MPI-NBPT gels displayed delays in gelation time due to altered buffering capacities. NBPT caused significant (p < 0.05) decreases in final surface tension values. NBPT marginally increased the heat stability of MPI. Overall, NBPT significantly impacted the structural and functional properties of MPI dispersions due to the displacement of Ca²⁺ from phosphoserine (SEP) residues in colloidal calcium phosphate (CCP).

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N-（正丁基）硫代磷酸三酰胺（NBPT）对乳分离蛋白（MPI）分散体理化性质的影响：胶束完整性的研究

研究了脲酶抑制剂N-（正丁基）硫磷三酰胺（NBPT）对乳分离蛋白（MPI）分散体的影响。在MPI中加入NBPT后，MPI的颗粒大小显著（p <； 0.05）减小（从154到119 nm）， MPI对照和含有3 mg/mL NBPT的MPI的样品多分散性指数显著（p <； 0.05）增加，这表明胶束解离可能是由于钙敏感酪蛋白的释放和随后产生的小蛋白聚集体。当3 mg/mL NBPT存在时，MPI的Zeta电位值从MPI对照组的- 26.4增加到- 44.7 Mv。含有NBPT的MPI血清相钙（Ca2 +）离子的增加由于kappa-酪蛋白的水解减慢而延迟了凝血酶的凝胶化，这些凝胶也表现出强度的增加，这可能归因于增强的Ca2+交联。酸诱导的MPI-NBPT凝胶由于缓冲能力的改变而显示出凝胶时间的延迟。NBPT导致最终表面张力值显著降低（p <； 0.05）。NBPT略微提高了MPI的热稳定性。总的来说，NBPT显著影响了MPI分散体的结构和功能特性，这是由于在胶体磷酸钙（CCP）中，磷酸丝氨酸（SEP）残基取代了Ca2+。

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来源期刊

Food Structure-Netherlands Chemical Engineering-Bioengineering

CiteScore

7.20

自引率

0.00%

发文量

期刊介绍： Food Structure is the premier international forum devoted to the publication of high-quality original research on food structure. The focus of this journal is on food structure in the context of its relationship with molecular composition, processing and macroscopic properties (e.g., shelf stability, sensory properties, etc.). Manuscripts that only report qualitative findings and micrographs and that lack sound hypothesis-driven, quantitative structure-function research are not accepted. Significance of the research findings for the food science community and/or industry must also be highlighted.