{"title":"Comparing coagulation behaviour of reassembled and native casein micelles during renneting, acid gelation and gastric clotting","authors":"Renske Bouma, Etske Bijl, Abigail Thiel, Kasper Hettinga","doi":"10.1016/j.foodhyd.2025.111441","DOIUrl":null,"url":null,"abstract":"<div><div>Casein micelles are important structuring elements in dairy products due to their coagulation properties during both manufacture and digestion. A possible approach to high-quality dairy alternatives is therefore the assembly of recombinant casein into casein micelles. However, to effectively assemble caseins produced by precision fermentation in functional casein micelles, we first need to understand how the coagulation properties of bovine casein micelles assembled in-vitro might differ from native casein micelles. The aim of this study was therefore to compare the coagulation behaviour of bovine reassembled casein micelles (RCM) to native casein micelles (NCM) during renneting, acid gelation and gastric clotting. Assembly of bovine caseins led to RCM that were able to coagulate in all three conditions. Coagulation behaviour of RCM differed from NCM, forming stronger rennet gels (G′ 82 ± 7 Pa vs 34 ± 12 Pa) and weaker acid gels (G’ 0.7 ± 0.2 Pa vs 3.0 ± 1.3 Pa) than NCM. Gastric clotting behaviour was surprisingly similar. RCM were smaller (120 ± 3 nm vs 157 ± 4 nm), more hydrated (3.89 ± 0.04 g/g vs 2.61 ± 0.07 g/g) and less mineralized (14.8 ± 0.2 mM Ca vs 18.7 ± 1.7 mM Ca) than NCM, which may explain the differences in coagulation behaviour. These results showed that assembly leads to functional casein micelles, with differences in coagulation behaviour relatable to micellar properties. These learnings can inform casein micelle assembly of recombinant casein, as basis for high-quality dairy alternatives.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"168 ","pages":"Article 111441"},"PeriodicalIF":11.0000,"publicationDate":"2025-04-10","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/S0268005X25004011","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
Casein micelles are important structuring elements in dairy products due to their coagulation properties during both manufacture and digestion. A possible approach to high-quality dairy alternatives is therefore the assembly of recombinant casein into casein micelles. However, to effectively assemble caseins produced by precision fermentation in functional casein micelles, we first need to understand how the coagulation properties of bovine casein micelles assembled in-vitro might differ from native casein micelles. The aim of this study was therefore to compare the coagulation behaviour of bovine reassembled casein micelles (RCM) to native casein micelles (NCM) during renneting, acid gelation and gastric clotting. Assembly of bovine caseins led to RCM that were able to coagulate in all three conditions. Coagulation behaviour of RCM differed from NCM, forming stronger rennet gels (G′ 82 ± 7 Pa vs 34 ± 12 Pa) and weaker acid gels (G’ 0.7 ± 0.2 Pa vs 3.0 ± 1.3 Pa) than NCM. Gastric clotting behaviour was surprisingly similar. RCM were smaller (120 ± 3 nm vs 157 ± 4 nm), more hydrated (3.89 ± 0.04 g/g vs 2.61 ± 0.07 g/g) and less mineralized (14.8 ± 0.2 mM Ca vs 18.7 ± 1.7 mM Ca) than NCM, which may explain the differences in coagulation behaviour. These results showed that assembly leads to functional casein micelles, with differences in coagulation behaviour relatable to micellar properties. These learnings can inform casein micelle assembly of recombinant casein, as basis for high-quality dairy alternatives.
酪蛋白胶束由于其在生产和消化过程中的凝固特性而成为乳制品中重要的结构元素。因此,一种可能的方法是将重组酪蛋白组装成酪蛋白胶束。然而,为了在功能性酪蛋白胶束中有效地组装精确发酵产生的酪蛋白,我们首先需要了解体外组装的牛酪蛋白胶束与天然酪蛋白胶束的凝血特性有何不同。因此,本研究的目的是比较牛重组酪蛋白胶束(RCM)和天然酪蛋白胶束(NCM)在凝血、酸凝胶和胃凝血过程中的凝血行为。牛酪蛋白的组装导致在所有三种条件下都能够凝固的RCM。RCM的凝血行为与NCM不同,形成较强的凝血酶凝胶(G′82±7 Pa vs 34±12 Pa)和较弱的酸性凝胶(G′0.7±0.2 Pa vs 3.0±1.3 Pa)。胃凝血行为惊人地相似。RCM比NCM更小(120±3 nm vs 157±4 nm),更水化(3.89±0.04 g/g vs 2.61±0.07 g/g),更少矿化(14.8±0.2 mM Ca vs 18.7±1.7 mM Ca),这可能解释了凝血行为的差异。这些结果表明,组装导致功能性酪蛋白胶束,与胶束性质相关的凝血行为的差异。这些研究成果可以为重组酪蛋白胶束组装提供信息,作为高质量乳制品替代品的基础。
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.