{"title":"Fabrication and characterization of industrially stable whey protein nanogels via thermal denaturation and calcium interaction","authors":"","doi":"10.1016/j.foodhyd.2024.110641","DOIUrl":null,"url":null,"abstract":"<div><p>Colloidal nanogels based on whey protein isolate (WPI) hold significant promise for the food industry due to their nutritional value and functional properties. However, fabricating an industrially stable nanogel, particularly at high protein concentrations, has proven challenging. Addressing the need for stable WPI nanogels, this study explored the thermal denaturation of whey protein across a broad range of concentrations (3–11%, w/w on protein basis), paired with varying calcium levels (0–20 mM). It focused on elucidating the controlled aggregation mechanisms and assessing the stability of these nanogels under several common food processing conditions such as blending with food salts, pH adjustment, thermal sterilization, and spray-drying. The results revealed that controlled aggregation of WPI into nanogels primarily occurred through disulfide bond formation when subjected to denaturation with a limited amount of calcium. However, an excess of calcium induced complete aggregation into macroscopic gels. Once formed, these self-assembled nanogels exhibited resilience to a wide pH range (pH3-7). They also demonstrated exceptional stability under typical industrial processing and food formulation conditions, such as simulated milk ultrafiltration (SMUF), and remained stable through ultra-high temperature thermal sterilization (140 °C) and spray drying. In conclusion, this study not only advances our understanding on the mechanisms behind the formation of calcium induced protein denaturation but also provides significant insights into developing stable whey protein nanogels, addressing a crucial need of stable high-protein food products.</p></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":null,"pages":null},"PeriodicalIF":11.0000,"publicationDate":"2024-09-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S0268005X24009159/pdfft?md5=5641ddeb3bd05e7a39c99692f75d6e1d&pid=1-s2.0-S0268005X24009159-main.pdf","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Food Hydrocolloids","FirstCategoryId":"97","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0268005X24009159","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
Colloidal nanogels based on whey protein isolate (WPI) hold significant promise for the food industry due to their nutritional value and functional properties. However, fabricating an industrially stable nanogel, particularly at high protein concentrations, has proven challenging. Addressing the need for stable WPI nanogels, this study explored the thermal denaturation of whey protein across a broad range of concentrations (3–11%, w/w on protein basis), paired with varying calcium levels (0–20 mM). It focused on elucidating the controlled aggregation mechanisms and assessing the stability of these nanogels under several common food processing conditions such as blending with food salts, pH adjustment, thermal sterilization, and spray-drying. The results revealed that controlled aggregation of WPI into nanogels primarily occurred through disulfide bond formation when subjected to denaturation with a limited amount of calcium. However, an excess of calcium induced complete aggregation into macroscopic gels. Once formed, these self-assembled nanogels exhibited resilience to a wide pH range (pH3-7). They also demonstrated exceptional stability under typical industrial processing and food formulation conditions, such as simulated milk ultrafiltration (SMUF), and remained stable through ultra-high temperature thermal sterilization (140 °C) and spray drying. In conclusion, this study not only advances our understanding on the mechanisms behind the formation of calcium induced protein denaturation but also provides significant insights into developing stable whey protein nanogels, addressing a crucial need of stable high-protein food products.
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.