{"title":"从微尺度线形蛋白质组件衍生的中尺度分形乳清蛋白颗粒(第2部分):发泡特性和热稳定性。","authors":"Hanyu Shi, Haotian Zheng","doi":"10.3168/jds.2025-27190","DOIUrl":null,"url":null,"abstract":"<p><p>This study investigates the functionality of mesoscale whey protein particles (WPP) derived from fiber- and ribbon-shaped whey protein assemblies produced via a liquid antisolvent precipitation-based method. The air-water (A-W) interfacial characteristics, foaming properties, and heat stability of WPP were evaluated and compared with the original whey protein source, whey protein isolate (WPI). Adsorption dynamics and dilatational rheology at the A-W interface were characterized using pendant drop and oscillating drop methods, respectively. Foamability and foam stability were assessed using a dynamic foam analyzer, and heat stability was evaluated by examining changes in particle size distribution (PSD) profiles and turbidity before and after heat treatment at 95°C for 5 min. Whey protein particles achieved a quasi-equilibrium surface pressure comparable to WPI after 3 h of adsorption but showed lower dilatational elastic moduli during dilatational deformation. Although WPI exhibited faster surface adsorption, no significant difference was observed in the rate constant of penetration (k<sub>p</sub>) between WPP and WPI. Compared with WPI, reconstituted freeze-dried WPP dispersions did not improve foamability, likely due to slower A-W interface adsorption associated with their larger particle sizes; however, they demonstrated enhanced foam stability, evidenced by a longer 75%-volume lifetime. This improvement is likely attributed to the entrapment of WPP within the lamellae and Plateau borders of foam structure, which may increase local viscosity and block the liquid drainage channels, thereby retarding foam collapse. Moreover, WPP exhibited minimal changes in their PSD and turbidity after heat treatment, suggesting enhanced heat stability relative to WPI.</p>","PeriodicalId":354,"journal":{"name":"Journal of Dairy Science","volume":" ","pages":""},"PeriodicalIF":4.4000,"publicationDate":"2025-10-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Mesoscale fractal whey protein particles derived from microscale linear-shaped protein assemblies (Part 2): Foaming properties and heat stability.\",\"authors\":\"Hanyu Shi, Haotian Zheng\",\"doi\":\"10.3168/jds.2025-27190\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>This study investigates the functionality of mesoscale whey protein particles (WPP) derived from fiber- and ribbon-shaped whey protein assemblies produced via a liquid antisolvent precipitation-based method. The air-water (A-W) interfacial characteristics, foaming properties, and heat stability of WPP were evaluated and compared with the original whey protein source, whey protein isolate (WPI). Adsorption dynamics and dilatational rheology at the A-W interface were characterized using pendant drop and oscillating drop methods, respectively. Foamability and foam stability were assessed using a dynamic foam analyzer, and heat stability was evaluated by examining changes in particle size distribution (PSD) profiles and turbidity before and after heat treatment at 95°C for 5 min. Whey protein particles achieved a quasi-equilibrium surface pressure comparable to WPI after 3 h of adsorption but showed lower dilatational elastic moduli during dilatational deformation. Although WPI exhibited faster surface adsorption, no significant difference was observed in the rate constant of penetration (k<sub>p</sub>) between WPP and WPI. Compared with WPI, reconstituted freeze-dried WPP dispersions did not improve foamability, likely due to slower A-W interface adsorption associated with their larger particle sizes; however, they demonstrated enhanced foam stability, evidenced by a longer 75%-volume lifetime. This improvement is likely attributed to the entrapment of WPP within the lamellae and Plateau borders of foam structure, which may increase local viscosity and block the liquid drainage channels, thereby retarding foam collapse. Moreover, WPP exhibited minimal changes in their PSD and turbidity after heat treatment, suggesting enhanced heat stability relative to WPI.</p>\",\"PeriodicalId\":354,\"journal\":{\"name\":\"Journal of Dairy Science\",\"volume\":\" \",\"pages\":\"\"},\"PeriodicalIF\":4.4000,\"publicationDate\":\"2025-10-09\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of Dairy Science\",\"FirstCategoryId\":\"97\",\"ListUrlMain\":\"https://doi.org/10.3168/jds.2025-27190\",\"RegionNum\":1,\"RegionCategory\":\"农林科学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"AGRICULTURE, DAIRY & ANIMAL SCIENCE\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of Dairy Science","FirstCategoryId":"97","ListUrlMain":"https://doi.org/10.3168/jds.2025-27190","RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"AGRICULTURE, DAIRY & ANIMAL SCIENCE","Score":null,"Total":0}
引用次数: 0
摘要
本研究研究了中尺度乳清蛋白颗粒(WPP)的功能,这些颗粒是通过基于液体抗溶剂沉淀法生产的纤维和带状乳清蛋白组合而成的。评价了乳清分离蛋白(whey protein isolate, WPI)与WPP的空气-水(A-W)界面特性、发泡性能和热稳定性。采用垂滴法和振荡滴法分别表征了水-水界面的吸附动力学和膨胀流变性。泡沫性和泡沫稳定性通过动态泡沫分析仪进行评估,热稳定性通过检测95°C 5分钟热处理前后颗粒尺寸分布(PSD)曲线和浊度的变化进行评估。乳清蛋白颗粒在吸附3 h后达到了与WPI相当的准平衡表面压力,但在膨胀变形过程中表现出较低的膨胀弹性模量。虽然WPI表现出更快的表面吸附,但WPP和WPI在渗透速率常数(kp)上没有显著差异。与WPI相比,重组的冷冻干燥WPP分散体并没有改善起泡性能,这可能是由于它们的粒径较大,A-W界面吸附速度较慢;然而,它们表现出增强的泡沫稳定性,证明了75%体积寿命的延长。这种改善可能是由于WPP在泡沫结构的片层和高原边界内被截留,从而增加了局部粘度,阻塞了液体排水通道,从而延缓了泡沫的崩塌。此外,热处理后WPP的PSD和浊度变化最小,表明相对于WPI,热稳定性增强。
Mesoscale fractal whey protein particles derived from microscale linear-shaped protein assemblies (Part 2): Foaming properties and heat stability.
This study investigates the functionality of mesoscale whey protein particles (WPP) derived from fiber- and ribbon-shaped whey protein assemblies produced via a liquid antisolvent precipitation-based method. The air-water (A-W) interfacial characteristics, foaming properties, and heat stability of WPP were evaluated and compared with the original whey protein source, whey protein isolate (WPI). Adsorption dynamics and dilatational rheology at the A-W interface were characterized using pendant drop and oscillating drop methods, respectively. Foamability and foam stability were assessed using a dynamic foam analyzer, and heat stability was evaluated by examining changes in particle size distribution (PSD) profiles and turbidity before and after heat treatment at 95°C for 5 min. Whey protein particles achieved a quasi-equilibrium surface pressure comparable to WPI after 3 h of adsorption but showed lower dilatational elastic moduli during dilatational deformation. Although WPI exhibited faster surface adsorption, no significant difference was observed in the rate constant of penetration (kp) between WPP and WPI. Compared with WPI, reconstituted freeze-dried WPP dispersions did not improve foamability, likely due to slower A-W interface adsorption associated with their larger particle sizes; however, they demonstrated enhanced foam stability, evidenced by a longer 75%-volume lifetime. This improvement is likely attributed to the entrapment of WPP within the lamellae and Plateau borders of foam structure, which may increase local viscosity and block the liquid drainage channels, thereby retarding foam collapse. Moreover, WPP exhibited minimal changes in their PSD and turbidity after heat treatment, suggesting enhanced heat stability relative to WPI.
期刊介绍:
The official journal of the American Dairy Science Association®, Journal of Dairy Science® (JDS) is the leading peer-reviewed general dairy research journal in the world. JDS readers represent education, industry, and government agencies in more than 70 countries with interests in biochemistry, breeding, economics, engineering, environment, food science, genetics, microbiology, nutrition, pathology, physiology, processing, public health, quality assurance, and sanitation.