摘要
蛋黄是一个由多样化蛋白质组成的复杂的超分子结构体系,具有丰富的营养价值和突出的功能特性。冷冻保藏是工业上常用的延长蛋黄保质期、提高运输便捷性的有效方式。但在低温条件下,蛋黄内部的蛋白质会发生聚集,导致蛋黄凝胶化,从而出现流动性降低、溶解性下降等问题,影响其功能特性,不利于其在食品加工中的应用。本文介绍蛋黄的组成结构、功能特性,以及蛋黄冷冻原因和蛋黄凝胶化的形成机制,论述蛋黄的冷冻凝胶化对蛋黄品质的影响,重点阐述采用物理、化学和生物等方法对蛋黄进行预处理,抑制冷冻过程中蛋白质的聚集,对抑制蛋黄冷冻凝胶化的产生、改善冷冻蛋黄的品质具有指导意义。
Egg yolk is a complex supramolecular system composed of diverse proteins with high nutritional value and outstanding functional characteristics.Cryopreservation is commonly used in the food industry as an effective way to prolong egg yolk shelf life and improve transportation convenience.However,low temperature induces the aggregation of protein in egg yolk,resulting in egg yolk gelation and consequently reduced fluidity and solubility,affecting the functional properties of egg yolk,which are not conducive to the application of egg yolk in food processing.This article introduces the composition,structure and functional characteristics of egg yolk as well as the causes of egg yolk freezing and the mechanism of egg yolk gelation,and discusses the effect of egg yolk gelation induced by freezing on egg yolk quality.This review focuses on the physical,chemical and biological pretreatments for inhibiting protein aggregation during egg yolk,which is of guiding significance for inhibiting egg yolk gelation induced by freezing and for improving the quality of frozen egg yolk.
作者
杨田
李凤红
李鑫
董世建
李述刚
黄群
何雨
YANG Tian;LI Fenghong;LI Xin;DONG Shijian;LI Shugang;HUANG Qun;HE Yu(Guizhou Province Engineering Research Center of Health Food Innovative Manufacturing,School of Public Health,Guizhou Medical University,Guiyang 550025,China;Anhui Rongda Food Co.Ltd.,Xuancheng 242200,China;School of Food and Biological Engineering,Hefei University of Technology,Hefei 230009,China)
出处
《食品科学》
EI
CAS
CSCD
北大核心
2024年第21期39-47,共9页
Food Science
基金
“十四五”国家重点研发计划重点专项(2022YFD2101001)
国家自然科学基金地区科学基金项目(32260597,32360552)
现代农业产业技术体系建设专项(CARS-40-K25)
贵州省自然科学基金重点项目(KY[2022]036)
贵州省自然科学基金一般项目(ZK[2022]360,ZK[2022]348)。
关键词
蛋黄
冷冻凝胶化
品质劣变
蛋白质聚集
抑制方法
egg yolk
freezing-induced gelation
quality deterioration
protein aggregation
inhibition methods