丝素
再结晶(地质)
丝绸
材料科学
冰晶
化学工程
化学
生物物理学
复合材料
地质学
光学
生物
岩石学
工程类
物理
作者
Yong Xie,Mingzhu Wang,Xiaoyan Liu,Kai Zhou,Zhaoming Wang,Feiran Xu,Hui Zhou,Haimei Hu,Baocai Xu
标识
DOI:10.1021/acs.jafc.4c06306
摘要
Effectively controlling ice recrystallization (IR) during the frozen storage of food remains highly challenging. Inspired by the structural characteristics of antifreeze proteins in nature, silk fibroin (SF) derived from silk fibers has been developed. Through dual validation using the "splat" assay and "sucrose sandwich" assay, the IR inhibition activity of SF at various concentrations was confirmed, revealing that its regular alternating hydrophilic/hydrophobic domains endow SF with the potential to inhibit the axial growth of single ice crystal and significantly reduce the average maximum crystal size by approximately 67%. Additionally, the quality stability of frozen muscle foods treated with SF was comprehensively evaluated. In stark contrast to traditional commercial antifreeze agents (4% sucrose and 4% sorbitol), prepared steaks with the addition of 2% SF maintained rich juiciness and excellent color acceptability over a three-month frozen storage period. Thus, SF holds promise as a potential protective agent for frozen muscle foods, enhancing their quality during storage.
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