食品科学 ›› 2022, Vol. 43 ›› Issue (1): 119-126.doi: 10.7506/spkx1002-6630-20201130-307

• 食品工程 • 上一篇    

超高压和巴氏杀菌对蛋清蛋白结构及起泡性能的影响

张根生,刘欣慈,岳晓霞,丁一丹,赵陈美慧,勾凤琦,吕云雄   

  1. (1.哈尔滨商业大学食品工程学院,黑龙江 哈尔滨 150028;2.弥勒市朋普镇人民政府,云南 弥勒 652300)
  • 发布日期:2022-01-29
  • 基金资助:
    黑龙江省“百千万”工程科技重大专项(2019ZX07B03)

Comparative Effects of Ultra-high Pressure and Pasteurization on Structure and Foaming Properties of Egg White Protein

ZHANG Gensheng, LIU Xinci, YUE Xiaoxia, DING Yidan, ZHAO Chenmeihui, GOU Fengqi, LÜ Yunxiong   

  1. (1. College of Food Engineering, Harbin University of Commerce, Harbin 150028, China; 2. People’s Government of Pengpu Town, Mile 652300, China )
  • Published:2022-01-29

摘要: 本实验以市售鲜蛋制备得到的蛋清为原料,分别利用巴氏杀菌和超高压杀菌处理(200~300?MPa,2.5~12.5?min),经喷雾干燥后,采用圆二色光谱、傅里叶变换红外光谱、紫外光谱、荧光光谱和动态光散射激光粒度仪等研究超高压杀菌处理对蛋清蛋白的构象、粒径、表面电位、起泡特性的影响。结果表明,巴氏杀菌和超高压杀菌处理均对蛋清蛋白构象产生不可逆改变;随着杀菌压力的增加,α-螺旋和无规卷曲的相对含量增大,β-折叠和β-转角相对含量降低;超高压处理后样品荧光强度低于未处理鲜蛋,随压力的升高和保压时间的延长,总体呈先升高后降低趋势;高压处理能够促使酪氨酸、色氨酸和苯丙氨酸残基暴露,但随着保压时间的延长,暴露的氨基酸残基又会被重新包埋。此外,压力还会诱导蛋清聚集,随着杀菌压力的升高和保压时间的延长,蛋清粒径呈先升高后下降的趋势,且分布均匀;300?MPa下,表面电位、起泡性和泡沫稳定性随着杀菌时间的延长出现了先增强后减弱的趋势,在7.5?min达到最大值;200?MPa及250?MPa下起泡性和泡沫稳定性持续增强。与巴氏杀菌相比,超高压杀菌对二级结构破坏更大,对三级结构破坏较小,有效提高了蛋清多分散系数、表面电位、起泡性和泡沫稳定性。

关键词: 蛋清蛋白质;二级结构;三级结构;超高压杀菌

Abstract: In this study, egg white protein prepared from commercial fresh eggs was subjected to pasteurization or ultra-high pressure (UHP) sterilization (200–300 MPa and 2.5–12.5 min). After spray drying, circular dichroism (CD) spectroscopy, Fourier transform infrared (FT-IR) spectroscopy, ultraviolet (UV) spectroscopy, fluorescence spectroscopy and a dynamic light scattering laser particle size analyzer were employed to characterize the effects of the sterilization treatments on the conformation, particle size, surface potential, and foaming characteristics of egg white protein. The results showed that both pasteurization and ultra-high pressure sterilization irreversibly changed the conformation of egg white protein. The relative contents of α-helix and random coil increased, whereas the relative contents of β-sheet and β-turn decreased with increasing sterilization pressure. After UHP treatment, the fluorescence intensity decreased, and it increased first and then decreased with increasing pressure and dwell time. UHP treatment resulted in the exposure of tyrosine, tryptophan and phenylalanine residues, but the exposed amino acid residues were re-buried inside the protein molecule with increasing dwell time. In addition, high pressure induced the aggregation of egg white protein. The particle size increased first and then decreased with increasing sterilization pressure and holding time, and the particle size distribution became more uniform. At 300 MPa, the surface potential, foaming ability and foam stability increased with increasing sterilization time up to 7.5 min and then decreased. At 200 and 250 MPa, the foam ability and foam stability continuously increased. Compared with pasteurization, ultra-high pressure sterilization caused greater damage to the secondary structure and less damage to the tertiary structure, and effectively improved the polydispersity index, surface potential, foamability and foam stability of egg white protein.

Key words: egg white protein; secondary structure; tertiary structure; ultra-high pressure sterilization

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