Susceptibility of lysozyme to in-vitro digestion and immunoreactivity of its digests

被引：47

作者：

Jimenez-Saiz, R. ^{[1
]}

Martos, G. ^{[1
]}

Carrillo, W. ^{[1
]}

Lopez-Fandino, R. ^{[1
]}

Molina, E. ^{[1
]}

机构：

[1] Univ Autonoma Madrid, Inst Invest Ciencias Alimentac, CIAL, CSIC UAM, E-28049 Madrid, Spain

来源：

FOOD CHEMISTRY | 2011年 / 127卷 / 04期

关键词：

Lysozyme; alpha-Lactalbumin; In-vitro gastric digestion; In-vitro duodenal digestion; IgE-binding; EGG-WHITE LYSOZYME; ALPHA-LACTALBUMIN; MAJOR ALLERGEN; FOOD ALLERGENS; MILK; PROTEOLYSIS; ABSORPTION; STABILITY; PROTEINS; BEHAVIOR;

D O I：

10.1016/j.foodchem.2011.02.047

中图分类号：

O69 [应用化学];

学科分类号：

081704 ;

摘要：

This paper examines lysozyme (LYS) behaviour upon in-vitro digestion, mimicking different conditions in the stomach and intestine, and assessing the effect of natural surfactants, such as phosphatidylcholine (PC) or bile salts (BS), on hydrolysis and residual immunogenicity of the digests. The hydrolysis pattern of LYS was compared to that of alpha-lactalbumin (LA). Hydrolysis of LYS only occurred at low pH. PC slightly increased its resistance to pepsinolysis. A similar behaviour was found for LA. Circular dichroism revealed that the more rigid structure of LYS, as compared with that of LA, could protect it from proteolysis at acidic pH and fluorescence spectra suggested that, at acidic pH, both proteins associated to PC films. The gastric digests of LYS showed high IgE-binding capacity using sera from egg-allergic patients. On the other hand, it was found that LYS precipitated under conditions that simulated a duodenal environment, mainly due to the presence of BS. Published by Elsevier Ltd.

引用

页码：1719 / 1726

页数：8

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