Re-formation of Fibrils from Hydrolysates of β-Lactoglobulin Fibrils during in Vitro Gastric Digestion

被引：39

作者：

Bateman, Libei ^{[1
]}

Ye, Aiqian ^{[1
]}

Singh, Harjinder ^{[1
]}

机构：

[1] Massey Univ, Riddet Inst, Palmerston North 4442, New Zealand

来源：

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY | 2011年 / 59卷 / 17期

关键词：

beta-Lactoglobulin; fibrils; in vitro pepsin digestion; re-formation; PERCOLATION CONCENTRATION; INDUCED AGGREGATION; WHEY-PROTEIN; PEPTIDES; FOOD; GELS; PH; GELATION; IDENTIFICATION; PRESSURE;

D O I：

10.1021/jf2020057

中图分类号：

S [农业科学];

学科分类号：

09 ;

摘要：

In this study, in vitro digestion of beta-lactoglobulin (beta-Lg) fibrils and the re-formation of fibril-like structures after prolonged enzymatic hydrolysis (up to 48 h) were investigated using matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS), thioflavin T fluorescence photometry, and transmission electron microscopy (TEM). Pure beta-Lg fibrils that had been formed by heat treatment at pH 2.0 were rapidly hydrolyzed by pepsin in the simulated gastric fluid (pH 1.2), and some new peptides that were suitable for further fibril formation were produced. TEM showed that the new fibrils were long and straight but thinner than the original fibrils, and both TEM and MALDI-MS indicated that the peptides in the new fibrils were shorter/smaller than the peptides in the original fibrils. The formation of new fibrils was found to be affected more by pH than by enzyme activity or temperature.

引用

页码：9605 / 9611

页数：7

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