Tuning the properties of β-lactoglobulin nanofibrils with pH, NaCl and CaCl2

被引：109

作者：

Loveday, S. M. ^{[1
]}

Wang, X. L. ^{[1
]}

Rao, M. A. ^{[2
]}

Anema, S. G. ^{[3
]}

Creamer, L. K. ^{[1
]}

Singh, H. ^{[1
]}

机构：

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

[2] Cornell Univ, Dept Food Sci & Technol, Geneva, NY 14456 USA

[3] Fonterra Res Ctr, Palmerston North, New Zealand

来源：

INTERNATIONAL DAIRY JOURNAL | 2010年 / 20卷 / 09期

关键词：

HEAT-INDUCED GELATION; FIBRIL FORMATION; AMYLOID FIBRILS; WHEY-PROTEIN; GLOBULAR-PROTEINS; IONIC-STRENGTH; AGGREGATION; KINETICS; GELS; BETA(2)-MICROGLOBULIN;

D O I：

10.1016/j.idairyj.2010.02.014

中图分类号：

TS2 [食品工业];

学科分类号：

0832 ;

摘要：

We investigated the effects of pH (1.6-2.4), NaCl and CaCl2 (0-100 mM) on the kinetics of beta-lactoglobulin fibril formation during heating at 80 degrees C. The morphology of fibrils was also examined. At pH 1.8-2.4 fibril formation occurred slightly faster with decreasing pH. At pH 1.6 fibril formation during the growth phase occurred much faster than at any other pH. Fibril morphology was unchanged between pH 1.6 and pH 2.0. Addition of NaCl or CaCl2 accelerated fibril formation during the growth phase, and CaCl2 shortened the lag phase as well. Worm-like fibrils were seen at >= 60 mm NaCl or >= 33 mm CaCl2, and these had a persistence length which was much shorter than the long semi-flexible fibrils formed without salts. The efficiency of fibril formation can be substantially enhanced by varying pH and salt concentration. (c) 2010 Elsevier Ltd. All rights reserved.

引用

页码：571 / 579

页数：9

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