Heat-induced aggregation of β-lactoglobulin AB at pH 2.5 as influenced by ionic strength and protein concentration

被引：95

作者：

Schokker, EP

Singh, H

Pinder, DN

Creamer, LK

机构：

[1] Massey Univ, Inst Food Nutr & Human Hlth, Palmerston North, New Zealand

[2] Massey Univ, Inst Fundamental Sci, Palmerston North, New Zealand

[3] New Zealand Dairy Res Inst, Food Sci Sect, Palmerston North, New Zealand

来源：

INTERNATIONAL DAIRY JOURNAL | 2000年 / 10卷 / 04期

关键词：

heat-induced aggregation; beta-lactoglobulin; low pH;

D O I：

10.1016/S0958-6946(00)00047-9

中图分类号：

TS2 [食品工业];

学科分类号：

0832 ;

摘要：

Heat-induced (80 degrees C) aggregation of beta-lactoglobulin AB at pH 2.5 was studied using size-exclusion chromatography in combination with multi-angle laser light scattering, dynamic light scattering and electrophoretic techniques. Upon heating, large aggregates with molar masses of 10(6)-10(7) Da were formed, whereas the concentration of intermediate-sized aggregates was very low. The rate of disappearance of native-like beta-lactoglobulin increased with increasing protein concentration (reaction order 2) and ionic strength. Aggregate size increased slightly with heating time and ionic strength, but was independent of protein concentration. Aggregates were held together entirely with non-covalent bonding. (C) 2000 Elsevier Science Ltd. All rights reserved.

引用

页码：233 / 240

页数：8

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