Caseinomacropeptide modifies the heat-induced denaturatione-aggregation process of β-lactoglobulin

被引：18

作者：

Croguennec, Thomas ^{[1
,2
,3
]}

Leng, Ning ^{[1
,2
,3
]}

Hamon, Pascaline ^{[1
,2
]}

Rousseau, Florence ^{[1
,2
]}

Jeantet, Romain ^{[1
,2
,3
]}

Bouhallab, Said ^{[1
,2
]}

机构：

[1] Agrocampus Ouest, STLO, UMR1253, F-35042 Rennes, France

[2] INRA, STLO, UMR1253, F-35042 Rennes, France

[3] Univ Europeenne Bretagne, Rennes, France

来源：

INTERNATIONAL DAIRY JOURNAL | 2014年 / 36卷 / 01期

关键词：

WHEY PROTEINS; KAPPA-CASEIN; IONIC-STRENGTH; PH; GELATION; CHROMATOGRAPHY; PEPTIDES; KINETICS;

D O I：

10.1016/j.idairyj.2014.01.004

中图分类号：

TS2 [食品工业];

学科分类号：

0832 ;

摘要：

The effect of caseinomacropeptide (CMP) concentration on the kinetics of denaturation of beta-lactoglobulin (beta-Lg) and on the size and structure of the heat-induced aggregates was investigated over a wide range of pH (3.0-6.7) and temperature (65-95 degrees C). Irrespective of pH and heating temperature, CMP increased the rate of beta-Lg denaturation. When beta-Lg and CMP were negatively charged (i.e., at pH 6.7), increasing CMP concentration hindered aggregate formation; the aggregates had a smaller hydrodynamic diameter and the protein solution turbidity decreased. However, when beta-Lg and CMP were oppositely charged (i.e., at pH 4.0), CMP promoted aggregate formation and large particles (>5 mu m) were formed on heating. Nevertheless, the covalent aggregates constituting these large particles were of smaller size than those formed on heating beta-Lg in the absence of CMP. At pH 4.0, CMP induced the formation of large particles when added in a solution of preformed aggregates of beta-Lg. (C) 2014 Elsevier Ltd. All rights reserved.

引用

页码：55 / 64

页数：10

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