Effect of pectin adsorption on the hydrophobic binding sites of β-lactoglobulin in solution and in emulsion systems

被引：20

作者：

Benjamin, O. ^{[1
,2
]}

Lasse, M. ^{[1
,3
]}

Silcock, P. ^{[2
]}

Everett, D. W. ^{[1
,2
]}

机构：

[1] Riddet Inst, Palmerston North, New Zealand

[2] Univ Otago, Dept Food Sci, Dunedin, New Zealand

[3] Univ Canterbury, Sch Biol Sci, Christchurch 1, New Zealand

来源：

INTERNATIONAL DAIRY JOURNAL | 2012年 / 26卷 / 01期

关键词：

MOLTEN GLOBULE STATE; IN-WATER EMULSIONS; AROMA COMPOUNDS; SURFACE HYDROPHOBICITY; MULTILAYER EMULSIONS; STRUCTURAL-CHANGES; HIGH-PRESSURE; PH; PROTEINS; HEAT;

D O I：

10.1016/j.idairyj.2011.12.007

中图分类号：

TS2 [食品工业];

学科分类号：

0832 ;

摘要：

The impact of high methoxyl pectin adsorption on beta-lactoglobulin (beta LG) conformation in solution and at the interface of an oil-in-water emulsion was investigated using 6-propionyl-2-(dimethylamino) naphthalene and retinol probes to monitor beta LG binding availability for hydrophobic compounds. The effects of pH (2.0-9.0) and ionic strength of NaCl (0-330 mM) and CaCl2 (0-1 M) were also examined. An increase in surface hydrophobicity (S-0) and retinol binding was observed for pH above 7 where the protein had a more flexible and open conformation. Pectin attachment to beta LG at pH 4 had a significant impact on S-0 due to protein unfolding, confirmed by differential scanning calorimetry. Retinol binding was not affected in the closed calyx structure of beta LG. Similar behaviour occurred for multilayer emulsions. The addition of salts caused a reduction in S-0 and retinol binding as the protein underwent partial aggregation in solution and at the interface of the primary emulsion. (C) 2012 Elsevier Ltd. All rights reserved.

引用

页码：36 / 40

页数：5

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