The complexity of protein haze formation in wines

被引:54
作者
Batista, Luis [1 ]
Monteiro, Sara [1 ,2 ]
Loureiro, Virgilio B. [1 ]
Teixeira, Artur R. [1 ]
Ferreira, Ricardo B. [1 ,2 ]
机构
[1] Univ Tecn Lisboa, Inst Super Agron, Dept Bot & Engn Biol, P-1349017 Lisbon, Portugal
[2] Univ Nova Lisboa, Inst Tecnol Quim & Biol, Dis & Stress Biol Lab, P-2781901 Oeiras, Portugal
关键词
wine proteins; haze; turbidity; pH; X factor; BOTRYTIS-CINEREA INFECTION; HEAT-UNSTABLE PROTEINS; WHITE WINE; FOAMING PROPERTIES; POLYPHENOL HAZE; GRAPE JUICE; GLYCOPROTEINS; RESISTANCE; STABILITY; REMOVAL;
D O I
10.1016/j.foodchem.2008.05.070
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
The mechanism responsible for protein haze formation in wines remains essentially to be elucidated. Current knowledge suggests the absolute requirement of one or more as yet unknown non-proteinaceous wine components (termed the X factor) for protein precipitation in wines. Using the single grape variety Arinto wine, naturally containing 280 mg protein/l, a series of heat stability tests were performed over a range of wine-relevant pH values (from 2.8 to 3.8). The results obtained indicate the existence of at least two different mechanisms responsible for the heat-induced precipitation of the Arinto wine proteins: one occurring only at the higher pH values, that appears to result from isoelectric precipitation of the proteins; another prevailing at the lower pH values, but possibly operating also at other pH values, that depends on the presence of the X factor. Therefore, conclusive evidence is provided for the existence of the X factor, here defined as one or more low molecular mass wine components that sensitise proteins for heat-induced denaturation at low wine pH values and whose presence is a pre-requisite for the precipitation of proteins in wines under these circumstances. The chemical nature of protein aggregation was further analysed as a function of pH. Neither of the two proposed mechanisms responsible for the heat-induced precipitation of the wine proteins is electrostatic in nature, lectin-mediated or divalent cation-dependent. Both mechanisms show minimum turbidity at pH 7, but increased turbidity towards lower and higher pH values. (c) 2008 Elsevier Ltd. All rights reserved.
引用
收藏
页码:169 / 177
页数:9
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