Marangon Matteo, Van Sluyter Steven C, Waters Elizabeth J, Menz Robert I
The Australian Wine Research Institute, Adelaide, South Australia, Australia.
The Australian Wine Research Institute, Adelaide, South Australia, Australia; School of Botany, University of Melbourne, Victoria, Australia.
PLoS One. 2014 Dec 2;9(12):e113757. doi: 10.1371/journal.pone.0113757. eCollection 2014.
Grape thaumatin-like proteins (TLPs) play roles in plant-pathogen interactions and can cause protein haze in white wine unless removed prior to bottling. Different isoforms of TLPs have different hazing potential and aggregation behavior. Here we present the elucidation of the molecular structures of three grape TLPs that display different hazing potential. The three TLPs have very similar structures despite belonging to two different classes (F2/4JRU is a thaumatin-like protein while I/4L5H and H2/4MBT are VVTL1), and having different unfolding temperatures (56 vs. 62°C), with protein F2/4JRU being heat unstable and forming haze, while I/4L5H does not. These differences in properties are attributable to the conformation of a single loop and the amino acid composition of its flanking regions.
葡萄类甜蛋白(TLPs)在植物与病原体的相互作用中发挥作用,并且除非在装瓶前去除,否则会在白葡萄酒中导致蛋白质浑浊。TLPs的不同亚型具有不同的致浊潜力和聚集行为。在此,我们阐述了三种具有不同致浊潜力的葡萄TLPs的分子结构。尽管这三种TLPs属于两个不同的类别(F2/4JRU是一种类甜蛋白,而I/4L5H和H2/4MBT是VVTL1),且具有不同的解折叠温度(56对62°C),其中蛋白质F2/4JRU热不稳定并形成浑浊,而I/4L5H则不会,但它们的结构非常相似。这些性质上的差异归因于一个单环的构象及其侧翼区域的氨基酸组成。