Institute of Food Chemistry and Food Biotechnology, Justus Liebig University Giessen, Heinrich-Buff-Ring 17, 35392 Giessen, Germany.
Institute of Inorganic and Analytical Chemistry, Justus Liebig University Giessen, Heinrich-Buff-Ring 17, 35392 Giessen, Germany.
Molecules. 2022 Sep 28;27(19):6409. doi: 10.3390/molecules27196409.
Cross-linking net aggregates of thermolabile thaumatin-like proteins (TLPs) and chitinases (CHIs) are the primary source of haze in white wines. Although bentonite fining is still routinely used in winemaking, alternative methods to selectively remove haze proteins without affecting wine organoleptic properties are needed. The availability of pure TLPs and CHIs would facilitate the research for the identification of such technological advances. Therefore, we proposed the usage of recombinant TLP (rTLP) and CHI (rCHI), expressed by , as haze-protein models, since they showed similar characteristics (aggregation potential, melting point, functionality, glycosylation levels and bentonite adsorption) to the native-haze proteins from . Hence, rTLP and rCHI can be applied to study haze formation mechanisms on a molecular level and to explore alternative fining methods by screening proteolytic enzymes and ideal adsorptive resins.
热稳定类硫素蛋白(TLPs)和几丁质酶(CHIs)的交联网络聚集物是白葡萄酒中浊度的主要来源。尽管膨润土精制仍在酿酒中常规使用,但需要寻找替代方法来选择性地去除浊度蛋白而不影响葡萄酒的感官特性。纯 TLPs 和 CHIs 的可用性将有助于研究此类技术进步。因此,我们提出使用由 表达的重组 TLP(rTLP)和 CHI(rCHI)作为浊度蛋白模型,因为它们表现出与来自 的天然浊度蛋白相似的特性(聚集潜力、熔点、功能、糖基化水平和膨润土吸附)。因此,rTLP 和 rCHI 可用于在分子水平上研究浊度形成机制,并通过筛选蛋白酶和理想的吸附树脂来探索替代的精制方法。