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首页> 外文期刊>Journal of Agricultural and Food Chemistry >Thermal Stability of Thaumatin-Like Protein, Chitinase, and Invertase Isolated from Sauvignon blanc and Semillon Juice and Their Role in Haze Formation in Wine
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Thermal Stability of Thaumatin-Like Protein, Chitinase, and Invertase Isolated from Sauvignon blanc and Semillon Juice and Their Role in Haze Formation in Wine

机译：从长相思和赛美蓉汁中分离得到的类索马甜蛋白，几丁质酶和转化酶的热稳定性及其在葡萄酒混浊中的作用

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摘要

A thermal unfolding study of thaumatin-like protein, chitinase, and invertase isolated from Vitis vinifera Sauvignon blanc and Semillon juice was undertaken. Differential scanning calorimetry demonstrated that chitinase was a major player in heat-induced haze in unfined wines as it had a low melt temperature, and aggregation was observed. The kinetics of chitinase F1 (Sauvignon blanc) unfolding was studied using circular dichroism spectrometry. Chitinase unfolding conforms to Arrhenius behavior having an activation energy of 320 kJ/mol. This enabled a predictive model for protein stability to be generated, predicting a half-life of 9 years at 15 °C, 4.7 days at 30 °C, and 17 min at 45 °C. Circular dichroism studies indicate that chitinase unfolding follows three steps: an initial irreversible step from the native to an unfolded conformation, a reversible step between a collapsed and an unfolded non-native conformation, followed by irreversible aggregation associated with visible haze formation.
机译：进行了热解研究，从葡萄，长相思和果汁中分离出奇异蛋白类似蛋白，几丁质酶和转化酶。差示扫描量热法表明，几丁质酶是未精制葡萄酒中热诱导混浊的主要参与者，因为它的熔解温度低，并且观察到聚集。几丁质酶F1（长相思）展开的动力学使用圆二色光谱法进行了研究。几丁质酶的展开符合Arrhenius行为，其活化能为320 kJ / mol。这使得能够生成蛋白质稳定性的预测模型，预测在15°C下9年的半衰期，在30°C下4.7天的半衰期和在45°C下17分钟的半衰期。圆二色性研究表明，几丁质酶的展开遵循三个步骤：从天然构象到展开构象的初始不可逆步骤，在折叠和展开的非天然构象之间的可逆步骤，然后是与可见的雾度形成相关的不可逆聚集。

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