Thermophilic microorganisms that thrive in extreme environments are of great importance because they express heat-resistant enzymes with the potential to serve as biocatalysts in industrial applications. Thermal proteome profiling (TPP) is a multiplexed quantitative mass spectrometry method for analyses of structural information and melting behavior of thousands of proteins, simultaneously determining the thermal denaturation profiles of each protein. We report, in this study, TPP applied to a thermophilic bacterial proteome, a recently isolated strain of Geobacillus thermoleovorans named as ARTRW1. The proteome was investigated in terms of thermostable enzymes that are relevant to industrial applications. In this study, we present the thermostability profiles of its 868 proteins. The majority of G. thermoleovorans proteome was observed to melt between 62.5°C and 72°C, with melting point (T_m) mean value of 68.1°C ± 6.6°C. Unfolding characteristics of several enzymes, including amylase, protease, and lipase, were demonstrated which are highly informative in terms of their applicability to specific industrial processes. A significant correlation was observed between protein melting temperature and the structural features such as molecular weight and abundance, whereas correlations were modest or weak in relation to the α-helix structure percentages. Taken together, we demonstrated a system-wide melting profile analysis of a thermal proteome and listed proteins with elevated T_m values that are highly promising for applications in medicine, food engineering, and cosmetics in particular. The extracted T_m values were found similar to those obtained by biophysical methods applied to purified proteins. TPP analysis has significant industrial and biomedical potentials to accelerate thermophilic enzyme research and innovation.

中文翻译：

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嗜热细菌菌株的热蛋白质组分析和 Meltome 分析，嗜热地芽孢杆菌 ARTRW1：走向工业应用

在极端环境中茁壮成长的嗜热微生物非常重要，因为它们表达耐热酶，有可能在工业应用中用作生物催化剂。热蛋白质组分析 (TPP) 是一种多重定量质谱方法，用于分析数千种蛋白质的结构信息和熔解行为，同时确定每种蛋白质的热变性曲线。我们报告，在这项研究中，TPP 应用于嗜热细菌蛋白质组，这是最近分离的一种名为 ARTRW1的嗜热地芽孢杆菌菌株。根据与工业应用相关的热稳定酶研究蛋白质组。在这项研究中，我们展示了其 868 种蛋白质的热稳定性。多数的观察到G.thermoleovorans蛋白质组在 62.5°C 和 72°C 之间熔化，熔点 (T _m ) 平均值为 68.1°C ± 6.6°C。展示了几种酶（包括淀粉酶、蛋白酶和脂肪酶）的展开特性，这些特性在它们对特定工业过程的适用性方面具有很高的信息量。观察到蛋白质熔解温度与分子量和丰度等结构特征之间存在显着相关性，而与 α-螺旋结构百分比的相关性中等或较弱。综上所述，我们展示了对热蛋白质组和列出的具有升高 T _{m 的}蛋白质的全系统熔解曲线分析特别是在医学、食品工程和化妆品中的应用非常有前景。发现提取的 T _m值与通过应用于纯化蛋白质的生物物理方法获得的值相似。TPP 分析在加速嗜热酶研究和创新方面具有巨大的工业和生物医学潜力。