High hydrostatic pressure stabilized galactose oxidase (GaOx) at 70.0–80.0°C against thermal inactivation. The pseudo‐first‐order rate constant of inactivation kinact decreased by a factor of 8 at 80°C and by a factor of 44 at 72.5°C. The most pronounced effect of pressure was at the lowest studied temperature of 70.0°C with an activation volume of inactivation ΔV‡ of 78.8 cm3 mol−1. The optimal pressure against thermal inactivation was between 200 and 300 MPa. Unlike other enzymes, as temperature increased the ΔV‡ of inactivation decreased, and as pressure increased the activation energy of inactivation Eai increased. Combining the results for GaOx with earlier research on the pressure‐induced stabilization of other enzymes suggests that ΔV‡ of inactivation correlates with the total molar volume of cavities larger than ~100 Å3 in enzyme monomers for enzymes near the optimal pH and whose thermal unfolding is not accompanied by oligomer dissociation.

中文翻译：

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高静水压稳定半乳糖氧化酶：关于空腔尺寸作用的见解

高静水压可在 70.0–80.0°C 下稳定半乳糖氧化酶 (GaOx)，防止热失活。失活的伪一级速率常数k不作为在 80°C 时下降 8 倍，在 72.5°C 时下降 44 倍。压力最显着的影响是在最低研究温度 70.0°C 下，失活的活化体积为 ΔV‡78.8 厘米3摩尔−1。防止热失活的最佳压力为 200 至 300 MPa。与其他酶不同，随着温度升高，ΔV‡失活的能量降低，并且随着压力的增加，失活的活化能乙人工智能增加。将 GaOx 的结果与其他酶的压力诱导稳定性的早期研究相结合表明 ΔV‡失活的程度与大于 ~100 Å 的空腔总摩尔体积相关3酶单体中的酶接近最佳 pH，且其热解折叠不伴随低聚物解离。