Scholarlink

<p>We report the effects of high hydrostatic pressure (HHP) on D-amino acid oxidase (DAAO) from pork kidney stability and activity. At 20&#xa0;°C, the activity decreased with increasing pressure, but at 40&#xa0;°C, it was not significantly affected because the increased catalytic rate compensated for the enzyme inactivation within the time frame of the experiment. At 50–300&#xa0;MPa, raising the temperature increased the rate of DAAO inactivation, indicating that increases in both pressure and temperature contributed to inactivation. In contrast to other oxidases pressure did not stabilize DAAO against thermal inactivation. Treatments between 0.1 and 100&#xa0;MPa had no significant effect on its stability at 55&#xa0;°C. However, the rate of inactivation increased with increasing pressure from 100 to 300&#xa0;MPa, resulting in an activation volume (ΔV<sup>‡</sup>) of inactivation of -15.8 ± 1.7&#xa0;cm³mol⁻¹. Unlike other oxidases that have buried cavities larger than 100 Å<sup>3</sup> (0.1 nm<sup>3</sup>), DAAO has cavities smaller than 75 Å<sup>3</sup> (0.075 nm<sup>3</sup>), thus supporting the hypothesis that cavity size determines whether pressure stabilizes an enzyme against thermal inactivation.</p>

错误：搜索内容不能为空，请输入英文关键词
错误：关键词超出字数限制，请精简
高级检索

Effect of high hydrostatic pressure on D-amino acid oxidase activity and stability

  • 期刊论文

  • 出版模式：

    开放获取

  • 发表日期：

    2026年1月19日

查看全文
  • Marisabel Morales-Muralles,
  • Spencer J. Serrano,
  • George Makhatadze,
  • José I. Reyes-De-Corcuera

摘要

We report the effects of high hydrostatic pressure (HHP) on D-amino acid oxidase (DAAO) from pork kidney stability and activity. At 20 °C, the activity decreased with increasing pressure, but at 40 °C, it was not significantly affected because the increased catalytic rate compensated for the enzyme inactivation within the time frame of the experiment. At 50–300 MPa, raising the temperature increased the rate of DAAO inactivation, indicating that increases in both pressure and temperature contributed to inactivation. In contrast to other oxidases pressure did not stabilize DAAO against thermal inactivation. Treatments between 0.1 and 100 MPa had no significant effect on its stability at 55 °C. However, the rate of inactivation increased with increasing pressure from 100 to 300 MPa, resulting in an activation volume (ΔV‡) of inactivation of -15.8 ± 1.7 cm³mol⁻¹. Unlike other oxidases that have buried cavities larger than 100 Å3 (0.1 nm3), DAAO has cavities smaller than 75 Å3 (0.075 nm3), thus supporting the hypothesis that cavity size determines whether pressure stabilizes an enzyme against thermal inactivation.