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首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >Opposing effects of NaCl on reversibility and thermal stability of halophilic beta-lactamase from a moderate halophile, Chromohalobacter sp. 560.
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Opposing effects of NaCl on reversibility and thermal stability of halophilic beta-lactamase from a moderate halophile, Chromohalobacter sp. 560.

机译：NaCl对中等嗜盐菌嗜盐菌嗜盐菌β-内酰胺酶的可逆性和热稳定性的相反影响。 560。

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摘要

Beta-lactamase from a moderately halophilic organism is expected to show salt-dependent stability. Here we examined the temperature-dependence of stability at different salt concentrations using circular dichroism (CD) and enzyme activity. NaCl showed opposing effects on melting temperature and reversibility of the thermal melting. Increasing NaCl concentration greatly increased the melting temperature from, e.g., 41 degrees C in the absence of NaCl to 61 degrees C in 3 M NaCl. Conversely, reversibility decreased from 92% to 0% in the corresponding NaCl solutions. When beta-lactamase was heated at different temperatures and NaCl concentrations, the activity recovery followed the reversibility, not the melting temperature. Heating beta-lactamase at 63 degrees C, slightly above the onset temperature of melting in 2 M NaCl and far above the melting in 0.2 M NaCl, showed a much greater recovery of activity in 0.2 M NaCl than in 2 M NaCl, again consistent with the reversibility of melting.
机译：预期来自中等嗜盐生物的β-内酰胺酶将显示盐依赖性稳定性。在这里，我们使用圆二色性（CD）和酶活性研究了在不同盐浓度下稳定性的温度依赖性。 NaCl对熔化温度和热熔化的可逆性表现出相反的影响。 NaCl浓度的增加极大地将熔融温度从例如在不存在NaCl的情况下的41℃提高到在3M NaCl中的61℃。相反，在相应的NaCl溶液中，可逆性从92％降低到0％。当在不同温度和NaCl浓度下加热β-内酰胺酶时，活性恢复遵循可逆性，而不是熔融温度。将β-内酰胺酶在63°C加热，略高于2 M NaCl的熔化起始温度，远高于0.2 M NaCl的熔化温度，显示0.2 M NaCl的活性回收率比2 M NaCl大得多。融化的可逆性。

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