Andrews G P, Martin S E
Appl Environ Microbiol. 1979 Jun;37(6):1180-5. doi: 10.1128/aem.37.6.1180-1185.1979.
The effects of heat on catalase from Staphylococcus aureus lysates were examined. Catalase activity increased with increasing concentrations of potassium phosphate buffer, when heated at temperatures between 50 and 65 degrees C for 10 min. Inactivation of catalase by NaCl during heating was demonstrated. Extended heating of S. aureus cells at 52 degrees C resulted in a slight decrease in catalase activity of the resultant lysates. This decrease was more pronounced in the presence of salt. Heating at 62 degrees C caused a decrease in catalase activity, but not complete inactivation. These results implicate the combined effects of heat, and NaCl in the inactivation of catalase from S. aureus. The findings are consistent with the hypothesis that H2O2 may accumulate as a result of decreased catalase activity and be responsible for the decreased colony-forming ability of stressed S. aureus.
研究了热对金黄色葡萄球菌裂解物中过氧化氢酶的影响。当在50至65摄氏度的温度下加热10分钟时,过氧化氢酶活性随着磷酸钾缓冲液浓度的增加而增加。证明了加热过程中NaCl对过氧化氢酶的失活作用。在52摄氏度下对金黄色葡萄球菌细胞进行长时间加热,导致所得裂解物中过氧化氢酶活性略有下降。在有盐存在的情况下,这种下降更为明显。在62摄氏度下加热导致过氧化氢酶活性下降,但并未完全失活。这些结果表明热和NaCl共同作用导致金黄色葡萄球菌过氧化氢酶失活。这些发现与以下假设一致,即过氧化氢酶活性降低可能导致H2O2积累,并导致应激状态下金黄色葡萄球菌的集落形成能力下降。