来自嗜热栖热放线菌YX的碱性丝氨酸蛋白酶。对热和变性剂的稳定性。
Alkaline serine proteinase from Thermomonospora fusca YX. Stability to heat and denaturants.
作者信息
Kristjansson M M, Kinsella J E
机构信息
Institute of Food Science, Cornell University, Ithaca, NY 14853.
出版信息
Biochem J. 1990 Aug 15;270(1):51-5. doi: 10.1042/bj2700051.
Abstract
The serine proteinase isolated from Thermomonospora fusca YX shows considerable thermal stability up to 80 degrees C, and progressive inactivation occurs at higher temperatures. Lyotropic salts affected the thermal stability of the enzyme at 85 degrees C, suggesting that disruption of hydrophobic interactions play an important role in the decreased thermal stability of the enzyme above 80 degrees C. Thermal stability is highly pH-dependent; above pH 6.0-6.5 there is a sharp decrease in the stability of the enzyme, reflecting increased autolysis. Although some stabilization occurs upon increasing ionic strength, Ca2+ binding does not appear to play a role in thermal stability. Denaturants, i.e. 8 M-urea, 6 M-guanidinium chloride or 1% SDS, had no significant effect on the activity of the enzyme after 24 h at 25 degrees C.
摘要
从嗜热栖热放线菌YX中分离出的丝氨酸蛋白酶在高达80℃时表现出相当高的热稳定性，在更高温度下会逐渐失活。离液盐影响该酶在85℃时的热稳定性，这表明疏水相互作用的破坏在80℃以上酶热稳定性降低中起重要作用。热稳定性高度依赖于pH值；在pH 6.0 - 6.5以上，酶的稳定性急剧下降，这反映出自溶增加。尽管增加离子强度时会有一定程度的稳定作用，但Ca2+结合似乎在热稳定性中不起作用。变性剂，即8M尿素、6M氯化胍或1%十二烷基硫酸钠，在25℃下作用24小时后对酶的活性没有显著影响。
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