短小芽孢杆菌碱性蛋白酶的性质  

STUDY ON SOME PROPERTIES OF ALKALINE PROTEINASE FROM BACILLUS PUMILUS

作　　者：冯耀宇[1] 何志敏[1] 杨文博[2] 

机构地区：[1]天津大学化学工程研究所 [2]南开大学

出　　处：《天津大学学报》1998年第2期229-233,共5页Journal of Tianjin University(Science and Technology)

基　　金：国家自然科学基金

摘　　要：对短小芽孢杆菌ｃ１７２（ｐＢＸ９６）转化子发酵淀粉产生的碱性蛋白酶，采用硫酸铵沉淀、ＳｅｐｈａｄｅｘＧ－２５脱盐、ＤＥＡＥ－纤维素柱层析等方法进行纯化，并对纯化酶的性质进行了研究．结果表明，酶反应的最适ｐＨ值为１１．０；在ｐＨ８．０～１１．０之间稳定；最适反应温度为４０℃；热稳定性较好，４５℃下处理３０ｍｉｎ酶活性不变，６０℃下处理３０ｍｉｎ活力保留６５％．对甲基苯磺酰氟（ＰＭＳＦ）能完全抑制该酶活性，洗涤剂中的三聚磷酸钠对酶有较大钝化作用．The alkaline proteinase produced by bacillus pumilus c172(pBX 96) transformant was purified through a process involving ammonium sulfate precipitation,Sephadex G 25 filtration and chromatography on DEAE cellulose.Some properties of the purified enzyme were examined.The optimal pH and temperature for casein hydrolysis were 11.0 and 40℃,respectively.The enzyme was stable over a pH range from 8.0 to 11.0.The enzyme had good heat stability in that its activity remained stable when treated under the condition of 45 ℃,30 min and 65% when treated at 60 ℃,30 min,respectively.The enzyme was completely inactivited after treatment with PMSF(1mM).The sodium phosphate trimer in the detergent can inhibit the enzyme activity greatly.

关 键 词：短小芽孢杆菌 碱性蛋白酶 性质 

分 类 号：TQ925.2[轻工技术与工程—发酵工程]