CAJ | 학술논문

将大肠杆菌K12菌株来源的腺苷脱氨酶基因(add)克隆到载体pET-28a中,并转化至大肠杆菌BL21(DE3)中进行表达.通过IPTG诱导,SDS-PAGE检测和酶活性的测定发现,重组菌表达产生大量腺苷脱氨酶,活性达到51 07 U/mg蛋白.通过酶性质的研究,腺苷脱氨酶对腺苷最适pH和温度分别为7 5和40℃,且在40℃下维持稳定.
장대장간균K12균주래원적선감탈안매기인(add)극륭도재체pET-28a중,병전화지대장간균BL21(DE3)중진행표체.통과IPTG유도,SDS-PAGE검측화매활성적측정발현,중조균표체산생대량선감탈안매,활성체도51 07 U/mg단백.통과매성질적연구,선감탈안매대선감최괄pH화온도분별위7 5화40℃,차재40℃하유지은정.
The gene encoding adenosine deaminase(add)from Escherichia coli K12 was cloned into expression vector pET-28a and transformed into the strain E.coli BL21(DE3).The protein was highly expressed after the induction with IPTG,then was analyzed with SDS-PAGE and confirmed by the assay of activity.The activity of adenosine deaminase expressed could reached up to 51.07 U/mg protein.The study of characterization showed that adenosine deaminase had optimum pH 7.5 and optimum temperature at 40℃ with thermal stability at 40℃.