%0 Journal Article
%T Study on Heterologous Expression of Penicillinase Gene and the Penicillinase Degrading Residual Penicillin in Milk<br>青霉素酶基因异源表达及该酶分解牛奶中残留青霉素的研究
%A ZHAO Hong-Kun
%A DU Lian-Xiang
%A LI Yu
%A WANG Xiao-Juan
%A LU Fu-Ping
%A <br>赵洪坤
%A 杜连祥
%A 李 玉
%A 王晓娟
%A 路福平
%J 微生物学报
%D 2008
%I 
%X To obtain a number of penicillinases and degrade penicillin in milk by using the penicillinases, the gene encoding penicillinase was amplified by PCR from Bacillus cereus ATCC10987, cloned into pET28a(+), transformed into E. coli BL21; analysis of SDS-PAGE and penicillinase activity of the recombinant protein were done under induction of IPTG and the result showed that the maximum penicillinase activity reached 480 U/mL; the purity of penicillinase purified by Ni2+ Purification System was more than 90%; the immobilized penicillinases were obtained by sodium periodate method and the residual quantity of penicillin in milk(containing 0.5 U penicillin G/mL) was less than 4 ppb after degraded by the immobilized penicillinase.
%K Penicillinase
%K Heterologous expression
%K Purification
%K Immobilized penicillinase<br>青霉素酶
%K 异源表达
%K 纯化
%K 固定化青霉素酶
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=A3C6BA55AB623B90FA9104CFFC826F3C&aid=722EFE4308054C0F0B45FA796757860C&yid=67289AFF6305E306&vid=6209D9E8050195F5&iid=B31275AF3241DB2D&sid=C7D2CDF0EAED78EC&eid=0CE79991D4EDA1AE&journal_id=0001-6209&journal_name=微生物学报&referenced_num=0&reference_num=0