文献类型：期刊文献

英文题名：Enhancing enzymatic activity of penicillin G acylase by coexpressing pcm gene

作者：Wang, Tianwen[1]; Zhu, Hu[1]; Ma, Xingyuan[1]; Fei, Zhuoya[1]; Ma, Yushu[1]; Wei, Dongzhi[1]

机构：[1] State Key Laboratory of Bioreactor Engineering, New World Institute of Biotechnology, East China University of Science and Technology, Shanghai 200237, China

年份：2006

卷号：72

期号：5

起止页码：953

外文期刊名：Applied Microbiology and Biotechnology

收录：EI(收录号：20064010152116)

语种：英文

外文关键词：Antibiotics - Biotechnology - Cells - Escherichia coli - Genes

摘要：Penicillin G acylase (PGA; E.C. 3.5.1.11) is an important enzyme which has broad applications in industries of β-lactim antibiotics production. In this study, a promising PGA gene from Alcaligenes faecalis (afpga) and another pcm gene encoding protein isoaspartate methyltransferase (PIMT) were constructed into pET43.1a(+) and pET28a(+), respectively. The recombinant plasmids pETAFPGA and pETPCM were transformed into the same host cell Escherichia coli BL21 (DE3). Results suggested that the two plasmids could peacefully exist in the host cell and the two genes could be efficiently expressed after induction. The product of pcm gene could function as a helper molecule for enzyme AFPGA. PIMT increased the enzymatic activities in supernatant of ferment broth (1.6 folds) and cell lysate (1.8 folds), while it did not significantly affect the expression level of penicillin G acylase. ? 2006 Springer-Verlag.