本文選題：Ⅱa類乳酸菌細(xì)菌素　切入點(diǎn)：sakacin　出處：《食品工業(yè)》2017年05期

【摘要】：Sakacin P是來自乳酸菌(Lactobacillus sakei)的細(xì)菌素,是潛在的抗微生物細(xì)菌素,其對(duì)食源性病原體例如單核增生李斯特氏菌具有較強(qiáng)的活性。在乳酸菌中,編碼sakacin P的結(jié)構(gòu)基因(spp A)通過嚴(yán)格的調(diào)節(jié)機(jī)制控制,使得分泌的sakacin P的量有限。通過拼接重疊延伸PCR(SOE-PCR)合成了sppA基因,并將其克隆到大腸桿菌中。用異丙基-β-d-硫代半乳糖苷(IPTG)誘導(dǎo)后,重組sakacin P成功表達(dá)。收集的細(xì)胞進(jìn)行超聲處理,并通過使用無細(xì)胞上清液的抑制法鑒定其活性。結(jié)果表明,20℃低溫誘導(dǎo)合成了更具活性的sakacin P,具有更強(qiáng)的抗微生物活性。
[Abstract]:Sakacin P, a bacteriocin from Lactobacillus sakeii, is a potential antimicrobial bacteriocin, which has strong activity against foodborne pathogens such as Listeria monocytogenes.In lactic acid bacteria, the structural gene encoding sakacin P, spp A, is controlled by strict regulatory mechanisms, resulting in a limited amount of sakacin P secreted.The sppA gene was synthesized by splicing and cloned into E. coli.The recombinant sakacin P was successfully expressed after induction by isopropyl- 尾 -d- thiogalactoside (IPTG).The collected cells were treated by ultrasound and their activity was determined by the inhibition method of acellular supernatant.The results showed that more active sakacin P was synthesized at 20 鈩，

本文編號(hào)：1719010