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作 者:罗秀针[1] 郑金华[1] 林燕燕[1] 吴伟斌 LUO Xiu-zhen;ZHENG Jin-hua;LIN Yan-yan;WU Wei-bin(Zhangzhou Health Vocational College,Zhangzhou,Fujian 363000,China;Fujian Vocational College of Bioengineering,Fuzhou,Fujian 350007,China)
机构地区:[1]漳州卫生职业学院,福建漳州363000 [2]福建生物工程职业技术学院,福建福州350007
出 处:《福建农业科技》2022年第8期8-13,共6页Fujian Agricultural Science and Technology
基 金:福建省自然科学基金项目(2021J01348);漳州市自然科学基金项目(ZZ2020J38)。
摘 要:通过酪氨酸脱羧酶(TDC)催化L-酪氨酸脱羧生成酪胺,是一种低成本、高效、绿色制备酪氨的方法。利用pBAD/His为载体在宿主细胞E.coli BL21-AI(DE3)中表达了短乳杆菌来源的TDC,构建基因工程菌E.coli BL21-AI(DE3)-tdc,并对该菌L-阿拉伯糖诱导表达的条件进行优化。结果表明:在26℃培养6 h后加入终浓度为1.0 g·L^(-1)的L-阿拉伯糖诱导表达8 h,TDC酶活达183.2 U·g^(-1);在5 L发酵罐进行放大,TDC酶活达到192 U·g^(-1),菌体最高湿重为18.2 g·L^(-1),相对于摇瓶发酵的1.92 g·L^(-1)增长了8.47倍。L-tyrosine decarboxylation catalyzed by tyrosine decarboxylase(TDC)to produce tyramine,is a low-cost,efficient,green preparation method to produce tyrosine.The TDC derived from Lactobacillus brevis was expressed in the host cell of E.coli BL21-AI(DE3)by using the pBAD/His vector,and the genetically engineered bacteria E.coli BL21-AI(DE3)-tdc was constructed,and the conditions of L-arabinose induced expression of the strain were optimized.The results showed that the enzyme activity of TDC reached 183.2 U·g^(-1)after the induced expression with 1.0 g·L^(-1)L-arabinose at 26℃for 6 h.The TDC activity reached 192 U·g^(-1)and the maximum wet weight of bacteria was 18.2 g·L^(-1),which was 8.47 times higher than that in the shaking flask fermentation,being 1.92 g·L^(-1).
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