The United Graduate School of Agricultural Sciences, Iwate University, 18-8, Ueda 3-chome, Morioka 020-8550, Japan.
J Biosci Bioeng. 2010 Aug;110(2):147-51. doi: 10.1016/j.jbiosc.2010.01.019. Epub 2010 Feb 23.
We have cloned a gene encoding an alcohol oxidase (AOD) specific to aldehyde alcohols from Paenibacillus sp. AIU 311. The AOD gene contains an open reading frame consisting of 618 nucleotides corresponding to 205 amino acid residues. The deduced amino acid sequence exhibits a high similarity to that of manganese superoxide dismutases (SODs). We expressed the cloned gene as an active product in Escherichia coli BL21 cells. The productivity (total units per culture broth volume) of the recombinant AOD expressed in E. coli BL21 is 26,000-fold higher than that of AOD in Paenibacillus sp. AIU 311. The recombinant AOD also exhibits aldehyde alcohol oxidase activity and SOD activity. The recombinant cells described in this study have utility for the production of glyoxal from glycolaldehyde.
我们已经从芽孢杆菌 AIU 311 中克隆出一种专门针对醛醇的醇氧化酶(AOD)的基因。AOD 基因包含一个开放阅读框,由 618 个核苷酸组成,对应 205 个氨基酸残基。推导的氨基酸序列与锰超氧化物歧化酶(SODs)高度相似。我们在大肠杆菌 BL21 细胞中表达了克隆的基因作为活性产物。在大肠杆菌 BL21 中表达的重组 AOD 的生产率(每培养肉汤体积的总单位数)比芽孢杆菌 AIU 311 中的 AOD 高 26,000 倍。重组 AOD 还表现出醛醇氧化酶活性和 SOD 活性。本研究中描述的重组细胞可用于从乙二醇醛生产乙二醛。