Cloning and Bioinformatics Analysis of Arginine Decarboxylase Gene in Scomberomorus niphonius
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Abstract:
In this study, Enterobacter hormaechei, a spoilage amine-producing bacteria during storage of mackerel, was used as the research object. The physico-chemical properties of arginine decarboxylase of Enterobacter hormaechei in Scomberomorus niphonius were examined by various of genetic engineering and bioinformatic methods. The ADC gene was cloned and sequenced by T-A, translated into a protein sequence, before the primary structure, secondary structure and three-dimensional conformation of the protein were predicted, and the physico-chemical properties and functions of the ADC protein were analyzed. The results showed that the ADC protein was composed of 93 amino acids, with the estimated molecular weight roughly as 10.82 ku, the theoretical isoelectric point as 8.64, the atomic composition as C492 H746 N136 O135 S3, and the half-life >10 h (E. coli, in vivo), and the fat coefficient as 86.02. With the total average hydrophilicity as -0.35, the overall performance of the protein was hydrophilic. Behaving like a soluble protein with the instability coefficient as 48.57, the ADC protein did not have a signal peptide and was a secreted protein. These results as well as the simultaneously predicted secondary structure and three-dimensional conformation of the ADC protein provide a reference for subsequent in-depth research. In the future, on the basis of gene cloning, protein expression, separation and purification and properties research should be carried out to analyze further arginine decarboxylase.
