RÉSUMÉ
Objective: To clone chalcone isomerase (sbCHI) gene from the callus of Scutellaria baicalensis and to analyze its bioinformatics. Methods: RNA was obtained from scutellariae callus, cDNA was reversely transcribed, specific primers were designed, and then CHI was cloned. The protein characteristics was analyzed using bioinformatics and the phylogenetic tree of CHI was constructed using MEGA5.1. Results: The 648 bp sbCHI (accession number: KP064512) sequence was obtained, which has a complete open reading frame (ORF), encoding an unstable protein with 215 amino acids. The sbCHI encoding protein has isoelectric point (pI) of 5.09 and a calculated molecular weight about 22 980, without transmembrane regions and signal peptide has a conserved domain of chalcone-flavanone isomerase family. In the secondary structure, the percentage of alpha helix, β-extended, and random coil were 37.21%, 23.25%, and 39.54%, respectively. The homologous analysis indicates the nucleotide sequence 99.69% similarity and the amino acid sequence 99.07% similarity with S. baicalensis (ADQ13184.1), only in 31 and 160 were different. Conclusion: The sbCHI in scutellariae callus is successfully cloned, which provides the foundation for further characterization sbCHI functionality and the synthetic biology research of baicalin.