As a key enzyme in sucrose metabolism, acid invertase expression and enzyme activity was significantly higher in reducing sugar accumulation litchi than in sucrose accumulation litchi. In order to fully understand the biological characteristics of acid invertase, we systematically analyzed the basic physical and chemical properties, protein secondary structure, hydrophilic/hydrophobic, transmememal domain, signal peptide, phosphorylation site, conserved domain and phylogenetic evolution of LcSAI by bioinformatics, and analyzed the expression of LcSAI in different tissues and fruits at different developmental stages of Litchi chinesis 'Feizixiao' by using qRT-PCR. The results were as follows:(1)The acid invertase of litchi fruit was a hydrophilic unstable protein localized to vacuole, and there was no signal peptide. The secondary structure of the protein mainly consisted of irregularly coiled and extended chain members, which were scattered throughout the protein.(2)LcSAI contained a transmembrane region at the N-terminus, including two conserved domains, the N-terminal Pfam DUF3357 domain and the Glyco_32 domain, belonging to the glycosyl hydrolase gene family 32 superfamily. Phylogenetic evolution indicated LcSAI homology with the longan acid invertase gene, the LcSAI expression levels were male flower > root > young stem > seed > young leaf > female flower > peel >mature leaf; the expression of LcSAI in different stages of fruit development was specific, LcSAI expression reached a peak in the second week, then LcSAI expression dropped sharply in the third week, gradually increased in the fourth and fifth weeks, and decreased to a minimum in the eighth week of fruit development. This study provides a theoretical reference for further study of the mechanism of LcSAI fruit acid invertase gene regulation of sucrose metabolism pathway. [ABSTRACT FROM AUTHOR]