To explore the role of the UDP-glucosyltransferase EcUGT88E3 of Eurotium cristatum in regulating glycosylation of flavonoids， the EcUGT88E3 gene was cloned with homologous sequence cloning method and analyzed with bioinformatics. The pET28a-EcUGT88E3/BL21（DE3） expression system was constructed and the induction conditions were optimized to achieve heterologous expression and purification of the EcUGT88E3 gene. Results showed that the full-length EcUGT88E3 gene was 1 704 bp， with a 75 bp of 5′-UTR， 207 bp of 3′-UTR. The complete open reading frame （ORF） was 1 422 bp， encoding 473 amino acids. Bioinformatics predicted that the encoded protein is a hydrophobic protein with molecular weight of 52.03 ku. The prediction of protein structure indicated that EcUGT88E3 lacks signal peptide and transmembrane domain， and belongs to a microsomal-targeted protein containing GT1 and GT-B superfamily domains. The recombinant EcUGT88E3 protein was expressed as inclusion bodies， with a molecular weight consistent with that predicted. The optimal induction conditions for the pET28a-EcUGT88E3 prokaryotic expression vector in E. coli BL21 （DE3） were 27 ℃ and 0.2 mmol/L IPTG for 4 hours.