Screening for antimicrobial peptide genes in the immune-induced Antheraea yamamai larvae led to the identification of a novel antifungal moricin-like peptide (MLP10) gene. The complete MLP10 cDNA is comprised of 403 bp with 174 bp open reading frame encoding a 58 amino acid precursor that contains a putative 23-residue signal peptide, a 2-residue propeptide and a 33-residue mature peptide. The deduced amino acid sequence of MLP10 has 26∼52% identity to those of moricin-related peptides from lepidopteran insects. The MLP10 was highly expressed in E. coli BL21(DE3) by fusing with ketosteroid isomerase (KSI) to avoid the cell death during induction. The resulting expressed KSI-MLP10 fusion protein was in a insoluble form. Recombinant MLP10 was released by cleavage of the fusion protein with cyanogen bromide (CNBr). Subsequently, we purified pure active MLP10 by FPLC chromatography, and 5.2mg of MLP10 was obtained from 1L culture medium. The purified MLP10 was prevented the growth of candida albicans at 6.25 uM, and was also active against gram negative and gram positive bacteria. This potent antimicrobial activity suggests that MLP10 may play a role in the immune response of A. yamamai.