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Molecular cloning and expression pattern of two serine proteases released from the midgut of Hermetia illucens (Diptera:Stratiomyidae)
- 언어ENG
- URLhttps://db.koreascholar.com/Article/Detail/289590
The black soldier fly (BSF), Hermetia illucens, is known as a beneficial insect and feeds on organic materials derived from animals and human, resulting in reduction of food waste and conversion of organic materials. Despite of many studies on the BSF, there have been no reports of cloned genes encoding serine proteases in the BSF. Thus, the primary objective of this study is to clone and to investigate expression pattern of genes encoding serine proteases released from the midgut of the BSF larvae in order to gain a better understanding of expression mechanism of serine proteases. We cloned two serine proteases from the BSF larva. Based on phylogenetic tree analysis, one was chymotrypsin, the other was trypsin. The open reading frame (ORF) of chymotrypsin was 804bp, which encoded a polypeptide of 267 amino acids. In case of trypsin, the ORF was 744bp, which encoded a polypeptide of 247 amino acids. To investigate expression pattern of two serine proteases, we conducted semi-quantitative RT-PCR at different tissues and different developmental stages. A chymotrypsin and trypsin transcripts were revealed strongly in mid gut. Especially, a chymotrypsin was detected largely at feeding stage more than molting stage, while trypsin was expressed similarly between feeding stage and molting stage
