Recombinant Expression and Enzyme Activity of Chymotrypsin-like Protease from Black Soldier Fly, Hermetia illucens (Diptera: Stratiomyidae)

Chymotrypsin serine protease is one of the main digestive proteases in the midgut of and is involved in various essential processes. In a previous study, a gene encoding a chymotrypsin-like protease, Hi-SP1,was cloned from the larvae of Hermetia illucens and characterized. In this study, we produced...

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Published in:International Journal of Industrial Entomology 2012, 25(2), , pp.181-185
Main Authors: Park, Kwan Ho, Choi, Young Cheol, Nam, Sung Hee, Kim, Won Tae, Kim, A Young, Kim, Sin Young
Format: Article
Language:English
Subjects:
농학
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Summary:Chymotrypsin serine protease is one of the main digestive proteases in the midgut of and is involved in various essential processes. In a previous study, a gene encoding a chymotrypsin-like protease, Hi-SP1,was cloned from the larvae of Hermetia illucens and characterized. In this study, we produced the recombinant chymotrypsin-like protease Hi-SP1 in Escherichia coli cells. The molecular weight of the recombinant Hi-SP1 was estimated to be approximately 26 kDa by sodium dodecyl sulfate–polyacrylamide gel electrophoresis and Western-blotting. Chymotrypsin activity was detected when AAPF was used as the substrate. Examination of the effects of temperature and pH revealed that the proteolytic activity of recombinant Hi-SP1 decreased markedly at temperatures above 30oC, and the optimum pH was found to be 10.0. KCI Citation Count: 0
ISSN:1598-3579
2586-4785
DOI:10.7852/ijie.2012.25.2.181