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Distinct Enzyme Activities of Serine Protease P37k in Silkworm Midgut and Molting Fluid by Lingzhen Yang; Yuejing Cheng; Qinglang Wang; Haonan Dong; Taixia Shen; Jing Gong; Qingyou Xia; Yong Hou is a Materials Science article available to read on EtoBox.

What is Distinct Enzyme Activities of Serine Protease P37k in Silkworm Midgut and Molting Fluid about?

Serine proteases possess various biological functions. The serine protease p37k exhibits gelatinolytic activity in the silkworm midgut and degrades cuticular proteins in the molting fluid. In this study, we analyzed the activity changes of recombinant p37k (re-p37k) and p37k in the midgut and molting fluid of Bombyx mori. Firstly, in vitroexpressed re-p37k was activated when a 22 kDa band was observed by western blot. Re-p37k exhibits strong gelatinolytic activity, with the highest activity observed at pH 7.0-9.0 and 45 • C. Compared to p37k in the midgut, re-p37k loses thermal stability but can be restored by midgut extract or ions. E64, AEBSF, and an inhibitor cocktail inhibited the hydrolytic activity of re-p37k on epidermal proteins but did not inhibit the gelatinolytic activity. Subsequently, zymography showed that the positions of gelatinolytic band produced by p37k in the midgut and molting fluid were different, 35 kDa and 40 kDa, respectively. Finally, when heated midgut extract was added to re-p37k or molting fluid, the gelatinolytic band shifted from 40 kDa to 35 kDa, and the proteolytic activity of p37k in the molting fluid was inhibited. Collectively, our results demons

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Author

Lingzhen Yang; Yuejing Cheng; Qinglang Wang; Haonan Dong; Taixia Shen; Jing Gong; Qingyou Xia; Yong Hou

Publisher

Elsevier BV

Published

2024

Language

EN

Field

Materials Science (Physical Sciences)