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Purification And Biophysical Characterization Of 37 KDa Serine Protease Zymogen From Silkworm, Bombyx Mori | 28418
ISSN: 2155-952X
Journal of Biotechnology & Biomaterials
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Numerous enzymes have been synthesized as a zymogen in different stage and activated time-specific manner in many insect
pests for its growth and development. Particularly, 37kDa serine protease was synthesized as a zymogen precursor in the
midgut and activated upon pupation of B. mori. 37 kDa serine protease encodes a 37 kDa composed of 329 amino acid which
is playing a critical role in the process of digestion of food and physiological process including apoptosis and tissue remodelling
in B. mori. To purify and characterize the 37 kDa serine protease, it was over expressed by using PET30a expression vector in
Escherichia coli (BL21 DE3) with N-terminal His6-tag. The over expressed His-tag protein was successfully purified using Ni-
NTA and observed as a single band with a molecular mass of 42.5 kDa on SDS-PAGE. The pI of the purified protein was found
to be three major spots between the pI of 6.2 to 6.8 with MW 45kDa were determined by using 2D-PAGE. The resulted protein
spots were also confirmed by MALDI-TOF-MS analysis. Circular Dichroism showed that 37 kDa serine protease zymogen was
consistent over the range of 6-7 for the pH, with approximately half of the protein having well-defined ?-helical and ?-sheet
secondary structure. The composition of purified p37k serine protease was analysed using HPLC. Computational prediction of
cleavage site for signal peptide and propeptide of 37 kDa serine protease between positions of 18-19, 35-66 aa respectively were
determined through Signal P-4.1 tool. This result revealed that pI/Mw of active protease of 37kDa serine protease after removal
of pro-peptide showed 5.91 / 28007.38. This overall results revealed that the complex structure of this protease reasoned for
inactive zymogen and slightly acidic pH at (>5) plays a major role in activation 37 kDa serine protease in the midgut for tissue
remodelling during pupation or anti-feeding stage. In future, the identification of zymogen (pro-protein) processing enzyme
will be much helpful for the development of novel drug/pesticide for the control of insect pests.
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