Purification and characterization of a novel heterodimer protease inhibitor from Streptomyces spp. VL J2 with potential biopesticidal activity against H. armigera
K Marathe, S Kasar, A Chaudhari, V Maheshwari - Process Biochemistry, 2016 - Elsevier
A protease inhibitor (PI) was isolated and purified from halo-alkaliphilic Streptomyces spp.
VL J2. SDS-PAGE of purified PI revealed it to be a heterodimer of two unidentical subunits of
27.5 and 11.08 kDa, which corroborates well with intact molecular mass of 38.5 kDa
obtained by GPC and MALDI− TOF. Inhibitory activity was confirmed by activity staining and
reverse zymogram studies and the inhibitor was found to retain activity at< 50° C and pH 2–
9.5. It showed presence of two isoforms with isoelectric point of 5.5 and 5.7. The inhibition of …
VL J2. SDS-PAGE of purified PI revealed it to be a heterodimer of two unidentical subunits of
27.5 and 11.08 kDa, which corroborates well with intact molecular mass of 38.5 kDa
obtained by GPC and MALDI− TOF. Inhibitory activity was confirmed by activity staining and
reverse zymogram studies and the inhibitor was found to retain activity at< 50° C and pH 2–
9.5. It showed presence of two isoforms with isoelectric point of 5.5 and 5.7. The inhibition of …