Antiplatelet mechanism of a subtilisin-like serine protease from Solanum tuberosum (StSBTc-3).

The aims of this study are to characterize the antiplatelet activity of StSBTc-3, a potato serine protease with fibrino (geno) lytic activity, and to provide information on its mechanism of action. The results obtained show that StSBTc-3 inhibits clot retraction and prevents platelet aggregation induced by thrombin, convulxin, and A23187. Platelet aggregation inhibition occurs in a dose-dependent manner and is not affected by inactivation of StSBTc-3 with the inhibitor of serine proteases phenylmethylsulfonyl fluoride (PMSF).

Optimization of caseinolytic and coagulating activities of Solanum tuberosum rennets for cheese making.

Background: In recent years, the rising global demand for cheese, the high cost and limited supply of calf rennet, and consumer choices have increased research into new alternatives to animal or recombinant chymosins for cheese making. Plant proteases with caseinolytic activity (CA) and milk-clotting activity (MCA) have been proposed as alternatives for milk clotting to obtain artisanal cheeses with new organoleptic properties. They have been named vegetable rennets (vrennets).

Optimization of fibrinogenolytic activity of subtilisin-like protease (SBTc-3) by response surface methodology.

The aim of this study was to optimize conditions to enhance fibrinogenolytic activity of subtilisin-like protease (SBTc-3). The effects of STBc-3 concentration (0.2-5 μM), pH value (6-10) and temperature (35-50 °C) on fibrinogenolytic activity were studied through response surface methodology (RSM).