Chemical Characterization of Aspartic Protease from Artichoke Flower (Cynara cardunculus L. var scolymus) Using MIR Spectroscopy and Analytical Measurements

Vegetable proteases have been studied as milk coagulants, and artichoke flower (Cynara cardunculus L. var scolymus) has potential coagulant action as a substitute for microbial chymosin. The objective was to perform chemical characterization of aspartic proteases from artichoke flower (Cynara cardunculus L. var scolymus) by mid-infrared spectroscopy (MIR) and analytical measurements. Artichoke flower extracts were obtained and crude thistle flower extract and microbial chymosin were used as a reference. Plant extracts and microbial chymosin were analyzed for protein concentration, proteolytic activity (PA), milk clotting activity (MCA), specificity ratio (SR), effects of pH, temperature, NaCl and CaCl₂ concentration on MCA and PA and characterized by electrophoretic, spectroscopic, chromatographic and storage stability. The results indicated that the crude extract of artichoke flower showed high MCA (510.08 SU mL ¹), low PA (10.50 µg mg^-1), SR (48.57) and storage stability for up to 90 days under frozen. The electrophoretic profile of artichoke flower resulted in a protein band with an apparent molecular weight of 32 kDa, associated with cardosin A. Artichoke flower may be a new alternative for commercial plant proteases with active enzymes for milk coagulation.

Keywords:
cardosines; enzyme; infrared; milk coagulation; peptidase; rennet