The Purification of Protease From Cowslip (Primula Veris) and Its Use in Food Processing

Abstract

Proteases perform very important functions and are used in different objectives as in vitro and in vivo. In recent years, proteases have been used for clinical, pharmaceutical and industrial applications. Most of these proteases are obtained from animal sources. News of diseases passing over from animals to human (severe acute respiratory syndrome [SARS], mad cow) has created suspicion of contamination in animal food and its product. Therefore, a new vegetal protease source for use in the food industry was studied.Ammonium sulfate fractionation and CM-sephadex ion exchange chromatography were used in the purification of the enzyme. The purified enzyme has an optimum pH of 7.0 and its optimum temperature was 70C. The V max and K m values determined by Lineweaver-Burk graphics were 0.44 mg/mL.min and 40 mM, respectively. The purification degree was determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The native molecular weight of the enzyme was 46 kDa using a gel filtration chromatograph. SDS-PAGE results show that the enzyme has two subunits, which have protease activity at 32 and 14 kD.It was investigated whether the purified and characterized protease enzyme would cause to congeal milk or could produce digestion of chicken and cow meat. The results showed that the protease enzyme can be used for industrial production. 3 Corresponding

Characterization of ginger proteases and their potential as a rennin replacement

“…Ideally, a rennin replacement should be an acid protease with a similar cutting site of chymosin to casein as well as a suitable milk‐clotting/total proteolytic activity ratio 10. There have been many studies on milk‐clotting activity of plant source protease 9, 11, 12. However, there is little literature available on milk‐clotting activity of ginger protease.…”

Çarkıfelek Çiçeğinin (Passiflora incarnata L.) Biyoaktif Kimyasallarının İncelenmesi

“…Ammonium sulphate precipitation was performed in the homogenate as between 10% and 100% (Demir et al, 2007). This sedimentation was carried out in the form of 0-20%, 20-40%, 40-60%, 60-80%, and 80-100%.…”

Purification and characterization of a novel serine protease compositain from compositae (Scorzonera hispanica L.)

“…Time of coagulation with protease enzyme in the test tube was recorded [17]. The unit of milk-clotting activity was deWned as the amount of milk that was clotted by 1.0 mL of enzyme in 1 min [22,23].…”