Abstract:

Anchovy endogenous crude protease is mainly composed of four proteases. Trypsin plays the most important role in reactions with casein. Trypsin-like protease was purified using a combined separation method of ion exchange chromatography and gel filtration chromatography. Preliminary characterization of purified trypsin was also conducted. Results suggested that the purified trypsin from anchovy exhibited excellent thermal and pH stability. The optimal pH and temperature of this enzyme was 9.0 and 55 ℃, respectively. It also exhibited high substrate specificity. According to inhibition profile of specific protease inhibitors and metal ions, trypsin was a kind of metal-activated enzyme rather than a kind of metalloenzyme.

Key words: anchovy endogenous proteases, trypsin, separation and purification, characterization