Proteolytic Properties of Cathepsin L, Chymotrypsin, and Trypsin from the Muscle and Viscera of Anchovy, Engraulis japonica

Abstract

Proteolytic properties of enzymes from the muscle and viscera of anchovy have been examined. Cathepsin L, chymotrypsin, and trypsin showed similar Km values for casein. However, they had higher Km values for myofibrillar proteins than those for casein. The of cathepsin L and chymotrypsin for myofibrillar proteins were higher than that of trypsin, and also cathepsin L and chymotrypsin caused higher hydrolysis in myofibrillar proteins of anchovy and yellowtail. In the presence of sodium chloride, proteolytic activity for myofibrillar proteins from yellowtail was higher than that for casein. Proteolytic activity was decreased with the increase of sodium chloride concentration. Cathepsin L had been less affected by NaCl concentration and temperature on the hydrolysis of myofibrillar proteins than chymotrypsin and trypsin. Cathepsin L and chymotrypsin were move responsible to the autolysis of muscle proteins from fish than trypsin.