Temperature dependent characteristics of intestinal glycyl-L-leucine dipeptidase in boreal zone fish.
Three kinds of boreal zone fish were investigated for gastrointestinal glycyl-L-leucine (GL) dipeptide cleaving activity as a function of feeding stage and seasonal changes. The enzyme activity tested in the perch (Perca fluviatilis L.) intestine increased steadily during digestion and rapidly disappeared after completion. The temperature characteristics and the seasonal changes in dipeptide cleaving activity in pike perch (Stizostedion lucioperca L.) and bream (Abramis brama L.) were studied. In summer, the maximal activities in the pike perch and the bream were found at temperatures of 40 and 30 degrees C, respectively. In winter, the temperature of maximal activity in pike perch fell to only 30 degrees C, whereas no changes were observed in bream. The activation energies in bream and pike perch were several times lower in winter than in summer. Seasonal changes in the dipeptide cleaving activity at low temperature relative to that at the temperature of maximal activity were found. At high temperatures, the stability of the enzyme decreases in winter and increases in summer, but in the presence of a substrate the thermal stability of the enzyme increases both in winter and in summer. In our experiments, we found that in these fish, GL dipeptidase was unstable at 0 and -10 degrees C.
Gelman
A
A
Fishery Products Laboratory, Kimron Veterinary Institute, P.O. Box 12, Bet Dagan 50250, Israel. alexander_gelman@hotmail.com
Kuz'mina
V
V
Drabkin
V
V
Glatman
L
L
D000818:Animals; D004150:Dipeptidases / Q000378:metabolism*; D004151:Dipeptides / Q000378:metabolism; D004795:Enzyme Stability; D005399:Fishes; D007413:Intestinal Mucosa / Q000201:enzymology*; D010471:Perches; D021541:Sea Bream; D013696:Temperature; D013997:Time Factors
D004151:Dipeptides; C015905:glycylleucine; D004150:Dipeptidases; C020825:cytosol non-specific dipeptidase