Polymorphism and partial characterization of digestive enzymes in the spiny lobster Panulirus argus.
We characterized major digestive enzymes in Panulirus argus using a combination of biochemical assays and substrate-(SDS or native)-PAGE. Protease and amylase activities were found in the gastric juice while esterase and lipase activities were higher in the digestive gland. Trypsin-like activity was higher than chymotrypsin-like activity in the gastric juice and digestive gland. Stability and optimal conditions for digestive enzyme activities were examined under different pHs, temperature and ionic strength. The use of protease inhibitors showed the prevalence of serine proteases and metalloproteases. Results for serine proteases were corroborated by zymograms where several isotrypsins-like (17-21 kDa) and isochymotrypsin-like enzymes (23-38 kDa) were identified. Amylases (38-47 kDa) were detected in zymograms and a complex array of non-specific esterases isoenzymes was found in the digestive gland. Isoenzyme polymorphism was found for trypsin, amylase, and esterase. This study is the first to evidence the biochemical bases of the plasticity in feeding habits of P. argus. Distribution and properties of enzymes provided some indication on how the digestion takes place and constitute baseline data for further studies on the digestion physiology of spiny lobsters.
Perera
Erick
E
Center for Marine Research, University of Havana, Havana, Cuba. erickpb@comuh.uh.cu
Moyano
F J
FJ
Díaz
M
M
Perdomo-Morales
R
R
Montero-Alejo
V
V
Alonso
E
E
Carrillo
O
O
Galich
G S
GS
D000818:Animals; D004064:Digestive System / Q000201:enzymology*; D004591:Electrophoresis, Polyacrylamide Gel; D004795:Enzyme Stability; D004798:Enzymes / Q000378:metabolism; D005750:Gastric Juice / Q000201:enzymology; D006863:Hydrogen-Ion Concentration; D033521:Palinuridae / Q000201:enzymology*; D011480:Protease Inhibitors / Q000494:pharmacology; D013696:Temperature
D004798:Enzymes; D011480:Protease Inhibitors