Characterization of proteases from a stored product mite, Tyrophagus putrescentiae.
Extracts of Tyrophagus putrescentiae feces exhibited higher (>50-fold) specific protease activity rates than those measured using mite body extracts for the substrates azocasein, BApNa, SA(2)PPpNa, HA, and HPA. This suggests that trypsin, chymotrypsin, and carboxypeptidases A and B are involved in mite digestion. Hydrolysis of the substrates ZAA(2)MNA and LpNa was only 3 times higher in fecal extracts, suggesting that levels of cathepsin B and aminopeptidases in the lumen of the digestive tract are low compared to the other enzymes. The hydrolysis of hemoglobin was only detected in body extracts indicating that cathepsin D is not a digestive protease in this species. Protease inhibitors of different specificity were tested invivo to establish their potential as control agents. We found that development from larvae to adult was significantly retarded in larvae fed on brewers' yeast containing inhibitors of serine proteases, whereas no such effect was found with inhibitors of cysteine and aspartyl proteases. Interestingly, when dietary mixtures of serine protease, aminopeptidase and carboxypeptidase inhibitors were fed to T.putrescentiae, a synergistic effect was observed that retarded development. Several plant lectins were also tested, but none affected development.
Ortego
F
F
CSIC, CIB, Departamento de Biología de Plantas, Madrid, Spain. ortego@cib.csic.es
Sánchez-Ramos
I
I
Ruiz
M
M
Castañera
P
P
D000626:Aminopeptidases / Q000737:chemistry; D000818:Animals; D016282:Aspartic Acid Endopeptidases / Q000737:chemistry; D043424:Carboxypeptidase B; D002268:Carboxypeptidases / Q000737:chemistry; D043422:Carboxypeptidases A; D002401:Cathepsin B / Q000737:chemistry; D002918:Chymotrypsin / Q000737:chemistry; D003546:Cysteine Endopeptidases / Q000737:chemistry; D010450:Endopeptidases / Q000737:chemistry*; D005243:Feces / Q000201:enzymology*; D008460:Meat; D008925:Mites / Q000201:enzymology* / Q000254:growth & development; D011480:Protease Inhibitors / Q000737:chemistry; D012697:Serine Endopeptidases / Q000737:chemistry; D013552:Swine; D014357:Trypsin / Q000737:chemistry
D011480:Protease Inhibitors; D002268:Carboxypeptidases; D010450:Endopeptidases; D000626:Aminopeptidases; D043422:Carboxypeptidases A; D043424:Carboxypeptidase B; D012697:Serine Endopeptidases; D002918:Chymotrypsin; D014357:Trypsin; D003546:Cysteine Endopeptidases; D002401:Cathepsin B; D016282:Aspartic Acid Endopeptidases