title: Digestive proteinases of red shrimp Pleoticus muelleri (Decapoda, Penaeoidea): partial characterization and relationship with molting.
abstract: The present study describes the activity and some characteristics of proteinases in the hepatopancreas of red shrimp Pleoticus muelleri during the different stages of the molting cycle. Proteolytic activity was highest between pH 7.5 and 8. The hepatopancreatic protein content in the premolt stage was higher than in the other stages of the molting cycle (P<0.05). No significant differences were found in total proteolytic activity in the hepatopancreas when comparing molting stages. The proteolytic activity of the P. muelleri hepatopancreas enzyme preparations is the main responsibility of serine proteinases. TLCK, a trypsin inhibitor, reduced azocasein hydrolysis between 26% (intermolt) and 37% (premolt). TPCK, a chymotrypsin inhibitor, did not decrease hydrolytic activity, except for in postmolt. Low trypsin and chymotrypsin activities were found during intermolt, and increased in postmolt. The electrophoretogram of the enzyme extracts shows 12 bands of activity during intermolt (from 16.6 to 53.1 kDa). Some fractions were not detected in the postmolt and premolt stages. Three low molecular weight trypsin forms (17.4, 19.1 and 20 kDa) were found in all molting stages. One band of chymotrypsin (21.9 kDa) was observed in all molting stages. High molecular mass active bands (66-205 kDa) could not be characterized with inhibitors. Comparison of the protease-specific activity of the hepatopancreas of some species indicated a relationship between digestive enzyme activity and feeding habits of the shrimp. Omnivorous shrimp, such as Penaeus vannamei (syn: Litopenaeus vannamei) and Penaeus monodon, showed higher protease activity than the carnivorous shrimp, Penaeus californiensis (syn: Farfantepenaeus californiensis) and P. muelleri. In fact, the enzymatic activity in the hepatopancreas of P. muelleri showed variations in relation to feeding habit and molting cycle.
authors.affiliation: Departamento Ciencias Marinas, Facultad Ciencias Exactas y Naturales, Universidad Nacional de Mar del Plata, CONICET, Funes 3350, B7602AYL, Mar del Plata, Argentina.
authors.forename: A V
authors.initials: AV
authors.lastname: Fernández Gimenez
authors.forename: F L
authors.initials: FL
authors.lastname: García-Carreño
authors.forename: M A
authors.initials: MA
authors.lastname: Navarrete del Toro
authors.forename: J L
authors.initials: JL
authors.lastname: Fenucci
mesh_terms: D000818:Animals; D002918:Chymotrypsin / Q000737:chemistry / Q000378:metabolism; D033364:Decapoda / Q000201:enzymology* / Q000502:physiology*; D004064:Digestive System / Q000187:drug effects / Q000201:enzymology*; D010450:Endopeptidases / Q000737:chemistry / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D018978:Molting; D011480:Protease Inhibitors / Q000494:pharmacology; D014107:Tosyllysine Chloromethyl Ketone / Q000494:pharmacology; D014108:Tosylphenylalanyl Chloromethyl Ketone / Q000494:pharmacology; D014357:Trypsin / Q000737:chemistry / Q000378:metabolism
chemical_list: D011480:Protease Inhibitors; D014107:Tosyllysine Chloromethyl Ketone; D014108:Tosylphenylalanyl Chloromethyl Ketone; D010450:Endopeptidases; D002918:Chymotrypsin; D014357:Trypsin