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Digestive proteinases of red shrimp Pleoticus muelleriPleoticus muelleri / Decapoda, Penaeoidea : partial characterization and relationship with molting relationship with molting Decapoda, Penaeoidea : partial characterization and relationship with molting A.V. Fernandez Gimeneza, F.L. Garcıa-Carrenob,, ´ ´ a, F.L. Garcıa-Carrenob,, ´ ´ M.A. Navarrete del Torob, J.L. Fenucciab, J.L. Fenuccia aDepartamento Ciencias Marinas, Facultad Ciencias Exactas y Naturales, Uniersidad Nacional de Mar del Plata, CONICET, Funes 3350, B7602AYL, Mar del Plata, Argentina Funes 3350, B7602AYL, Mar del Plata, Argentina Departamento Ciencias Marinas, Facultad Ciencias Exactas y Naturales, Uniersidad Nacional de Mar del Plata, CONICET, Funes 3350, B7602AYL, Mar del Plata, Argentina bCentro de Inestigaciones Biologicas del Noroeste, A.P. 128, La Paz, Baja California Sur, 23000, Mexico ´Centro de Inestigaciones Biologicas del Noroeste, A.P. 128, La Paz, Baja California Sur, 23000, Mexico ´ Received 21 February 2001; received in revised form 15 June 2001; accepted 3 July 2001 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 The hepatopancreatic protein content in the premolt stage was higher than in the other stages of the molting cycle 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 . P0.05 . 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 molting stages. The proteolytic activity of the P. muelleri hepatopancreas enzyme preparations is the main responsibility P0.05 . 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 responsibilityP. muelleri hepatopancreas enzyme preparations is the main responsibility . of serine proteinases. TLCK, a trypsin inhibitor, reduced azocasein hydrolysis between 26% intermolt and 37%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 chymotrypsin activities were found during intermolt, and increased in postmolt. The electrophoretogram of the enzyme 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 theextracts 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 moltingpostmolt 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 bandsstages. One band of chymotrypsin 21.9 kDa was observed in all molting stages. High molecular mass active bands . 66205 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. of some species indicated a relationship between digestive enzyme activity and feeding habits of the shrimp. 66205 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 annamei syn: Litopenaeus annamei and Penaeus monodon, showed higherOmnivorous shrimp, such as Penaeus annamei syn: Litopenaeus annamei 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. 2001 Elsevier Science Inc. All rights reserved. molting cycle. 2001 Elsevier Science Inc. All rights reserved. In fact, the enzymatic activity in the hepatopancreas of P. muelleri showed variations in relation to feeding habit and molting cycle. 2001 Elsevier Science Inc. All rights reserved. molting cycle. 2001 Elsevier Science Inc. All rights reserved. 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. 2001 Elsevier Science Inc. All rights reserved. molting cycle. 2001 Elsevier Science Inc. All rights reserved. P. muelleri showed variations in relation to feeding habit and molting cycle. 2001 Elsevier Science Inc. All rights reserved. 2001 Elsevier Science Inc. All rights reserved. Keywords: Digestive enzymes; Molting; Pleoticus muelleri; Protein digestion; ProteasesDigestive enzymes; Molting; Pleoticus muelleri; Protein digestion; Proteases

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