Biochemical characterisation of chymotrypsin from the midgut gland of yellowleg shrimp, Penaeus californiensis.

Chymotrypsin from shrimp, Penaeus californiensis, was compared to Bos taurus chymotrypsin, and its structure-function relationship was studied. Catalytic efficiency toward synthetic substrate is lower, but it has a broad specificity and higher activity toward protein substrates, including collagen. It is active at pH 4-10 and fully active up to 50 °C for 2 h and at least nine days at room temperature.

Purification and biochemical characterization of digestive lipase in whiteleg shrimp.

Penaeus vannamei lipase was purified from midgut gland of whiteleg shrimp. Pure lipase (E.C.

Phenoloxidase activity of hemocyanin in whiteleg shrimp Penaeus vannamei: conversion, characterization of catalytic properties, and role in postmortem melanosis.

Latent phenoloxidase activity of hemocyanin (Hc) in whiteleg shrimp Penaeus vannamei was assayed to determine its potential involvement in postmortem melanosis. Conversion of pure 12-mer, but not 6-mer, hemocyanin to phenoloxidase by endogenous (serine proteinases) and exogenous (SDS) effectors demonstrated the need of complex aggregation for displaying enzyme activity. Because Hc was converted to Hc-phenoloxidase (HcPO) by hemocytes extracts, the mechanism of conversion seems to be the same for polyphenoloxidases.

Invertebrate trypsins: a review.

Food protein hydrolysis, a crucial step in digestion, is catalyzed by trypsin enzymes from the digestive apparatus of invertebrates. Trypsin appeared early in evolution and occurs in all phyla and, in the digestive systems of invertebrates, it became the most abundant proteinase. As in vertebrates, invertebrate trypsin is also present in several forms (isoenzymes).

Isolation and characterization of trypsin from pyloric caeca of Monterey sardine Sardinops sagax caerulea.

Trypsin from pyloric caeca of Monterey sardine was purified by fractionation with ammonium sulfate, gel filtration, affinity and ionic exchange chromatography. Fraction 102, obtained from ionic exchange chromatography, generated one band in sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) and isoelectric focusing. The molecular mass of the isolated trypsin was 25 kDa and showed esterase-specific activity on Nalpha-p-tosyl-L-arginine methyl ester (TAME) that was 4.

Penaeus vannamei isotrypsins: purification and characterization.

Three isotrypsins from digestive gland of Penaeus vannamei were purified and characterized by molecular, biochemical and kinetic parameters. Purified isotrypsins A, B, and C are glycoproteins with molecular masses between 30.2 and 32.

Characterization of proteases in the digestive system of spiny lobster (Panulirus interruptus).

Enzymes responsible for digestion of food protein were evaluated and characterized in red lobster (Panulirus interruptus). Several tissues, organs, and body fluids were analyzed. The same composition of proteases was found in gastric juice, midgut gland, and intestinal contents.

Effects of dietary protein on the activity and mRNA level of trypsin in the midgut gland of the white shrimp Penaeus vannamei.

Protein food modulates the activity of proteases of the midgut gland of Penaeus vannamei. Shrimp fed with food containing 15, 30 and 50% protein exhibited differences in trypsin and chymotrypsin activity and trypsin mRNA levels. Shrimp fed with 30% protein showed higher trypsin and chymotrypsin activities than those fed 15 or 50% protein.

Influence of molting and starvation on the synthesis of proteolytic enzymes in the midgut gland of the white shrimp Penaeus vannamei.

We investigated the effect of starvation as a stimulant of the digestive system on digestive proteinase activities in the white shrimp Penaeus vannamei. The starved organisms were sampled periodically according to the molting stage and compared with a continuously fed group. Molting stage was included as an independent variable.

Digestive proteinases of Brycon orbignyanus (Characidae, Teleostei): characteristics and effects of protein quality.

Juvenile piracanjuba, Brycon orbignyanus, in the wild consume protein from both plant and animal sources. Digestion of protein in piracanjuba begins in the stomach with pepsin, at low pH, and is followed by hydrolysis at alkaline pH in the lumen of the intestine. The digestive system in piracanjuba was evaluated to characterize the enzymes responsible for the digestion of feed protein and their composition.