Effects of Aspergillus niger-fermented Terminalia catappa seed meal-based diet on selected enzymes of some tissues of broiler chicks.

Effects of Aspergillus niger-fermented Terminalia catappa seed meal-based diet on the activities of alkaline phosphatase (ALP), alanine transaminase (ALT), aspartate transaminase (AST) and gamma-glutamate transferase (gamma-GT) in the crop, small intestine, gizzard, heart, liver and serum of broiler chicks were investigated. Milled T. catappa seed was inoculated with spores of A.niger (2.21 x 10(4) spores per ml) for 3 weeks. Forty-five day-old broiler chicks weighing between 27.62 and 36.21 g, were divided into three groups. The first group was fed soybean-based (control) diet; the second on raw T. catappa seed meal-based diet; and the third on A. niger-fermented T. catappa seed meal-based diet for 7 weeks. The results revealed a significantly increased (p<0.05) activity of ALP in the tissues. Contrarily, there were significant reductions (p<0.05) in the activities of ALP, ALT, AST and gamma-GT in the liver and heart of the broilers fed the raw T. catappa seed meal-based diet while there were significant increase (p<0.05) in the activities of these enzymes in the serum of the broilers in this group. The data obtained showed that A. niger-fermented T. catappa seed meal reduced the toxic effects of the raw seed meal on the tissues of broiler chicks.

Purification and biochemical characterization of a turkey preduodenal esterase.

A preduodenal esterase was purified to homogeneity from turkey (Meleagris gallopavo) pharyngial tissue. Pure turkey pregastric esterase (TPrE) was obtained after anion exchange chromatography (DEAE-cellulose), Sephacryl S-200 gel filtration, anion exchange chromatography (Mono-Q sepharose) and affinity chromatography (Blue-Gel Affi Gel). The pure enzyme has an apparent molecular mass of 50 kDa, as determined by SDS/PAGE analysis. The optimum pH and temperature for enzyme activity using tributyrin as substrate were 8.5 and 48 degrees C, respectively. Under these conditions, the specific activity measured was 650 U/mg. No significant lipolytic activity was found when was tested on triolein or liprocil as substrates or with monolayer dicaprin with TPrE. In contrast, TPrE displayed a maximal activities of 800, 680 and 520 U/mg with vinyl acetate, vinyl propionate and vinyl butyrate, respectively. This enzyme retained 75% of its maximal activity when incubated for 30 min at pH 4 and 50 degrees C, but it was completely inactivated after an incubation for 10 min at 60 degrees C. The TPrE N-terminal amino acid sequence showed similarities to the N-terminal sequence of a thioesterase from mallard duck, but no similarity with known preduodenal lipases was found.

Urease activity in the digestive tract of the chick and its role in the utilisation of urea as a source of non-amino nitrogen.

Urease activity was found in caecal contents (about 10 mg urea metabolised/g h) and crop contents (about 0-5 mg urea metabolised/g h):there was very low activity in the contents of the colon but none in the rest of the digestive tract. 2. The urease activity of the crop contents was not bacterial in origin but the soyabean meal contained in the diet was found to have comparable activity. 3. Diets low in non-essential nitrogen and based on soyabean, fish meal or fish meal plus 0-2% jack bean urease, did not support higher growth rates when supplemented with urea. 4. The livers of chicks fed on the diet containing fish meal, urea and urease had significantly higher concentrations of free non-essential amino acids than those of chicks fed on the same diet but with urease excluded This suggested that dietary urease affects the availability of ammonia for the synthesis of non-essential amino acids but not for growth.

Effect of prolactin on lipoprotein lipase in crop sac and adipose tissue of pigeons.

The effect of prolactin on lipoprotein lipase activity of crop sac, omental adipose tissue, and esophagus was studied in adult female pigeons. Prolactin injected for 4 days, 1 mg/day, increased lipoprotein lipase activity from 17 to 177 U/g in crop sac and from 68 to 118 U/g in adipose tissue, but had no effect on the activity in esophagus, 4 U/g. (10 = 1 mumol of chylomicron triglyceride hydrolyzed to free fatty acid and glycerol per hour.? Prolactin increased the weight of crop sac from 1.4 to 7.2 G. The effect of prolactin on lipoprotein lipase activity and weight of crop sac occurred mostly during the 3rd and 4th days of treatment, whereas the effect on the activity of adipose tissue occurred later, during the 4th day of treatment. Crop "milk" collected from pigeons injected with 2 mg of prolactin daily for 4 days contained a small amount of lipoprotein lipase activity, 12 U/g, is smaller than 10% of that found in crop sac. The finding of markedly increased lipoprotein lipase activity in crop sac of prolactin-treated pigeons suggests that blood triglyceride may be used by crop sac for the formation of crop milk lipid.