Sesame meal as the first protein source in piglet starter diets and advantages of a phytase: a digestive study

Soybean meal (SBM) is the protein source that is used most in feeding piglets, but its high price has prompted a search for alternatives. One option is sesame meal (SM), a by-product of sesame oil. This study evaluated the effects of SM and phytase on the intestinal morphology, total trypsin activity (TTA) and specific trypsin activity (STA), apparent ileal digestibility (AID) of amino acids (AAs), and apparent total tract digestibility (ATTD) of phosphorus (P), calcium (Ca), and energy (E) in weaned piglets. Twenty piglets weaned at 17 days old were placed in metabolic cages in a temperature-controlled room. When the piglets were 21 days old, cannulas were fitted at the terminal ileum. From the fourth day after surgery, piglets received the experimental treatments for nine days, namely an SM or SBM diet, each with or without phytase. The protein source or phytase did not affect villus height, crypt depth, or TTA. However, phytase increased STA. The AID of dry matter (DM), E, crude protein (CP), and AA was similar among treatments, except for arginine, which was more digestible in the SM diets (85.8) than in the SBM ones (81.6). The ATTD of DM and E was higher in the SM than in the SBM diets. Phytase increased the ATTD of Ca (22.7 %) and P (27.9 %). The findings showed that SM can be used as a protein source for piglets and that its consumption increases arginine intake. The addition of phytase to the diet increases the ATTD of P and Ca.Keywords: Amino acids digestibility, arginine, piglets weaning, phosphorus digestibilit

Adaptive Changes of Some Enzyme Activities in Rats and Humans to Dietary Protein

A study of the adaptive changes of some enzyme activities to the dietary protein intake was made in the liver, kidney, and pancreas of rats and serum of humans. The rats fed the 40 per cent casein diet had a higher rate of weight gain and the weights of the liver and kidney were higher than in the rats fed the 10 per cent casein diet. Three enzymes involved in the elimination of excess nitrogen from the body were found to show a similar response to increased dietary protein intake. These enzymes were: D-amino acid oxidase in the kidneys, arginase in the liver and kidneys, and glutamic-pyruvic transaminase in the liver of rats. The rate of enzyme induction was detectable the second day, being high during the first four days and reaching the maximum value on the fourth day. Thereafter, the enzymatic activity did not change much. The alkaline phosphatase activities in the liver and kidneys of the rats did not show significant change during consumption of the diets containing 10 per cent or 40 per cent casein. Samples of pancreatic trypsinogen and chymotrypsinogen of the rats were not collected during the appropriate time to note any significant changes caused by the diets . A more appropriate experimental design, including proper timing for feedings and dissections, for the study of the adaptation of the proteolytic enzymes in the pancreas of the rats is desirable and recommended. The values for the circulating enzymes of the human serum, 0-amino acid oxidase, glutamic-pyruvic transaminase, and alkaline phosphatase were not found to be affected significantly by the diets containing 12 per cent and 30 per cent protein calories

Insulin protects acinar cells during pancreatitis by preserving glycolytic ATP supply to calcium pumps.

From Europe PMC via Jisc Publications RouterHistory: ppub 2021-07-01, epub 2021-07-19Publication status: PublishedFunder: Medical Research Council; Grant(s): MR/P00251X/1Funder: NIDDK NIH HHS; Grant(s): P30 DK089503, R01 DK059578, P30 DK020572, P60 DK020572, U2C DK110768Funder: Wellcome TrustAcute pancreatitis (AP) is serious inflammatory disease of the pancreas. Accumulating evidence links diabetes with severity of AP, suggesting that endogenous insulin may be protective. We investigated this putative protective effect of insulin during cellular and in vivo models of AP in diabetic mice (Ins2Akita) and Pancreatic Acinar cell-specific Conditional Insulin Receptor Knock Out mice (PACIRKO). Caerulein and palmitoleic acid (POA)/ethanol-induced pancreatitis was more severe in both Ins2Akita and PACIRKO vs control mice, suggesting that endogenous insulin directly protects acinar cells in vivo. In isolated pancreatic acinar cells, insulin induced Akt-mediated phosphorylation of 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 2 (PFKFB2) which upregulated glycolysis thereby preventing POA-induced ATP depletion, inhibition of the ATP-dependent plasma membrane Ca2+ ATPase (PMCA) and cytotoxic Ca2+ overload. These data provide the first mechanistic link between diabetes and severity of AP and suggest that phosphorylation of PFKFB2 may represent a potential therapeutic strategy for treatment of AP

Of piglets, dietary proteins, and pancreatic proteases

Newly weaned piglets often show digestive disorders, frequently resulting in diarrhoea. These disorders may be related to the dietary protein source, since young piglets are less capable of digesting proteins of vegetable origin than older pigs. This study was undertaken to investigate the development of protein digestive capacity in weaned piglets. In the first part of the thesis it was established that the difference in nitrogen digestibility between milk, soya and fish proteins was mainly due to differences in endogenous nitrogen losses and not to differences in true digestibility. In the second part, the pancreatic protease activities of newly weaned piglets fed various dietary protein sources was investigated. It was found that dietary protein source affected trypsin and chymotrypsin activities in pancreatic tissue and jejunal digesta, however, these differences could not explain the differences in endogenous nitrogen losses. It is more likely that other sources of endogenous nitrogen, e.g. the small intestinal wall, are responsible for the differences in protein digestibility observed in young piglets.Furthermore, it was concluded from the experiments described in this thesis, that postweaning feed intake has a greater effect on the development of pancreatic enzyme activities than dietary protein source per se. Young piglets are capable of increasing their pancreatic secretion in response to appropriate stimuli. Stimulating post-weaning feed intake may help to smooth the development of protein digestive capacity in young piglets. In this respect, feed intake patterns may be at least as important as quantitative feed intake

Effects of amylase inhibitor albumin from wheat on the alpha-amylase activity in carp and tilapia

The amylolytic activities of alpha-amylase extracted from Mirror carp (Cyprinus carpio) and Nile tilapia (Oreochromis niloticus) were significantly reduced by purified amylase inhibitor albumin of wheat when tested under in vitro conditions. The action of this inhibitor was rapid and maximum levels of inhibition were attained within 20 minutes. For both carp and tilapia, the enzyme residual activities after inhibition were found to be related inversely to inhibitor concentration and positively to the initial enzyme activity levels. The curvilinear relationships between these parameters were explained by deriving equations of the type: A2 = a+b A1 - c I + d I2 where a, b, c and d are constants, Ai = Initial amylase activity (mU/min), A2 = Residual amylase activity (MU/min), I= Inhibitor concentration as ug protein. Inhibitions were greatest for amylases from gut tissue and ýowest for amylases from gut fluids. 1ug of purified inhibitor was found to contain a potency, to reduce 298 Units of carp gut tissue alpha-amylase and 532 Units of tilapia intestinal tissue alpha-amylase, by 50%. When amylase inhibitor extracted from wheat was incorporated in the feed of carp in its active form for three weeks, it caused a significant reduction in the specific growth rate to only 0.16%/day, while in carp fed autoclaved inhibitort such reduction in growth was not seen and the SGR was maintained at over 1.00%/day. However, despite the presence of active inhibitor in the intestine, the fish were able to maintain alpha-amylase activities in the gut contents at a level similar to that in fish fed denatured inhibitor. This was achieved by hyperactivation of enzyme secretions in the tissues of hepatopancreas and intestine. Hepatopancreas from fish fed active inhibitor exhibited more than two-fold increase in amylase, activity compared to those fed denatured inhibitor. By the third week of the experiment this difference in enzyme activity levels was not apparent but there were also no indications of adaptation or improvement in growth rate. Degenerations in hepatopancreas were also not apparent. Feeding carp with diet containing wheat with its inherent content of inhibitor also caused pancreas hyperactivity and some reduction in growth rate for a short period in comparison to those fish fed autoclaved wheat. In carp, the alpha-amylase activity did not vary depending on the raw or gelatinized nature of starch, both forms elicited equal increases in enzyme activity. However, autoclaving wheat, though effective in inactivating the inhibitor, was found to lower the biological value and digestibility of wheat proteins. Contrary to the result of the carp trials in Nile tilapia, the growth was not significantly reduced by feeding on diet containing active inhibitor and a SGR of 1.57%/day was recorded in comparison to 1.81i/day in tilapia fed denatured inhibitor. Samples of stomach and intestinal contents collected 4 hours after feeding did not reveal the presence of active inhibitor. Apparently the acidic protease, pepsin, in the stomach of tilapia caused the total destruction of the inhibitor in the diet before the contents were passed into the intestinal region. The presence of active amylase inhibitor in tilapia feed did not affect the digestibilities of starch and protein in the diet. Both the groups were able to digest carbohydrates and protein to levels of over 90%. The implications of these results are discussed in relation to feed formulation and fish nutrition

Pea proteins for piglets : effects on digestive processes

White-flowered pea ( Pisum sativum ) contains 20 to 25% crude protein (Nx6.25). The pea proteins consist in globulins (60%) and albumins (25%). Because the pea albumin proteins have biological activities due to their metabolic roles in the seed, some of them are called antinutritional factors (ANFs) for monogastric animals. These are mainly protease inhibitors and lectins. The apparent ileal digestibility of N and amino acids of raw peas fed to piglets was low. The N apparent ileal digestibility of pea protein isolate consisting mainly of globulins without ANFs was 15 units higher. The addition of 3% of pea ANF concentrate decreased the N apparent ileal digestibility by 7 units. This effect is not entirely due to the alleged antinutritional activities of die protease inhibitors or the lectins. This was suggested by the results of the incorporation of another pea ANF concentrate with a higher ANF content than the former concentrate. The albumin proteins themselves were suspected to be low digestible. This was illustrated by the results of a mathematical study of the amino acid composition of ileal digesta from piglets fed a raw pea diet, showing that these amino acids would be mainly of "endogenous + bacterial" origin and partly of dietary origin and especially of albumin type. No relations, neither between N digestibility and pancreatic protease activity in the pancreatic tissue, in its secretions or in the small intestinal digesta, neither between the activities in these different sections of the gastro-intestinal tract could be established. The trypsin and chymotrypsin activity decreased in the jejunal digesta and increased in the ileo-caecal digesta upon addition of pea ANF concentrate to a pea protein isolate diet although the N apparent ileal digestibility was not affected. The enzyme activities in the pancreatic tissue was decreased with a raw pea diet compared to a pea protein isolate diet although equivalent activities were found in the pancreatic secretions. These observations suggested that the mode of action of pea protease inhibitors may depend on the demand of proteases to hydrolyse the dietary proteins in the upper intestine, and on the nutritional quality of the dietary proteins associated with these protease inhibitors