THE EFFECT OF TOXICANTS ON THE MEMBRANE HYDROLYSIS OF THE DIGESTIVE TRACT IN ANIMALS

Beef tallow was hydrolyzed to produce a series of fats with 3, 10, 20, 46, and 100% free fatty acids, which were incorporated at the level of 10% into semipurified diets. These diets along with a low-fat control diet were each fed to five piglets from 10 to 22 days of age. Tridodecyl glycerol ether was used as an indicator of fat absorption. Feces samples were collected between 19 and 22 days of age and the pigs were killed to allow samples of digesta to be collected. Analysis of feces and digesta allowed the progress of fat absorption to be monitored through the digestive tract. The corrected absorbability of the total lipid was between 88 and 93% for the partially hydrolyzed tallows, but was only 75% for the completely hydrolyzed tallow. The oleic acid was well absorbed (95–99%) in all the diets; palmitic and stearic acids were also well absorbed in the intact and partially hydrolyzed tallow (82–84% and 63–77%, respectively, for the palmitic and stearic acids), but their absorption was impaired in the completely hydrolyzed tallow (62% and 38%, respectively, for the palmitic and stearic acids).The flow of fatty acid through the digestive tract showed that the small intestine is the major site of fat uptake. Comparison of the amounts of fatty acids in the ileal digesta and in the feces showed that there was no change in the total amount of fat in the digesta as it passed through the large intestine.

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Hydrolysis of poly-L-methionyl proteins by some enzymes of the digestive tract

Journal of Agricultural and Food Chemistry ◽

10.1021/jf00068a037 ◽

1986 ◽

Vol 34 (2) ◽

pp. 291-297 ◽

Cited By ~ 1

Author(s):

Hubert F. Gaertner ◽

Antoine J. Puigserver

Keyword(s):

Digestive Tract ◽

Hydrolysis Of

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Mechanism of clearance of dipeptides by perfused hindquarters: sarcolemmal hydrolysis of peptides

AJP Endocrinology and Metabolism ◽

10.1152/ajpendo.1990.259.4.e463 ◽

1990 ◽

Vol 259 (4) ◽

pp. E463-E469

Author(s):

M. Raghunath ◽

E. L. Morse ◽

S. A. Adibi

Keyword(s):

Skeletal Muscle ◽

Amino Acids ◽

Plasma Membrane ◽

Present Experiment ◽

Hydrolase Activity ◽

Net Uptake ◽

Membrane Hydrolysis ◽

Peptide Hydrolases ◽

Hydrolysis Of ◽

Sarcolemmal Vesicles

The objective of the present experiment was to investigate the mechanism of clearance of a load of dipeptides (10 mumols) by perfused hindquarters of rats. The clearance was progressive over 60 min and was significantly (P less than 0.01) greater for glycylleucine than for glycylglycine (99 vs. 58% disappearance from the medium). Insulin had no significant effect on clearance of these dipeptides but stimulated the net uptake of their constituent amino acids. Investigation of the fate of peptides considered resistant to membrane hydrolysis showed a modest (24%) clearance for glycylsarcosine but a substantial one (89%) for glycylproline. Investigation of hydrolysis by sarcolemmal vesicles of skeletal muscle showed hydrolase activity against glycylglycine and glycylleucine but none against glycylsarcosine and glycylproline. Investigation of hydrolysis in the medium previously used to perfuse hindquarters for 60 min showed considerable activity against glycylleucine and glycylproline but none against glycylglycine and glycylsarcosine. These activities were entirely abolished by p-hydroxymercuribenzoate, an inhibitor of cytoplasmic peptide hydrolases. In conclusion, our data show that the mechanism of clearance of dipeptides by the perfused hindquarters is largely by hydrolysis, and the site of this hydrolysis differs for different dipeptides; hydrolysis is mediated either by plasma membrane enzymes, cytoplasmic enzymes released into the medium, or a combination of both.

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Enhanced hydrolysis of phosphatidylcholine by human group II non-pancreatic secreted phospholipase A2 as a result of interfacial activation by specific anions. Potential role of cholesterol sulphate

Biochemical Journal ◽

10.1042/bj3080507 ◽

1995 ◽

Vol 308 (2) ◽

pp. 507-512 ◽

Cited By ~ 21

Author(s):

A R Kinkaid ◽

D C Wilton

Keyword(s):

Phospholipase A2 ◽

Anionic Phospholipid ◽

Interfacial Activation ◽

Secreted Phospholipase A2 ◽

Cell Plasma ◽

Membrane Hydrolysis ◽

Membrane Bound ◽

Group Ii ◽

Hydrolysis Of

The extracellular concentration of the Group II human non-pancreatic secreted phospholipase A2 (hnpsPLA2) is elevated in a variety of inflammatory disorders. This enzyme is remarkable because it demonstrates almost zero activity with egg phosphatidylcholine (PC) or synthetic dioleoyl-phosphatidylcholine (DOPC) as substrate, but expresses high activity with the anionic phospholipid dioleoyl-phosphatidylglycerol (DOPG), a feature shared with the Group II enzyme from rat liver. The presence of certain membrane-bound anions can enhance hydrolysis of PC by the mammalian secreted PLA2S. In this study the ability of various non-polar anions to stimulate DOPC hydrolysis by secreted PLA2S has been investigated. The naturally occurring membrane anion, cholesterol sulphate, was particularly effective in stimulating the hydrolysis of both DOPC and also 1-stearoyl-2-arachidonyl phosphatidylcholine by hnpsPLA2. Activation of DOPC hydrolysis was also achieved with dioleoyl-phosphatidylserine (DOPS); however, DOPS was less effective than cholesterol sulphate. In contrast, the dianion dioleoyl-phosphatidic acid, a known activator of pig pancreatic PLA2, failed to activate the human enzyme. It remains to be established whether cell plasma-membrane hydrolysis by extracellular hnpsPLA2 can be activated in vivo by the presence of suitable membrane anions such as cholesterol sulphate and thus promote an inflammatory response within the cell.

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Digestion in the pig between 7 and 35 d of age 6. The digestion of hydrolyzed milk and soya-bean proteins

British Journal Of Nutrition ◽

10.1079/bjn19810008 ◽

1981 ◽

Vol 46 (1) ◽

pp. 59-69 ◽

Cited By ~ 20

Author(s):

Jane Leibholz

Keyword(s):

Digestive Tract ◽

Milk Protein ◽

Soya Bean ◽

Partial Hydrolysis ◽

Major Protein ◽

Total N ◽

Intact Proteins ◽

Hydrolyzed Protein ◽

Protein Diets ◽

Hydrolysis Of

1. Four pelleted diets were prepared containing milk or isolated soya-bean protein (ISP) as the major protein source. The milk and ISP were given either as intact proteins or partially (0·65) hydrolyzed with papain before feeding.2. The diets were given ad lib. to thirty-two pigs from 7–28 d of age. The pigs were slaughtered at 28 d of age.3. Weight gains, food conversion ratios and nitrogen balances of pigs given diets containing milk protein were better than those of diets containing ISP (231 g/d, 0·80 and 11·5 g/d compared to 209 g/d, 0·88 and 9·00 g/d respectively)4. Partial hydrolysis of proteins before feeding did not affect the performance of the pigs.5. Apparent digestibilities of N before the ileum and in the whole tract were 0·78 and 0.94 for the pigs given the ISP diets and 0·86 and 0·97 for the pigs given the milk-protein diets.6. Retention time of ISP diets in the whole digestive tract was 1475 min and that of the milk-protein diets was 1089min.7. pH of digesta in the stomach was 5·0–5·3 for all diets and increased to 6·9–7.1 in the ileum.8. There were no differences in flows of total N and protein N to the ileum and lower digestive tract between the pigs given the intact- and hydrolyzed-protein diets.9. Apparent absorptions of N in the stomach, duodenum and jejenum were greater in the pigs given diets containing hydrolyzed proteins than in those given diets containing the intact proteins.10. Flows of total N and protein N to the ileum tract were greater when the pigs were given the ISP diets than when they were given the milk-protein diets.11. Hydrolysis of proteins before feeding resulted in a reduced trypsin and chymotrypsin activity in the duodenum and pancreas.12. Retention of dietary N in the carcass was greater in pigs given the milk-protein diets (0·79) than in those given the ISP diets (0·68).

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Nuclear Membrane Hydrolysis of Adenosine Triphosphate

Nature ◽

10.1038/212609a0 ◽

1966 ◽

Vol 212 (5062) ◽

pp. 609-609 ◽

Cited By ~ 24

Author(s):

R. L. KLEIN ◽

B. A. AFZELIUS

Keyword(s):

Adenosine Triphosphate ◽

Nuclear Membrane ◽

Membrane Hydrolysis ◽

Hydrolysis Of

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Brush border membrane hydrolysis of S-benzyl-cysteine-p-nitroanilide, an activity of aminopeptidase M

Biochemical and Biophysical Research Communications ◽

10.1016/0006-291x(80)90050-9 ◽

1980 ◽

Vol 96 (3) ◽

pp. 991-996 ◽

Cited By ~ 27

Author(s):

Barbara B. Rankin ◽

Thomas M. McIntyre ◽

Norman P. Curthoys

Keyword(s):

Brush Border ◽

Brush Border Membrane ◽

Aminopeptidase M ◽

Membrane Hydrolysis ◽

Hydrolysis Of

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Produksi dan Pemurnian Xilooligosakarida dari Xilan Tongkol Jagung menggunakan Xilanase Streptomyces P26B4 dan Khamir IP4

Jurnal Ilmu Pertanian Indonesia ◽

10.18343/jipi.26.2.309 ◽

2021 ◽

Vol 26 (2) ◽

pp. 309-317

Author(s):

Andika Susantri ◽

Titi Candra Sunarti ◽

Anja Meryandini

Keyword(s):

Digestive Tract ◽

Reducing Sugars ◽

Degree Of Polymerization ◽

Sugar Component ◽

Corn Cobs ◽

Xylan Hydrolysis ◽

Hydrolysis Products ◽

Before And After ◽

Hydrolysis Of

Xylooligosaccharides (XOS) are sugar oligomers from xylan that can be used as prebiotics to improve digestive tract health. Xylan can be extracted from corncobs which are a by-product of agriculture. The purpose of this study was to produce XOS through hydrolysis of corn cobs xylan using Streptomyces P26B4 xylanase. The products of hydrolysis also consisted of monomer xylose; for that xilooligosaccharides were purified using yeast IP4. The xylan hydrolysis products are quantitatively analyzed based on the value of reducing sugars and degree of polymerization (DP), strengthened qualitatively with TLC. Sugar component was analyzed after the addition of yeast by HPLC. P26B4 xylanase isolates had the highest activity on the 7th day incubation, pH 5,5 buffer citrate and temperature of 50°C. The lowest DP value of xylan hydrolysis was 2.49 at a concentration of 6%, and the 24th hour of incubation. TLC chromatograms showed that xylose and XOS products were produced. Purification of XOS at 6%, showed a decreasing in the area of xylose before and after receiving yeast respectively 1.87% and 1.41%.Therefore, yeast IP4 has the potential to consume xylose amnd purify the XOS. Keywords: corncobs xylan, IP4 yeast, purification, Streptomyces P26B4 xylanase, xylooligosaccharides

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Hydrolysis of phytic acid and its availability in rabbits

British Journal Of Nutrition ◽

10.1079/bjn2002785 ◽

2003 ◽

Vol 89 (3) ◽

pp. 287-294 ◽

Cited By ~ 12

Author(s):

M. Marounek ◽

D. Dušková ◽

V. Skřivanová

Keyword(s):

Digestive Tract ◽

Phytic Acid ◽

Physiological Saline ◽

Phytase Activity ◽

Highly Active ◽

P Concentration ◽

Hydrolysis Of ◽

Inorganic Phosphates ◽

Total P

Twenty weaned rabbits were fed ad libitum two granulated feeds containing lucerne meal, barley, oats, wheat bran, oilseed meals and sugarbeet pulp in different proportions. Phytate P in these feeds represented 28·6 and 29·3 % of the total P. Digestibility trials were carried out in rabbits 7 and 10 weeks old. Digestibility of phytate P was 82·1 %, on average. Apparent digestibility of total P was 48·1 and 35·5 % in rabbits aged 7 and 10 weeks, respectively. Concentration of P in the faecal DM of these rabbits averaged 11·9 and 14·7 m/. Most of the faecal P was phosphates P (68·1 %). Proportion of phytate P in total faecal P was 9·0 %. Age effect on total P digestibility and faecal P concentration was significant (P<0·05). In five in vitro experiments twenty-four rabbits were killed at the age of 11 weeks, digesta samples diluted with physiological saline containing phytic acid and incubated anaerobically. Calculations of phytase activity in segments of the digestive tract were based on the estimation of phytic acid hydrolysed during the first 2 h of incubation. The caecum contained 58·6 % of the phytase activity of the digestive tract. Corresponding relative values for the phytase activity in the stomach, small intestine and colon were 22·3, 7·7 and 11·4 %, respectively. In incubations of the caecal contents, phytic acid was hydrolysed more rapidly at pH 5–6 than in the neutral pH region. The hydrolysis was inhibited by Ca cations, and to a small extent also by phosphate anions. Commercial fungal phytase (Natuphos®) was highly active in incubations of the contents of the stomach at pH 1·9. It can be concluded that phytic acid is hydrolysed quite efficiently in the digestive tract of rabbits. This hydrolysis occurred mainly in the caecum. Absorption of soluble inorganic phosphates in the gut is incomplete.

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