Pancreatin, digestion

Metal binding by corn flakes and grits was measured using the method of Camire and Clydesdale (14). Free amino groups in both cereals were measured after a pepsin-pancreatin digestion (5). 

The free amino content of both cereals was also measured after a pepsin-pancreatin digestion. The corn flakes contained... 

Figure 8-31. Distribution of radioactive materials after paper chromatography of a pancreatin digest of denatured yeast cells which had incorporated S-sulfate from the medium. The chromatogram was run on Whatman 3MM paper and developed in n-butanol-acetic acid-water. Individual strips 0.5 cm long were counted in a liquid scintillation counter. Met, Met-O, O, and F indicate S-methionine, S-methionine sulfoxide, origin, and solvent front, respectively. [From R. Graham and W. M. Stanley, Anal. Biochem., 47 505 (1972).]...

Data from Malagelada et al. (16) provided the basis for choosing a pH of 2 for the pepsin digestion. A final dialysate pH of 7 was chosen for the pancreatin digestion on the basis of the data of Murthy et al. (22). Attempts were made to adjust the... 

The dietary fiber content of various Norwegian wheat flours (9) with different extraction rates were analyzed. To analyze the dietary fiber content we used a gravimetric method, based on digestion of the samples with pepsin and pancreatin. The method is a modification of the procedure described by Hellendorn et al. and modified by Asp et al (10). The pepsin digestion was carried out at pH 1.5 for 1 hr, and the pancreatin digestion at pH 6.8 for 1 hr. 

Lo, W. M. Y. and Li-Chan, E. C. Y. (2005). Angiotensin 1 converting enzyme inhibitory peptides from in vitro pepsin-pancreatin digestion of soy protein. /. Agric. Food Chem. 9, 3369-3376. 

Another subclass of proteases attacks internal peptide bonds and Hberates large peptide fragments. Bromelain, a plant protease derived from the stem of the pineapple plant, can even produce detectable semm proteolysis after oral adrninistration (180). Oral therapy with bromelain significantly reduces bmising that stems from obstetrical manipulations (181). Bromelain—pancreatin combinations have been more effective in digestive insufficiency compared to either pancreatin or placebo (182,183). Bromelain may also enhance the activity of antibiotics, especially tetracycline, when adrninistered concurrently (184). 

Entozyme 18/100 Digestive enymes pancreatin/pepsin/bile salts Robins... 

Digestive Enzymes pancreatin Creon, Digepepsin, 1-2 tablets PO with meals... 

The enzymes pancreatin and pancrelipase, which are manufactured and secreted by the pancreas, are responsible for the breakdown of fats, starches, and proteins. These enzymes are necessary for the breakdown and digestion of food. Both enzymes are available as oral supplements. 

Pancreatin is a pancreatic extract usually obtained from the pancrease of slaughterhouse animals. It contains a mixture of enzymes, principally amylase, protease and lipase, and, thus, exhibits a broad digestive capability. It is administered orally mainly for the treatment of pancreatic insufficiency caused by cystic fibrosis or pancreatitis. As it is sensitive to stomach acid, it must be administered in high doses or, more usually, as enteric-coated granules or capsules that may be taken directly or sprinkled upon the food prior to its ingestion. Individual digestive activities, such as papain, pepsin or bromelains (proteases), or a-amylase are sometimes used in place of pancreatin. 

Exocrine pancreatic insufficiency is most commonly caused by cystic fibrosis, chronic pancreatitis, or pancreatic resection. When secretion of pancreatic enzymes falls below 10% of normal, fat and protein digestion is impaired and can lead to steatorrhea, azotorrhea, vitamin malabsorption, and weight loss. Pancreatic enzyme supplements, which contain a mixture of amylase, lipase, and proteases, are the mainstay of treatment for pancreatic enzyme insufficiency. Two major types of preparations in use are pancreatin and pancrelipase. Pancreatin is an alcohol-derived extract of hog pancreas with relatively low concentrations of lipase and proteolytic enzymes, whereas pancrelipase is an enriched preparation. On a per-weight basis, pancrelipase has approximately 12 times the lipolytic activity and more than 4 times the proteolytic activity of pancreatin. Consequently, pancreatin is no longer in common clinical use. Only pancrelipase is discussed here. 

Uses Type 2 DM Action a-Glucosidase inhibitor delays digestion of carbohydrates Dose Initial 25 mg PO rid maint 50-100 mg rid (w/ 1st bite of each meal) Caution [B, —] Contra DKA, obst/inflammatory GI disorders SCr >2 mg/dL Disp Tabs SE Flatulence, D, abd pain Interactions T Effects W/ celery, coriander, juniper berries, ginseng, garlic X- effects W/ENH, niacin, intestinal absorbents, amylase, pancreatin X- effects OF digoxin, propranolol, ranitidine EMS Can X- digoxin level-monitor ECG in pts on digoxin therapy OD May cause severe adverse GI Sxs symptomatic and supportive... 

Enzymic hydrolysis of PGA by crude extracts of papain and pancreatin was carried out as described by Miller 27). Samples withdrawn at intervals were analyzed for free amino groups using a ninhydrin reaction 41). Values were corrected for the ninhydrin reaction of an enzymic digest which contained no PGA. 

Hydrolytic enzymes Pancreatin Hydrolysis of starch (amylase), fat (lipase), and protein (protease) Porcine pancreas Digestive aid... 

Figure 4, where the curve is the result of opposite effects of colipase and bile salts. Maximum activities am reached in the range of 5-13 mM bile salts, a concentration aiso present in the duodenum during fat digestion, in me FI method for pancreatin lipase, about 10 mM FIP controlled sodium taurocholate is used. 

When pancreatin is administered to patients in some galenic formulation, it mUy with the food mass and performs some digestion in the stomach. However, most... 

Given the uncertainties of the quantities and the precise specificities of many digestive enzymes, notably the endopeptidases, and the surprises that biological systems sometimes throw up (who would have expected chitosan to be hydrolysed by pepsin, pancreatin, a lipase or a-amylase as has been reported (Muzzarelli 1997 Muzzarelli et al. 1995 Yalpani and Pantaleone 1994)) any therapeutic macromolecule or formulation destined for oral use should be... 

Pancreatic enzymes, preferably trypsin, have been used for the chemical characterisation and identification of many known bioactive peptides. For example, ACE-inhibitory peptides as well as CPPs are most commonly produced by trypsin (Maruyama and Suzuki, 1982 Berrocal et al., 1989). On the other hand, other enzymes and different enzyme combinations of proteinases, including alcalase, chymotrypsin, pancreatin and pepsin, as well as enzymes from bacterial and fungal sources have also been utilised to generate bioactive peptides. Higher yields of CPPs and, particularly, higher amounts of asl-casein f(59-79) in the hydrolysate have been obtained with casein micelles successively digested with pepsin and trypsin... 

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