Enzymes, digestive

Chymotrypsin (Section 27 10) A digestive enzyme that cat alyzes the hydrolysis of proteins Chymotrypsin selectively catalyzes the cleavage of the peptide bond between the car boxyl group of phenylalanine tyrosine or tryptophan and some other ammo acid... 

Sucrose polyesters, which are made by esterilying sucrose with long-chain fatty acids, have the physical properties of fat, but are resistant to digestive enzymes (40). Olestra, a sucrose polyester developed by Procter Gamble, was submitted for regulatory approval in May 1987. In order to faciUtate the approval process, Procter Gamble has since narrowed the scope of its food additive petition to include olestra s use only in savory and extmded snacks. 

In general, many species of algae have cell walls resistant to digestive enzymes, dark colors, and bitter flavor. AH of these characteristics must be altered to make an acceptable food or feed product. 

From a bioavailabihty standpoint, the fact that a significant amount of nicotinic acid is in a bound form has important biological consequences. Poor bioavailabihty stems from the fact that the ester linkage is resistance to digestive enzymes. In the case of com, this condition can be alleviated if com is pretreated with alkah. This food preparation method is frequently practiced in Mexico for the preparation of tortillas. 

Bile Acid Sequestrants. The bile acid binding resins, colestipol [26658424] and cholestyramine, ate also effective in controlling semm cholesterol levels (150). Cholestyramine, a polymer having mol wt > ICf, is an anion-exchange resin. It is not absorbed in the gastrointestinal tract, is not affected by digestive enzymes, and is taken orally after being suspended in water (151). 

On homogenization, the lysate may drastically increase in viscosity due to DNA release. This can be ameliorated to some extent using multiple passes to reduce the viscosity. Alternatively, precipitants or nucleic acid digesting enzymes can be used to remove these viscosity-enhancing contaminants. 

FIGURE 2.16 pH versus enzymatic activity. The activity of enzymes is very sensitive to pH. The pH optimum of an enzyme is one of its most important characteristics. Pepsin is a protein-digesting enzyme active in the gastric fluid. Trypsin is also a proteolytic enzyme, but it acts in the more alkaline milieu of the small intestine. Lysozyme digests the cell walls of bacteria it is found in tears. 

This is the only function of maltase, but it is one that no other enzyme can perform. Many such digestive enzymes are required for the metabolism of carbohydrates, proteins, and fats. It has been estimated that without enzymes, it would take upward of 50 years to digest a meal. 

AQP10 has only been identified in the small intestine so far and is thought to play a role in hormonal secretion. AQP11 is expressed in kidney, liver, testis and brain, but no function has been found so far. AQP12 has been identified in pancreatic acinar cells, where it is thought to facilitate the release of digestive enzymes into the pancreatic duct. 

Trypsin is a major proteolytic digestive enzyme and the identified endogenous ligand for proteinase-activated receptor 2 (PAR 2). 

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

No adverse reactions have been reported with the use of digestive enzymes however, high doses may cause nausea and diarrhea. 

Calcium carbonate or magnesium hydroxide antacids may decrease the effectiveness of the digestive enzymes. When administered concurrently with an iron preparation, the digestive enzymes decrease the absorption of oral iron preparations. 

These drug are prescribed as replacement therapy for those with pancreatic enzyme insufficiency. Conditions or diseases that may cause a decrease in or absence of pancreatic digestive enzymes include cystic fibrosis, chronic pancreatitis, cancer of the pancreas,... 

DIGESTIVE ENZYMES. When digestive enzymes are given in capsule or enteric-coated tablet form, the nurse... 

There are two main classes of proteolytic digestive enzymes (proteases), with different specificities for the amino acids forming the peptide bond to be hydrolyzed. Endopeptidases hydrolyze peptide bonds between specific amino acids throughout the molecule. They are the first enzymes to act, yielding a larger number of smaller fragments, eg, pepsin in the gastric juice and trypsin, chymotrypsin, and elastase secreted into the small intestine by the pancreas. Exopeptidases catalyze the hydrolysis of peptide bonds, one at a time, fi"om the ends of polypeptides. Carboxypeptidases, secreted in the pancreatic juice, release amino acids from rhe free carboxyl terminal, and aminopeptidases, secreted by the intestinal mucosal cells, release amino acids from the amino terminal. Dipeptides, which are not substrates for exopeptidases, are hydrolyzed in the brush border of intestinal mucosal cells by dipeptidases. 

Hydrolases such as the digestive enzymes amylase and lactase catalyse hydrolysis of glycosides, esters, anhydrides and amides. 

From the above description it will be appreciated that the efficiency of release of nutrients from ingested plant material is dependent upon the ease with which the digestive enzymes can penetrate the cell wall to release the nutrients so that they can diffuse out of the structure to be absorbed. Thus tissue maturity, cooking, macerating, mastication and mode of tissue failure, all of which control particle size, cell wall softening or cell disruption, are key features which regulate nutrient release. 

Diabetic patients have reduced antioxidant defences and suffer from an increased risk of free radical-mediated diseases such as coronary heart disease. EC has a pronounced insulin-like effect on erythrocyte membrane-bound acetylcholinesterase in type II diabetic patients (Rizvi and Zaid, 2001). Tea polyphenols were shown to possess anti-diabetic activity and to be effective both in the prevention and treatment of diabetes (Choi et al, 1998 Yang et al, 1999). The main mechanism by which tea polyphenols appear to lower serum glucose levels is via the inhibition of the activity of the starch digesting enzyme, amylase. Tea inhibits both salivary and intestinal amylase, so that starch is broken down more slowly and the rise in serum glucose is thus reduced. In addition, tea may affect the intestinal absorption of glucose. 

Some of the best investigated anti-nutrients are the enzyme inhibitors present in legumes and other plants. The Bowman-Birk and the Kunitz inhibitors of trypsin and other proteases are among the best characterized. In contrast to the non-specific and widespread influences of tannins and lectins (Carmona, 1996), the Bowman-Birk, Kunitz and other such inhibitors target specific enzymes. Corresponding with this, proteases and other digestive enzymes vary in sensitivity to the different inhibitors. 

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