Drug – bio-affecting and body treating compositions – Enzyme or coenzyme containing – Multienzyme complexes or mixtures of enzymes
Patent
1998-02-25
2000-04-18
Witz, Jean C.
Drug, bio-affecting and body treating compositions
Enzyme or coenzyme containing
Multienzyme complexes or mixtures of enzymes
424 941, 424 9421, 424 946, 424 9461, A61K 3854
Patent
active
060512202
DESCRIPTION:
BRIEF SUMMARY
The present invention relates to a composition for the improvement of digestibility and utilisation of nutrients. The invention also relates to the use of fungal acid stable amylase and acid stable lipase for the treatment of clinical conditions associated with an inadequate digestive capacity such as exocrine pancreas insufficiency and in the preparation of these compositions.
The efficiency with which nutrients are absorbed (and thus utilized) by the human and animal body depends among other things on the efficiency of digestion. Digestion is inter alia mediated by various enzymes that have specific functions at various locations in the digestive tract. Impairment of the activity of these enzymes will have an influence on the degradation of the food constituents and consequently on the up-take of nutrients. An impaired up-take will inter alia result in reduced growth.
In the whole process of digestion the pancreas has an important role. It secretes a juice having two major components, an alkaline fluid and enzymes, into the duodenum. The two components occur in variable proportions depending on the stimuli. The alkaline fluid component, ranging in volume from 200-800 ml/day, has a high concentration of bicarbonate, which neutralizes the gastric content entering the duodenum and helps to regulate the pH of the intestinal tract.
The enzymes of pancreatic juice are synthesized and secreted by the acinar cells which also secrete a fluid similar in electrolyte composition to an ultrafiltrate of plasma. In intermittent feeders such as man, dog and cat, the volume of the fluid secreted by the acinar cells is very small and it has little effect upon the volume and composition of pancreatic juice flowing in the main pancreatic duct.
The pancreatic juice contains four major enzyme groups: lipolytic, proteolytic, amylolytic and nucleic acid splitting enzymes. These pancreatic enzymes, some of them are secreted in multiple forms, possess specifities complementary to the intestinal membrane bound enzymes. Fresh, uncontaminated pancreatic juice is without proteolytic activity because these enzymes are in the form of inactive zymogens. An important fraction of the calcium in pancreatic juice accompanies the enzymes, especially alpha-amylase. The human pancreatic juice is most close to that of the pig with a high content of lipase and alpha-amylase with regard to other mammalia [1]. Therefore, pig pancreas extract, called pancreatin, has been up to now the preferred enzyme source for therapeutic exocrine pancreas substitution.
The major groups of patients requiring provision of digestive enzymes are those with acquired chronic pancreatitis, mostly secondary to alcoholism, children and adults with cystic fibrosis, and patients with pancreatic carcinomas. Exocrine pancreas insufficiency occurs in the majority of cystic fibrosis patients leading to a chronic steatorrhoea and a high incidence of a status of undernutrition, which is related to the severity of pulmonary disease and also to morbidity and mortality [2].
The final aim of exocrine pancreas substitution therapy is to eliminate the malabsorption and to maintain an adequate nutrition. Treatment of exocrine insufficiency of the pancreas ought to be relatively easy, by administering an extract of mammalian pancreas, such as porcine pancreas. Unfortunately adequate treatment proved to be difficult to manage and large variations in the degree of pancreas enzyme substitution have been reported notwithstanding the availability of potent porcine pancreatic extracts and the intake of often very high doses. Problems inherent to these pancreatin preparations themselves, as well as particularities in the environment in which the enzymes are expected to work, are to be considered [3].
The intragastric predigestion by gastric lipase [4] is not impaired in patients with exocrine pancreas insufficiency. For the completion of the digestion in the duodenum, the acid gastric content must be brought by means of pancreatic bicarbonate to a considerably higher pH value, because the pH o
REFERENCES:
patent: 5260074 (1993-11-01), Sipos
Therapiewoche (1977), 27(52), 9358-64, 1977, XP000604944. Weber, G. et al.: "Enzymsubstitution und digestive Leistung".
Fortschritte Der Medizin, vol. 96, No. 38, 1978, 1941-1943. XP000604943, Zorn, J.: "Erfahrungen bei der Substitutionstherapie mit einem neuen Pankreasferment-Praparat pflanzlicher Herkunft".
Griffen et al. "Acid resistant lipase as replacement therapy in chronic pancreatic exocrine insufficiency," Gut (1978) 96(38): 1941-43.
Uyttenbroeck et al. "Molecular characterization of an extracellular acid-resistant lipase produced by Rhizopus javanicus," Biol. Chem. Hoppe-Seyler (1993) 374(4): 245-54.
Minoda et al. "Acid-stable alpha-amylase of black Aspergilli. Part V. Amino acid composition and amino-terminal amino acid," Agri. Biol. Chem. (1969) 33(4): 572-78.
Minoda et al. Agric. Biol. Chem. (1968) 32(1): 104-109.
Medzyme N.V. and Simon Lodewijk Scharpe
Witz Jean C.
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