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High potency pancreatin pharmaceutical compositions

A technology of composition and pancreatin, which is applied in the directions of drug combination, pancreatin, medical preparations containing active ingredients, etc., can solve the problem of no separate purification and the like

Pending Publication Date: 2016-03-09
APTALIS PHARMA
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

Similarly, there is no motivation or report for the separate purification and subsequent recombination of enzymes from pancreatic origin; such an approach would defeat the purpose of achieving an isolated enzyme or enzymes

Method used

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  • High potency pancreatin pharmaceutical compositions
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Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0093] Example 1 Preparation of HA trypsin; 0.1g / mL; multi-step: suspension, separation, precipitation; (SP=38: acetone: aqueous solvent = 35:65; ethanol: solvent aqueous solvent = 45:55)

[0094] Step a1.1 - Suspension: The starting pancrelipase was dispersed in an aqueous solvent at a concentration of 0.1 g / mL at 4°C and kept under stirring for 30 minutes. Experiments were performed at laboratory scale using 650 mg (when the organic solvent was acetone) or 550 mg (when the organic solvent was ethanol) of starting pancreatic lipase. Four different aqueous solvents were tested for pancrelipase suspension: 1) pH=4.0 buffer (10 mM acetate buffer); 2) pH=7.0 buffer (10 mM phosphate); 3) deionized water (DW); 4) pH = 4.0 buffer (10 mM acetate) containing NaCl (0.5M).

[0095] Step a1.2 - Separation: The suspension from step a1.1 was centrifuged (10 min, 4°C, about 11,000 g) and the supernatant (SN) was separated from the pellet.

[0096] Step a1.3 - Precipitation: An organic s...

Embodiment 2

[0116] Example 2 Preparation of HA trypsin; 0.3g / mL; multi-step: suspension, separation, precipitation (SP=38: acetone: aqueous solvent = 35:65; ethanol: aqueous solvent = 45:55)

[0117] Step a1.1 - Suspension: Pancrelipase (API) was dispersed in an aqueous solvent at a concentration of 0.3 g / mL at 4°C and stirred for 30 minutes. Experiments were performed at laboratory scale using 650 mg (when the organic solvent was acetone) or 550 mg (when the organic solvent was ethanol) of starting pancreatic lipase. Two experiments were each run in different aqueous solvents: 1) pH=4.0 buffer (10 mM acetate buffer); 2) pH=7.0 buffer (10 mM phosphate).

[0118] Step a1.2 - Isolation: The suspension from step a1 was centrifuged (10 min, 4°C, about 11,000 g) and the supernatant (SN) was separated from the pellet.

[0119] Step a1.3 - Precipitation: An organic solvent was added to the supernatant of step a1.2 and the mixture was kept at rest at 4°C for 15 minutes. Described organic solv...

Embodiment 3

[0139] Example 3 Preparation of HA-trypsin; 0.1g / mL; two steps: suspension, precipitation (SP=38: acetone: aqueous solvent = 35:65; ethanol: aqueous solvent = 45:55, where SP (acetone) = 20.2, SP (Ethanol) = 26.0, SP (buffer) = 47.9)

[0140] Step a1.1 - Suspension: Pancrelipase was dispersed in an aqueous solvent at a concentration of 0.1 g / mL at 4°C and kept under stirring for 30 minutes. Experiments were performed at laboratory scale using 650 mg (when the organic solvent was acetone) or 550 mg (when the organic solvent was ethanol) of starting pancreatic lipase. Two experiments were each run in different aqueous solvents: 1) pH=4.0, 10 mM acetate buffer; 2) pH=7.0, 10 mM phosphate buffer.

[0141]Step a1.2 - Precipitation: An organic solvent is added to the suspension of step a1.1 and this mixture is kept at 4°C for 15 minutes. Described organic solvent is acetone or ethanol. Acetone was added in an amount of 35 parts (volume) per 65 parts (volume) of aqueous solvent....

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Abstract

The present invention provides high potency pharmaceutical compositions comprising high activity pancreatin enzymes. The invention is also directed to a process of producing HA- pancreatin enzymes and its compositions or dosage forms, and methods for their use.

Description

[0001] Related cross application [0002] This application claims the benefit under 35 USC §119(e) of US Provisional Patent Application Serial No.: 61 / 856,952, filed July 22, 2013, the disclosure of which is incorporated herein by reference in its entirety for all purposes. field of invention [0003] The present invention relates to a highly effective pharmaceutical composition comprising high activity pancreatin (high activity pancreatin, HA-pancreatin) enzyme. The present invention also relates to methods of producing HA-trypsinase, compositions or dosage forms thereof, and methods of using them. Background of the invention [0004] The FDA estimates that more than 200,000 Americans suffer from exocrine pancreatic insufficiency (EPI), which includes a physiological disorder in which individuals cannot digest food well due to a lack of digestive enzymes produced by their pancreas. Loss of such digestive enzymes leads to disorders such as nutrient maldigestion and malabsor...

Claims

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Application Information

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Patent Type & Authority Applications(China)
IPC IPC(8): A61K38/46A61K38/48C12N9/94A61P1/18
CPCA61K38/465A61K38/48C12N9/94A61K38/54A61P1/18A61K38/46A61K9/50
Inventor 温琴扎·皮隆蒂罗伯特·贝克尔路易吉·波尔特里路易吉·吉多斯保拉·阿尔祖菲
Owner APTALIS PHARMA
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