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PMID: 11343882 Published · ppublish English Journal Article

Enzymatic degradation of cross-linked high amylose starch tablets and its effect on in vitro release of sodium diclofenac.

Rahmouni M, Chouinard F, Nekka F, Lenaerts V, Leroux JC

Abstract

The influence of several physicochemical parameters on enzymatic hydrolysis and the in vitro release of sodium diclofenac (SDic) from cross-linked high amylose starch (Contramid) (CLA) tablets was evaluated. These parameters included pH, ionic strength of the medium, enzyme concentration, compression force and incorporation of gel-forming polymers such as hydroxypropyl methylcellulose (HPMC), poly(ethylene oxide) (PEO) and poly(vinyl alcohol) into the tablet. Pure CLA tablets were incubated in phosphate buffer (pH 6.8) containing alpha-amylase and the extent of enzymatic erosion was determined by gravimetry. Release of SDic from CLA tablets, in the presence of alpha-amylase, was measured using a USP type III dissolution apparatus. For low alpha-amylase concentrations (<2250 IU/l), the drug release was mainly diffusion-controlled. At higher alpha-amylase concentrations (>4500 IU/l) both diffusion and erosion contributed to the release of SDic. The hydrolysis kinetics of CLA tablets by alpha-amylase was biphasic. During the first phase (2-4 h), the hydrolysis rate was hyperbolically related to the alpha-amylase concentration but was practically alpha-amylase concentration-independent during the second phase. Enzymatic erosion and drug release kinetics appear to be relatively independent of ionic strength, pre-incubation time in simulated gastric fluid, and compression force of the tablets (6-34 kN). Incorporation of HPMC or PEO into the tablet resulted in a significant decrease of both tablet erosion and drug release rates.

MeSH Terms
Amylose/chemistry,metabolism Anti-Inflammatory Agents, Non-Steroidal/chemistry Chemistry, Pharmaceutical Delayed-Action Preparations Diclofenac/chemistry Enzyme Stability Gastric Acid/metabolism Hydrogen-Ion Concentration Hydrolysis Hypromellose Derivatives Methylcellulose/analogs & derivatives,chemistry Models, Biological Osmolar Concentration Polyvinyl Alcohol/chemistry Pressure Tablets/chemistry Time alpha-Amylases/metabolism
Chemicals
Anti-Inflammatory Agents, Non-Steroidal Delayed-Action Preparations Tablets Diclofenac Hypromellose Derivatives Polyvinyl Alcohol Methylcellulose Amylose alpha-Amylases
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Rahmouni M
Faculté de Pharmacie, Université de Montréal, Québec, Montreal, Canada.
Chouinard F
Nekka F
Lenaerts V
Leroux J C
Article Info
Journal
European journal of pharmaceutics and biopharmaceutics : official journal of Arbeitsgemeinschaft fur Pharmazeutische Verfahrenstechnik e.V
Abbr.
Eur J Pharm Biopharm
ISSN
0939-6411
Published
2001-05-00
Pages
191-8
Language
English
Region
Netherlands
NLM ID
9109778
Subset
IM
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