Measurement of the Thermal Energy Evolved upon Tablet Compression

Wurster, Dale Eric; Creekmore, J. Richard

doi:10.3109/03639048609065874

Cited by 12 publications

(2 citation statements)

References 3 publications

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“…The problems are not expected to arise from temperature development in die for tablet compaction of dry enzyme powder. Temperature rise over 80°C during compression is not probable [ 14 , 15 ]. Hence, possible activity loss during compression may not derive from warming in die.…”

Section: Resultsmentioning

confidence: 99%

Influence of Tableting on Enzymatic Activity of Papain along with Determination of Its Percolation Threshold with Microcrystalline Cellulose

Sharma

Majumdar

2014

International Scholarly Research Notices

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The binary mixture tablets of papain and microcrystalline cellulose (MCC), dicalcium phosphate dihydrate (DCP), carrageenan, tragacanth, and agar were prepared by direct compression. Carrageenan, tragacanth, and agar provided maximum protection to enzyme activity compared to MCC and DCP. However, stability studies indicated highest loss of enzyme activity with carrageenan, tragacanth, and agar. Therefore, compression behaviour of different binary mixtures of papain with MCC at different compaction pressures, that is, 40–280 MPa, was studied according to Heckel equation. The compressibility studies of binary mixtures indicated brittle behavior of papain. The application of percolation theory on the relationship between critical density as a function of enzyme activity and mixture composition revealed the presence of percolation threshold for binary mixture. Papain-MCC mixture composition showed significant percolation threshold at 18.48% (w/w) papain loading. Microcrystalline cellulose provided higher protection during stability study. However, higher concentrations of microcrystalline cellulose, probably as dominant particles, do not protect the enzyme with their plastic deformation. Below the percolation threshold, that is, 18.48% (w/w) papain amount in mixture with plastic excipient, activity loss increases strongly because of higher shearing forces during compaction due to system dominance of plastic particles. This mixture range should therefore be avoided to get robust formulation of papain.

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Section: Resultsmentioning

confidence: 99%

Influence of Tableting on Enzymatic Activity of Papain along with Determination of Its Percolation Threshold with Microcrystalline Cellulose

Sharma

Majumdar

2014

International Scholarly Research Notices

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“…The latter aspect is extremely important because, as previously reported, pancreatin, being an enzyme, can be inactivated at temperatures too high [ 1 , 2 ] and tableting is a process that generates large amounts of heat energy [ 29 , 30 , 31 ]. To monitor this factor, the study employed a thermal imaging camera, which allowed recording the maximum surface temperatures of the tablets immediately after they were ejected from the tablet press die.…”

Section: Discussionmentioning

confidence: 99%

Effect of Compaction Pressure on the Enzymatic Activity of Pancreatin in Directly Compressible Formulations

Zakowiecki,

Edinger,

Hess

et al. 2023

Pharmaceutics

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Tableting of biomolecules is a challenging formulation phase due to their sensitivity to various process parameters, such as compression pressure, process dynamics, or the temperature generated. In the present study, pancreatin was employed as a model enzyme mixture, which was formulated in tablet form utilizing the synergistic effects of brittle and plastic excipients (dibasic calcium phosphate and microcrystalline cellulose, respectively). The effect of varying compaction pressure and lubricant concentration on the generated temperature and enzymatic activity was evaluated. The tablets were analyzed for pancreatin content and the activity of two enzymes (protease and amylase) using pharmacopoeial tests. This study indicated that the formulations proposed here allow tableting over a wide range of compaction pressures without adversely affecting pancreatin content and its enzymatic activity.

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Pressure‐Induced Activity Loss in Solid State Catalase

Wurster

Ternik

1995

Journal of Pharmaceutical Sciences

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Measurement of the Thermal Energy Evolved upon Tablet Compression

Cited by 12 publications

References 3 publications

Influence of Tableting on Enzymatic Activity of Papain along with Determination of Its Percolation Threshold with Microcrystalline Cellulose

Influence of Tableting on Enzymatic Activity of Papain along with Determination of Its Percolation Threshold with Microcrystalline Cellulose

Effect of Compaction Pressure on the Enzymatic Activity of Pancreatin in Directly Compressible Formulations

Pressure‐Induced Activity Loss in Solid State Catalase

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