Pressure‐Induced Activity Loss in Solid State Catalase

Wurster, Dale Eric; Ternik, Robert L.

doi:10.1002/jps.2600840213

Cited by 8 publications

(6 citation statements)

References 27 publications

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“…However, above 190 MPa there is an apparent plateau at an activity loss of about 7%. It is well‐known from previous studies that compaction can successively reduce the activity of proteins, although marked differences were found in the pressure sensitivity of various proteins . The observed activity decrease of about 7% (Fig.…”

Section: Resultsmentioning

confidence: 71%

“…From this perspective, the influence of the tableting process and associated stress on the physical stability of biopharmaceuticals is of increasing interest. A negative influence of the compaction pressure on biological activity has been reported, for example, for α‐amylase and catalase . Furthermore, various studies have been performed using IR spectroscopy to monitor changes in the secondary structure of proteins upon compaction.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Influence of Tableting on the Conformation and Thermal Stability of Trypsin as a Model Protein

Klukkert¹,

Weert

Fano

et al. 2015

Journal of Pharmaceutical Sciences

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Section: Resultsmentioning

confidence: 71%

Section: Introductionmentioning

confidence: 99%

Influence of Tableting on the Conformation and Thermal Stability of Trypsin as a Model Protein

Klukkert¹,

Weert

Fano

et al. 2015

Journal of Pharmaceutical Sciences

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“…The unique protein structure should be maintained during processing, and potential structural changes must affect the functionality of the proteins minimally [ 7 , 8 ]. This has been investigated in several studies in which the activity and structural integrity of proteins after compaction have been analyzed [ 10 , 11 , 12 , 13 , 14 ]. The sensitive protein structure [ 10 , 15 , 16 ] consequently forces most protein products to be formulated as injectable drugs, either liquid formulations ready for injection or freeze-dried powder formulations, reconstituted right before administration to the patient.…”

Section: Introductionmentioning

confidence: 99%

Compaction Properties of Particulate Proteins in Binary Powder Mixtures with Common Excipients

Holmfred,

Hirschberg,

Rantanen

2023

Pharmaceutics

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The increasing interest in protein- and peptide-based oral pharmaceuticals has culminated in the first protein-based products for oral delivery becoming commercially available. This study investigates the compaction properties of proteins in binary mixtures with common excipients up to 30% (w/w) of particulate protein. Two model proteins, lysozyme and bovine serum albumin, were compacted with either microcrystalline cellulose, spray-dried lactose monohydrate, or calcium hydrogen phosphate dihydrate at two different compaction pressures. Compared to the compacted pure materials, a significant increase in the tensile strength of the compacts was observed for the binary blends containing lysozyme together with the brittle excipients. This could be attributed to the increased bonding forces between the particles in the blend compared to the pure materials. The use of bovine serum albumin with a larger particle size resulted in a decrease in tensile strength for all the compacts. The change in the tensile strength with an increasing protein content was non-linear for both proteins. This work highlights the importance of considering the particulate properties of protein powders and that protein-based compacts can be designed with similar principles as small-molecules in terms of their mechanical tablet properties.

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“…Therefore, manufacturing of tablets using the direct compression method (DC) seems to be the most appropriate formulation strategy. Nevertheless, the compression forces (compaction pressures) applied during the tableting process can be a key factor potentially affecting enzyme stability [ 5 , 8 , 9 ]. Schulz et al revealed that compaction pressure induced a reduction in powder volume, which was the main cause of the loss of enzymatic activity of butyrylcholine esterase and peroxidase during tableting [ 10 ].…”

Section: Introductionmentioning

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

Cited by 8 publications

References 27 publications

Influence of Tableting on the Conformation and Thermal Stability of Trypsin as a Model Protein

Influence of Tableting on the Conformation and Thermal Stability of Trypsin as a Model Protein

Compaction Properties of Particulate Proteins in Binary Powder Mixtures with Common Excipients

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

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