Application of ultraviolet, visible, and infrared light imaging in protein-based biopharmaceutical formulation characterization and development studies

Klijn, Marieke E.; Hubbuch, Jürgen

doi:10.1016/j.ejpb.2021.05.013

Cited by 12 publications

(7 citation statements)

References 220 publications

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“…Several other studies have since then been published describing work using an infrared camera to monitor freeze-drying processes [ 13 , 14 , 15 , 16 , 17 , 18 , 19 ]. Lietta et al described the use of an infrared camera mounted inside a freeze dryer compared with results from thermocouples when drying a sucrose formulation in glass vials.…”

Section: Introductionmentioning

confidence: 99%

Infrared Thermography for Monitoring of Freeze Drying Processes—Part 2: Monitoring of Temperature on the Surface and Vertically in Cuvettes during Freeze Drying of a Pharmaceutical Formulation

2022

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The coupling of an infrared (IR) camera to a freeze dryer for monitoring of the temperature of a pharmaceutical formulation (sucrose/mannitol solution, 4:1%, m/m) during freeze-drying has been exploited further. The new development allows monitoring of temperatures simultaneously at the surface as well as vertically, (e.g., in depth) along the side using custom-made cuvettes. The IR camera was placed on the chamber roof of a process-scale freeze dryer. Monitoring of cuvettes containing the formulation took place from above where one side of each cuvette was equipped with a germanium window. The Ge-window was placed next to an IR mirror having a 45° angle. The long-wave infrared radiation (LWIR) coming from the inside of the cuvette was reflected upwards toward the IR camera. Accurate recording of the temperature along the cuvettes’ depth profile was therefore possible. Direct imaging from −40 °C to 30 °C took place every 60 s on the surface and on the side with a 2 × 2 mm resolution per IR pixel for 45 h resulting in 2700 thermograms. Results are presented for freeze-drying of a pharmaceutical formulation as a function of time and spatially for the entire side (depth) of the cuvette. As the sublimation process was progressing, the spatial resolution (84 IR pixels for the side-view and 64 pixels for the surface-view) was more than sufficient to reveal lower temperatures deeper down in the material. The results show that the pharmaceutical formulation (a true solution at the onset) dries irregularly and that the sublimation front does not progress evenly through the material. During secondary drying, potential evaporative cooling of upper layers could be detected thanks to the high thermal and spatial resolution.

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Section: Introductionmentioning

confidence: 99%

Infrared Thermography for Monitoring of Freeze Drying Processes—Part 2: Monitoring of Temperature on the Surface and Vertically in Cuvettes during Freeze Drying of a Pharmaceutical Formulation

2022

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“…Fig. 4 shows that in the near ultraviolet region, β-LG shows its characteristic absorption peak around 280 nm; After phlorizin with different molar ratios was added, the absorbance of the complex increased, and the maximum wavelength shifted to red, which indicated that a complex was formed between β-LG and phlorizin, and the polarity of β-LG microenvironment also changed, which may be due to the exposure of aromatic compounds, and the chromogenic amino acids changed the external environment of β-LG (Marieke, & Jürgen, 2021) . With the increase of temperature, the characteristic absorption peak of β-LG shifts blue first and then red, indicating that β-LG may be affected by temperature to change the microenvironment of free Trp residues, and then higher temperature treatment causes the protein structure to expand, and Trp residues transfer to a more hydrophilic or polar microenvironment (Loveday, 2016); Compared with β-LG, the ultraviolet absorption peaks of phloridzin and β-lactoglobulin mixed system also shifted red, and the ultraviolet absorption peaks of the complex were significantly enhanced.…”

Section: Determination Of Antigenicitymentioning

confidence: 99%

Interaction Mechanism of β-lactoglobulin and Phlorizin Under Thermal Processing and the Effect of Immune Attenuation

Xue,

Zhang,

et al. 2023

Preprint

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βlactoglobulin (β-LG) is an important whey protein because of its high ability to bind hydrophobic small molecules. Phlorizin is a kind of apple polyphenol. The interaction mechanism between phlorizin and β-lactoglobulin in the milk system and the effect of phlorizin on β-LG after thermal processing are still unclear. Therefore, the interaction mechanism between β-LG and phlorizin and the structural and antigenic changes of the compound under different thermal processing was studied. Firstly, the binding mode of phlorizin and β-LG was simulated by molecular docking, and the binding mechanism of phlorizin and β-LG conformation changes were explored by spectroscopy. Indirect ELISA was used to evaluate the effect of phlorizin on the reduction of β-LG antigen. Phroside interacts with β-LG mainly by static quenching and hydrophobic force. Due to the addition of phlorizin, the hydrophobic groups on the surface of the compound heated at 100℃ were hidden, and the hydrophobic interaction between phlorizin and β-LG was weakened. And the addition of phlorizin after thermal processing changed the secondary structure of β-LG, β-sheet, and random coil were reducing, and α-helix was increasing. Phlorizin reduced the antigenicity of β-LG, but there was no significant difference between thermal processing under 100℃.

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“…Spectroscopy is known to be a powerful technique in monitoring processes. It has been widely used to determine and monitor detailed information about proteins' primary, secondary, tertiary, and quaternary structures [23], using different regions of the electromagnetic spectrum, such as the ultraviolet (UV; 190-380 nm), visible (Vis; 380-750 nm), or mid-infrared (MIR; 2.5-30 µm) light regions [54]. Using visible or near-infrared (NIR; 750 nm-2.5 µm) radiation, Raman spectroscopy is a non-invasive inline method which provides data of the chemical composition and molecular structure of small and large (bio)molecules.…”

Section: Liquid-phase Monitoring In Protein Crystallization Processesmentioning

confidence: 99%

Recent Advances in the Monitoring of Protein Crystallization Processes in Downstream Processing

Walla,

Bischoff,

Corona Viramontes

et al. 2023

Crystals

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Protein crystallization is nowadays performed at the micro to macro scale in academia and industry, being particularly interesting for pharmaceutical applications. Protein crystallization offers an attractive alternative to chromatography as a downstream processing step in the biotechnology industry, but also in the food and chemical industries. Monitoring of the protein crystallization process is required to understand the crystal growth mechanism and to obtain the information necessary for efficient process control, which needs to comply with the critical quality attributes of the product. Since a wide range of monitoring techniques have already been developed and established, this review focuses on the recent advances of selected techniques in monitoring protein crystallization processes such as the focused beam reflectance method (FBRM), and machine learning-based image analysis for solid-phase monitoring, as well as the spectroscopic methods for liquid-phase monitoring, such as attenuated total reflectance Fourier transform infrared (ATR-FTIR) and UV/Vis spectroscopy.

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Application of ultraviolet, visible, and infrared light imaging in protein-based biopharmaceutical formulation characterization and development studies

Cited by 12 publications

References 220 publications

Infrared Thermography for Monitoring of Freeze Drying Processes—Part 2: Monitoring of Temperature on the Surface and Vertically in Cuvettes during Freeze Drying of a Pharmaceutical Formulation

Infrared Thermography for Monitoring of Freeze Drying Processes—Part 2: Monitoring of Temperature on the Surface and Vertically in Cuvettes during Freeze Drying of a Pharmaceutical Formulation

Interaction Mechanism of β-lactoglobulin and Phlorizin Under Thermal Processing and the Effect of Immune Attenuation

Recent Advances in the Monitoring of Protein Crystallization Processes in Downstream Processing

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