Monipa focuses on simplified bioprocess monitoring: our measurement system is based on MIR spectroscopy and monitors multiple bioprocesses inline at the same time. Spectroscopy is a powerful technique that allows the analysis of various relevent parameters. There are applications for Monipa in both upstream bioprocessing; in metabolite monitoring and control, as well as in downstream bioprocessing to aid in aggregation studies, contaminant detection or monitoring of target proteins and excipients.
Our Single use Flow Cell
The single use flow cell is beside Monipa a core element. It is mounted to Monipa with an easy screw mechanism that enables a stable fixation. At the same time it allows the replacement of the flow cell after each monitored process, reducing contamination risk. The flow cell contains our single use silicon ATR crystal, enabling a disposable unit. By connecting the flow cell via loop to e.g. the bioreactor or a chromatography column, different parameters can be monitored online or inline. Stable measurement conditions are achieved due to the external flow cell, that is mounted e.g. outside of the bioreactor. This prevents disturbances of the measurements by gas bubbles or by the stirrer which both can occur inside the bioreactor.
No Calibration Model Building
Calibration model building is an important step for spectroscopic devices. The spectra depends on the molecules in the measured samples. Different cell lines, cell culture media, metabolite or nutrient concentration leads to changes in the spectra. Calibration models are built by correlating the spectroscopic measurements to the reference method.
IRUBIS inline and online monitoring solution Monipa offers an innovative approach to solve the time extensive and costly calibration model building. IRUBIS one point calibration is based on a relative measurement. Only the known start-value of the parameter need to be included. The measurement of reference processes for calibration model building are not necessary.
Monitoring and Control in Bioreactors
The use of mid-infrared (MIR) spectroscopy for inline measurement of glucose and lactate in mammalian cell cultures has already been demonstrated in recent studies (Sandor et al., 2013; Wu et al., 2015). To point out, drawbacks are high equipment costs and low robustness of the ATR probes. IRUBIS has managed to solve many of these teething issues with our Monipa system.
Benefits in Upstream Processing
24/7 inline monitoring of metabolites and nutrients as well as glucose control
Real-time data and glucose control (closed loop)
Single use flow cell decreases contamination risk
Parallel monitoring of up to 6 bioreactors
Increased robustness compared to other spectroscopic methods
Reduced calibration time
Suitable to to a variety of different cell types; from CHO mammalian cells, to microorganisms such as bacteria
Monipa in Upstream Processing: Schematic Overview
Inline Monitoring in Downstream Processing
There are a variety of different applications of Monipa in downstream processing, especially taking into account its fast acquisition time of less than 1 second per spectra. Such applications include protein concentration and aggregation monitoring as well as monitoring of antibody conjugates and excipients.
MIR Spectroscopy in Ultrafiltration and Diafiltration
A few studies using MIR Spectroscopy have been done in the field. In this case, the publication shows the measurement of the concentration of excipients and proteins comparing MIR spectroscopy to the current UV-Vis and HPLC methods. The publication shows that there is less than a 5% deviation between using MIR spectroscopy or UV-Vis /UPLC for Dia- and Ultrafiltration uses.
Wasalathanthri et.al, Journal of Biotechnology and Bioengineering (2020)
Protein Secondary Structure
MIR spectroscopy enables differentiation of protein secondary structure such as alpha helices, beta sheets and random coil structures. In particular, a distinct feature of protein aggregation is the increase of crossed β-sheet structures. Hence, IR Spectroscopy is a useful tool to analyze secondary structures of proteins, and their aggregation in complex samples.
Wang et al (2015), Anal BioanalChem 407: 4015-21
Ángela I. López-Lorente , I, A & Mizaikoff, B (2016), Anal BioanalChem 408: 2875–89
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