Enzyme deactivation in a bubble column, a stirred vessel and an inclined plane

Ghadge, Rajaram; Sawant, S.B.; Joshi, Jyeshtharaj B.

doi:10.1016/j.ces.2003.08.008

Cited by 16 publications

(19 citation statements)

References 21 publications

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“…The rate constant depended on the power input per unit volume and the hold-up, as might be expected for an interfacial effect. Similar results were obtained in a bubble column and in an inclined film (Ghadge et al 2003), with the rate constant correlated with the volumetric mass transfer coefficient, k L a. It was claimed that polyethylene glycol could reduce inactivation in stirred tanks (Patil et al 2000), and that it might be helpful in manufacture to reduce the fermenter impeller speed during the stationary phase.…”

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confidence: 69%

Effects of shear on proteins in solution

2010

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The effects of "shear" on proteins in solution are described and discussed. Research on this topic covers many decades, beginning with investigations of possible denaturation of enzymes during processing, whilst more recent concerns are how the quality of therapeutic proteins might be affected by shear or shear related effects.The paradigm that emerges from most studies is that shear in the fluid mechanical sense is unlikely by itself to damage most proteins and that interfacial phenomena are critically important. In particular, moving gas-liquid interfaces can be very deleterious. Aggregation of therapeutic proteins on nanoparticles shed from solid surfaces is a recent concern because of potential consequences on patient safety. It is clear that labeling such damage as "shear" is a mistake as this inhibits clear investigations of, and thinking about, the true causes of damage to proteins in solution during processing.

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confidence: 69%

Effects of shear on proteins in solution

2010

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“…This shows that tube shaking conditions are relevant for cell culture performance, especially at high cell density, and that they can induce a change in cell metabolism when fresh medium is not fed often enough. Although we have not investigated the effect of the tested culture conditions on product quality, it has been reported, that damage to proteins in solution by shear and the related phenomena exerted on proteins at the moving gas-liquid interface may result in protein unfolding, dissociation of subunits, or increased aggregation, thus leading to protein inactivation (and/or increased immunogenicity of protein drug products) (Ghadge et al, 2003;Klockner and Buchs, 2012;Thomas and Geer, 2011). Therefore, it is possible that the adjustment in the shaking angle and speed also altered the mechanical shear of the fluid inside the shake tubes, resulting in an increased product yield as determined by enzyme's activity (Fig.…”

Section: Comparison Between 90 • and 45 • Shaking Anglementioning

confidence: 95%

Development and application of a high-throughput platform for perfusion-based cell culture processes

Villiger-Oberbek¹,

Yang²,

Zhou³

et al. 2015

Journal of Biotechnology

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“…Upon exposure to the environment with higher hydrodynamic shear forces, the enzyme molecules became greatly deactivated or denatured due to the destruction of native threedimensional structure or conformation. A number of studies have reported that the presence of hydrodynamic shear forces and gas-liquid interface can give rise to the deactivation of enzymes such as lipase, cellulase, and hen eggwhite lysozyme [26][27][28]. Moreover, it has been shown from our data that the presence of agitation under high pressure would be undoubtedly detrimental to enzymatic activity.…”

Section: Resultsmentioning

confidence: 59%

Deactivation of isoamylase and β-amylase in the agitated reactor under supercritical carbon dioxide

Wang

Lai

Huang

et al. 2010

Bioprocess Biosyst Eng

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The current research examines the impact of agitation on deactivation of isoamylase and β-amylase under supercritical carbon dioxide (SC-CO2). Our experimental results showed that the activity of either enzyme decreased with increasing pressure or speed of agitation. The degree of enzymatic deactivation caused by pressure became more prominent in the presence of agitation, suggesting that the agitation plays an important role in enzymatic deactivation in SC-CO2 environment. Moreover, the enzymatic deactivation behavior associated with agitation and pressure was further quantitatively analyzed using a proposed inactivation kinetic model. Our analysis indicated that isoamylase and β-amylase exhibited significantly different relationships between the inverse of percentage residual activity and the product of number of revolution per time and time elapsed under pressurized carbon dioxide. We believe that the outcome from this work may provide a better understanding of the effects of agitation and pressure in enzyme deactivation behavior under SC-CO2.

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Enzyme deactivation in a bubble column, a stirred vessel and an inclined plane

Cited by 16 publications

References 21 publications

Effects of shear on proteins in solution

Effects of shear on proteins in solution

Development and application of a high-throughput platform for perfusion-based cell culture processes

Deactivation of isoamylase and β-amylase in the agitated reactor under supercritical carbon dioxide

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