The β-Lactam Antibiotics: Current Situation and Future Prospects in Manufacture and Therapy

F, Schmidt

doi:10.1007/978-3-642-11458-8_5

Industrial Applications 2010

DOI: 10.1007/978-3-642-11458-8_5

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The β-Lactam Antibiotics: Current Situation and Future Prospects in Manufacture and Therapy

Schmidt F

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Cited by 2 publications

References 94 publications

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Scale‐down of penicillin production in Penicillium chrysogenum

Jonge

Buijs

Pierick

et al. 2011

Biotechnology Journal

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In large-scale production reactors the combination of high broth viscosity and large broth volume leads to insufficient liquid-phase mixing, resulting in gradients in, for example, the concentrations of substrate and oxygen. This often leads to differences in productivity of the full-scale process compared with laboratory scale. In this scale-down study of penicillin production, the influence of substrate gradients on process performance and cell physiology was investigated by imposing an intermittent feeding regime on a laboratory-scale culture of a high yielding strain of Penicillium chrysogenum. It was found that penicillin production was reduced by a factor of two in the intermittently fed cultures relative to constant feed cultivations fed with the same amount of glucose per hour, while the biomass yield was the same. Measurement of the levels of the intermediates of the penicillin biosynthesis pathway, along with the enzyme levels, suggested that the reduction of the flux through the penicillin pathway is mainly the result of a lower influx into the pathway, possibly due to inhibitory levels of adenosine monophosphate and pyrophosphate and lower activating levels of adenosine triphosphate during the zero-substrate phase of each cycle of intermittent feeding.

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Scale‐down of penicillin production in Penicillium chrysogenum

Jonge

Buijs

Pierick

et al. 2011

Biotechnology Journal

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Surface Patterning for Enhanced Protein Stability: Insights from Molecular Simulations

2019

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Reduced activity of enzymes upon immobilization is a major challenge for the industrial use of enzymes. Enzyme–surface interactions and interactions between the immobilized enzymes are thought of as primary reasons for the reduced activity. In the current paper, we study the thermal and structural stability of proteins on a patterned hydrophobic surface in the framework of a hydrophobic–polar lattice model. Our results indicate that, while a homogeneous hydrophobic surface denatures the proteins, carefully patterned surfaces can dramatically increase the stability of adsorbed proteins. The size, shape, and the distance between surface patterns play a significant role in determining the stability of proteins. When the spacing between the patterns is large, maximum stability is observed when the surface pattern is complementary to the exposed hydrophobic domain of the protein, while at smaller spacing, patterns with lower hydrophobicity stabilize the protein more compared to the complementary pattern. The findings from the paper can be rationalized to design novel enzyme-specific surfaces for immobilization with enhanced enzymatic activity.

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The β-Lactam Antibiotics: Current Situation and Future Prospects in Manufacture and Therapy

Cited by 2 publications

References 94 publications

Scale‐down of penicillin production in Penicillium chrysogenum

Scale‐down of penicillin production in Penicillium chrysogenum

Surface Patterning for Enhanced Protein Stability: Insights from Molecular Simulations

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