Download Advances in Bioprocess Engineering by N. W. F. Kossen (auth.), Enrique Galindo, Octavio T. Ramírez PDF

By N. W. F. Kossen (auth.), Enrique Galindo, Octavio T. Ramírez (eds.)

ISBN-10: 9048144590

ISBN-13: 9789048144594

Bioprocess engineering performs a key position within the improvement and optimization of bioprocesses resulting in the goods of biotechnology. A survey of the cutting-edge during this box is tremendously wanted. This paintings covers all of the crucial sub-areas and as such is needed studying for scientists energetic in the entire disciplines occupied with bioprocess engineering. This overview of easy and utilized techniques is introduced jointly through a extensive foreign team of specialist authors.
The paintings is a mirrored image of the 1st foreign Symposium on Bioprocess Engineering, June 1994. despite the fact that, it needs to be emphasised that the ebook can't be perceived as a standard symposium lawsuits quantity: a strict peer-review strategy assures the readers of a excessive point of caliber; greater than 1 / 4 of the paintings comprises invited contributions, whereas below half the spontaneously submitted manuscripts have been authorised for e-book.
Advances in Bioprocess Engineering belongs one of the imperative set of tools of latest researcher during this box.

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Extra info for Advances in Bioprocess Engineering

Example text

Chisti, Y. , Biotechnol. , 11, 469-479 (1993). Fermentation of cellulosic materials to mycoprotein foods. NOMENCLATURE C- -/ Impeller clearance above bottom of tank (m) Diameter of fermenter (m) Diameter of impeller (m) static liquid or slurry height (m) Impeller speed (rpm) Specific protein production rate (h- 1 ) Relative protein production rate (-) LITERATURE CITED 1. 2. 3. Chisti, Y. , Enzyme Microb. , 8, 194204 (1986) . Disruption of microbial cells for intracellular products. , Chisti, Y.

The kinetic constants of the free enzyme, the immobilized enzyme and the enzyme in whole cells have been determined [~,l]. Models have also been proposed for the thermal and pH stability of the enzyme [~]. particula~ One of the main properties required for a successful biocatalyst is the stability. In the case of PA, the pH is the most important parameter affecting the half-life of the enzyme. Stable derivatives have been reported with half lifes between 1000 to 2000 hours. Stabilization procedures such as multipoint covalent attachment to agarose gels increase the stability 1400 fold compared to the wild strain [2].

All microorganisms, animal and plant cells are sensitive to various levels of hydrodynamic and mechanical forces. In fact, disruption of cells by fluidshear, solid-shear or impact are established operations in bioprocessing [1]; however, in production of microbial or eucaryotic cells and their metabolites, exposure of the biocatalysts to high shear fields can be counterproductive [2,3]. Investigations of the safe limits of exposure of biocatalysts to fluid mechanical forces and design of bioreactors to not exceed the identified limits is of increasing importance especially because the newer genetically modified biocatalysts tend to be less robust than their wild counterparts [4,5].

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