Protein Engineering For Industrial Biotechnology

Protein Engineering For Industrial Biotechnology

Language: English

Pages: 388

ISBN: 9057024128

Format: PDF / Kindle (mobi) / ePub

Protein engineering has proved to be one of the more fruitful technological approaches in biotechnology, being both very powerful and able to generate valuable intellectual property. This book aims to present examples in which the application of protein engineering has successfully solved problems arising in industrial biotechnology. There is a section on its use to enhance purification of recombinant proteins. The use of protein engineering to modify the activity or the stability of industrial enzymes from lipases to proteases, from carboxypeptidases to glucanases and glucosidases, and from pectin modifying enzymes to enzymes able to degrade recalcitrant compounds is extensively covered. It is shown how areas as diverse as agrofood technology, fine chemistry, detergents, bioremediation and biosensors receive significant contributions from protein and solvent engineering.

The application of protein engineering to health care is also covered, from the development of new vaccines to new potential therapeutic proteins. A specific notation is given to protein engineering in the development of target molecules for drug discovery.

International in scope, the many contributions are drawn from academia and industry. The text should be of interest to students and researchers in industrial biotechnology as well as to everybody interested in basic research in protein structure, molecular genetics, bio-organic chemistry, biochemistry, agrobiotechnology, pharmaceutical sciences and medicine.
















displayed after residue Ser 116 of the VH domain of the D1.3 Fv fragment. 145 000 clones were screened via the filter sandwich assay. Out of these merely nine clones gave rise to a detectable binding signal for streptavidin. Their subsequent characterization revealed that just one peptide was suitable for the detection in a Western blot and exhibited sufficient affinity for the purification of the Fv fragment on immobilized streptavidin (Schmidt and Skerra, 1993). However, this peptide sequence

more amino acids and evaluating the effect of these pre-selected substitutions in the mutated product. By definition, this strategy, also called “rational mutagenesis”, requires a prior knowledge of the role played by specific residues or regions of the protein. This means availability of the protein 3D structure, if possible also in complex with substrates, ligands, regulation elements or at least availability of sequence of proteins with related but not identical activity for comparison. In

Enzymatic hydrolysis of meso (sγn-sγn)-l,3,5-triacetoxy-2,4dimethylpentane and acetylation of meso (sγn-sγn)-3-benzyloxy-2,4-dimethylpentane-l,5-diol by lipase. Chem. Pharm. Bull., 44, 1391–1394. Nakamura, K., Chi, Y.M., Yamada, Y. and Yano, T. (1986) Lipase activity and stability in supercritical carbon dioxide. Chem. Eng. Commun., 45, 207–212. Norin, M., Haeffner, F., Achour, A., Norin, T. and Hult, K. (1994) Computer modeling of substrate binding to lipases from Rhizomucor miehei. Humicola

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chemical separation processes has been of considerable research interest for the past decade (McHugh and Krukonis, 1985). The fundamentals of SCF extraction technology and a number of potential applications have been described in several review papers (Ikushima et al., 1992). One very interesting and, as yet, not fully tested offshoot of SCF extraction technology is the use of an SCF solvent as a reaction medium in which an SCF either actively participates in the reaction or functions only as the

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