Bacterial Enzymes

  • Wim J. Quax


In the living world, each chemical reaction is catalyzed by its own enzyme. Enzymes exhibit a high specificity, as they are able to discriminate between slightly different substrate molecules. Furthermore, they have the ability to operate at moderate temperature, pressure, and pH, which makes them attractive catalysts for industrial and household conversion processes. The first reports on the industrial use of enzyme products go back to the beginning of the last century. It was the German scientist Röhm who introduced the use of bovine pancreas extracts for the removal of stains in dirty clothing (Röhm 1915, Fig. 6.1). Around the same time, the Laboratoire Amylo in France experimented with the use of extract from Bacillus for conversion of starch into sugars (Fig. 6.2). As a result, the company Rapidase (Seclin, France), which is now part of the life science division of DSM, was formed. With the development of microbial fermentations in the second half of the last century, the number of industrial processes performed by enzymes and the amount of enzyme produced have increased sharply. At present, a renewed worldwide research effort has been directed to identifying more sustainable and environmentally friendly biocatalytic processes. The availability of highly specific and cheap enzymes resulting from genetic and protein engineering has been very instrumental in reviving interest in the industrial application of enzymes.


Bacillus Licheniformis Protein Engineering Bacterial Enzyme Bacillus Amyloliquefaciens Glucose Isomerase 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.



This chapter is a compilation of numerous collaborations that have allowed the author to develop insights and ideas in the bacterial enzyme field. Special thanks to all the colleagues and students who have contributed material and illustrations presented in this chapter. The sponsoring of EU under contracts BIO2-CT950119, BIO4-9-98-0249, QLK3-CT-1999-00413, QLTR-2001-00519, and of NWO/STW under contract GBI.4707 is highly acknowledged.


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© Springer-Verlag Berlin Heidelberg 2013

Authors and Affiliations

  1. 1.University of GroningenGroningenThe Netherlands

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