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Engineering Novel And Improved Biocatalysts Using Cell Surface Display

2229 words - 9 pages


By definition, biocatalysis is the use of natural catalysts to mediate chemical transformations in applications for which they have not naturally evolved. However, biocatalysis encompasses a continuum of two distinct but closely related subfields – biotransformation and fermentation. Here, we focus on the application of biocatalysts as biotransformants and review the history and scope of biocatalysis in biochemical engineering. The use of biocatalysts offers a great promise in the processes of synthetic chemistry, but tapping into its potential for industrial applications has depended strongly on advancements in biotechnological innovations, both for improving our understanding ...view middle of the document...

The “first wave”, inspired by the work of Buchner and others, saw possibility of employing enzymes from living cells to enable desired chemical conversions, exemplified by the myriad of enzyme mediated biochemical reactions that occur ubiquitously. This represented traditional biocatalysis, wherein substrate to product conversion is enabled by natural properties and pathways associated with the biocatalyst. Despite the sustainability of enzymes, they caused significant impediments to this approach of biocatalytic processes, particularly their limited availability and narrow range of stability. [4][5]

As enzymes are inherently soluble species, their “insolubilization” by a novel idea termed immobilization helped improve, to some extent, biocatalyst stability under process conditions. It also aided in their separation from the reaction mixture, enabling reuse of the enzyme and hence, partially tackling the issue of availability. Additional benefits of immobilization included minimization of protein contaminant in final product, advent of continuous and economical bioprocessing, enhanced stability under storage conditions, higher productivity and low allergenicity.[6] Key immobilization techniques included (a) surface binding to a carrier by covalent, hydrophobic or ionic interactions, (b) encapsulation/entrapment within a polymeric matrix and (c) carrier free cross-linking of enzyme aggregates. The choice of technique varied, as each method is associated with its own merits and demerits, but in each case, it was vital to ensure, at the very least, the maintenance of enzyme activity.[7]

Some studies have, however, reported a loss in biocatalytic activity as a result of immobilization [XX]. Novel strategies were devised to improve enzyme immobilization, one of them being the development of mesoporous silica supports, with a well-defined pore geometry & mechanical stability, to physically adsorb the enzyme on their surface and thus maintain enzyme activity. A major drawback of physical adsorption, though, is the potential leaching of the biocatalyst, but functionalization and surface modification of these supports have shown significant reduction in leaching.[8] Bio-inspired silica supports, cited as inexpensive, rapid and robust method for stable yet reversible immobilization of enzymes under mild conditions, have also been developed.[9] Such innovative advances notwithstanding, issues with immobilization of enzymes persisted, thus encouraging biochemical engineers to explore newer horizons in biocatalytic engineering.

It was soon realized that for some chemical conversion processes, customary reaction conditions, such as the media, were not suitable for the efficiency of biocatalysts. This led to the concept of “medium engineering”, an empirical approach to improving enzyme properties which involved modifying process conditions to better suit the biocatalyst.[10] A widely probed area of medium engineering is the facilitation of biocatalysis...

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