Biocatalysts or enzymes are protein compounds that have essential roles in biological systems. From a biological viewpoint, the most important function of enzymes is to hasten or catalyze chemical reactions by lowering the activation energy (Nelson, Cox, & Lehninger, 2004). …
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This trait is also utilized in the production of industrial goods. These biocatalysts are becoming more popular and preferred over chemical catalysts in conversion reactions because they are environmentally friendly, more economical, and have cleaner action. In many industries, biocatalysts are replacing chemical catalysts for production and conversion processes. Among the industries that benefit from biocatalysts are the food industry, laundry detergent manufacture, pharmaceutical industry, and chemical production. Microorganisms like bacteria are the main source of these biocatalysts. Traditionally pure bacterial cultures are maintained, and allowed to express the biocatalysts or enzymes, which are then purified from the cultures. However, with the increased array and variability of industrial products, the need for cleaner technologies, and decreasing emphasis on the use of chemical catalysts, the need for more novel biocatalysts also increased. Worth mentioning are industrial enzymes that are produced from hyperthermophilic microorganisms or those that can survive high temperatures like those that can be found in certain marine environments (Uria, Fawzya, & Chasanah, 2005). The discovery, isolation, and study of potentially important biocatalysts from microorganisms have been conducted on cultivated or cultured microorganisms. From a mixture of organisms, pure cultures are grown from where biocatalysts are extracted. This has been the norm for many years. However, not all microorganisms can be grown in culture. This is due to the fact that some microorganism have special and still unknown cultural and nutritional requirements. The culture media, which is normally agar, is not suitable for many many microorganisms of potential commercial value, because these microbes thrive in temperatures that are above the melting point of agar. Microbial organisms that are culturable account for only a very small fraction of the total microbial diversity, and most industrial biocatalysts are sourced from this culturable fraction (Amann, Ludwig, & Schleifer, 1995; Wilmes, et al., 2009). However, there is a large, untapped potential of unculturable microorganisms to produce more useful and unique biocatalysts for other processes that are not catalyzed by the current crop of biocatalysts. Characterization of bacterial species was based on phylogenetic markers, most used of these are 16S rRNA. However, this was not enough to provide genome sequence information. The advent of metagenomics, or the DNA sequence-based and functional analysis of the total microbial genome present in a mixture, provided the ability to explore the vast diversity and unique properties of microorganisms (Riesenfeld, Schloss, & Handelsman, 2004). Metagenomics does not require the cultivation of microorganisms, instead the DNA is extracted from the mixture of microorganisms collected from a certain environment. The DNA is then subjected to different genomic analysis, and the sequence data can be stored in databases for reference or for manipulations in genetic transformation. Metagenomics provides a rapid means for the discovery of new genes, biocatalysts and pathways (Uria, Fawzya, & Chasanah, 2005). Industrial applications require that biocatalysts are more efficient, and these has led to the creation of engineered enzymes with desired properties such as stability, activity in specific environments and substrate selectivity. Biocatalyst engineering approaches are site-directed mutagenesis and random mutagenesis (Uria, Fawzya, & Chasanah, 2005). Steps in Metagenomics towards the Discovery of Novel Biocatalysts Several initial steps are employed towards the discovery and development of biocatalyst using metagenomics (Figure 1)
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