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Industrial enzymes are enzymes that are commercially used in a variety of industries such as pharmaceuticals, chemical production, biofuels, food and beverage, and consumer products. Due to advancements in recent years, biocatalysis through isolated enzymes is considered more economical than use of whole cells.
The commercial production of amino acids usually relies on mutant bacteria that overproduce individual amino acids using glucose as a carbon source. Some amino acids are produced by enzymatic conversions of synthetic intermediates. 2-Aminothiazoline-4-carboxylic acid is an intermediate in the industrial synthesis of L-cysteine for example.
Aminoacylases have been used for the production of L-amino acids in industrial settings since the late 1950s. [18] Since aminoacylases are substrate specific for N-acyl-L-amino acids and not N-acyl-D-amino acids , aminoacylases can be used to reliably take a mixture of these two reactants and only convert the L enantiomers into products - which ...
Microbial enzymes are widely utilized as biocatalysts in fields such as biotechnology, agriculture, and pharmaceuticals. Metagenomic data serve as a valuable resource for identifying novel CUEs from previously unknown microbes present in complex microbial communities across diverse ecosystems.
The synthesis of essential amino acids such as are L-Methionine, L-Lysine, L-Tryptophan and the non-essential amino acid L-Glutamic acid are used today mainly for feed, food, and pharmaceutical industries. The production of these amino acids is due to Corynebacterium glutamicum and fermentation.
It usually consists of three to four amino acids, while other amino acids within the protein are required to maintain the tertiary structure of the enzymes. [2] Each active site is evolved to be optimised to bind a particular substrate and catalyse a particular reaction, resulting in high specificity. This specificity is determined by the ...
Regioselectivity and diastereoselectivity: Due to their complex three-dimensional structure, enzymes may distinguish between functional groups which are chemically situated in different regions of the substrate molecule. Enantioselectivity: Since almost all enzymes are made from L-amino acids, enzymes are chiral catalysts. As a consequence, any ...
These enzymes can be identified by a conserved HEXXH motif in their active site. This motif is crucial for the enzyme's function, as the histidine amino acids within the motif coordinate (bind) the metal ion, which then uses hydrolysis to break the peptide bond between the first amino acid and the rest of the protein. [9]