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  2. Industrial microbiology - Wikipedia

    en.wikipedia.org/wiki/Industrial_microbiology

    The production of these amino acids is due to Corynebacterium glutamicum and fermentation. C.glutamicum was engineered to be able to produce L-lysine and L-Glutamic acid in large quantities. [7] L-Glutamic acid had a high demand for production because this amino acid is used to produce Monosodium glutamate (MSG) a food

  3. Industrial enzymes - Wikipedia

    en.wikipedia.org/wiki/Industrial_enzymes

    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.

  4. Amino acid synthesis - Wikipedia

    en.wikipedia.org/wiki/Amino_acid_synthesis

    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.

  5. Enzyme - Wikipedia

    en.wikipedia.org/wiki/Enzyme

    Enzymes are usually much larger than their substrates. Sizes range from just 62 amino acid residues, for the monomer of 4-oxalocrotonate tautomerase, [28] to over 2,500 residues in the animal fatty acid synthase. [29] Only a small portion of their structure (around 2–4 amino acids) is directly involved in catalysis: the catalytic site. [30]

  6. List of enzymes - Wikipedia

    en.wikipedia.org/wiki/List_of_enzymes

    Function: An enzyme that is produced by animals that forms part of the innate immune system and is abundant in the secretions of saliva, human milk, tears, and mucus. It functions as an antimicrobial agent by splitting the peptidoglycan component of bacterial cell walls, which then leads to cell death.

  7. Active site - Wikipedia

    en.wikipedia.org/wiki/Active_site

    Since most enzymes have an optimum pH of 6 to 7, the amino acids in the side chain usually have a pK a of 4~10. Candidate include aspartate, glutamate, histidine, cysteine. These acids and bases can stabilise the nucleophile or electrophile formed during the catalysis by providing positive and negative charges. [6]: 164–70

  8. Aminoacylase - Wikipedia

    en.wikipedia.org/wiki/Aminoacylase

    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 ...

  9. Biotransformation - Wikipedia

    en.wikipedia.org/wiki/Biotransformation

    Biotransformation is the biochemical modification of one chemical compound or a mixture of chemical compounds. Biotransformations can be conducted with whole cells, their lysates, or purified enzymes. [1]