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  2. 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.

  3. Industrial microbiology - Wikipedia

    en.wikipedia.org/wiki/Industrial_microbiology

    Medicinally, microbes can be used for creating antibiotics in order to treat infection. Microbes can also be used for the food industry as well. Microbes are very useful in creating some of the mass produced products that are consumed by people. The chemical industry also uses microorganisms in order to synthesize amino acids and organic solvents.

  4. 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.

  5. Aminoacylase - Wikipedia

    en.wikipedia.org/wiki/Aminoacylase

    In enzymology, an aminoacylase (EC 3.5.1.14) is an enzyme that catalyzes the chemical reaction. N-acyl-L-amino acid + H 2 O ⇌ carboxylate + L-amino acid. Thus, the two substrates of this enzyme are N-acyl-L-amino acid and H 2 O, whereas its two products are carboxylate and L-amino acid.

  6. Enzyme - Wikipedia

    en.wikipedia.org/wiki/Enzyme

    In some enzymes, no amino acids are directly involved in catalysis; instead, the enzyme contains sites to bind and orient catalytic cofactors. [31] Enzyme structures may also contain allosteric sites where the binding of a small molecule causes a conformational change that increases or decreases activity.

  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. Isomerase - Wikipedia

    en.wikipedia.org/wiki/Isomerase

    The use of glucose isomerase very efficiently converts xylose to xylulose, which can then be acted upon by fermenting yeast. Overall, extensive research in genetic engineering has been invested into optimizing glucose isomerase and facilitating its recovery from industrial applications for re-use.

  9. Xylose isomerase - Wikipedia

    en.wikipedia.org/wiki/Xylose_isomerase

    The metals are in an octahedral geometry. Metal site 1 binds the substrate tightly, while metal site 2 binds the substrate loosely. Both share an acid residue, Glutamic acid 216 of the enzyme, that bridges the two cations. Two basic amino acids surround the negatively charged ligands to neutralize them. The second cavity faces the metal cavity ...