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For Stabilization of Enzymes

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Submitted By cxchr13
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The examples below describe some interesting aspects for stabilization of enzymes, DNA, RNA, cytoplasmic membrane, and cytoplasmic solute in hyperthermophilic archaea. * This is a good example of the fact that an increase in internal hydrophobicity of an enzyme and stabilization of a secondary structure α-helix leads to an increase in the thermostability of a protein. * When enhancement of protein (thermo) stability is desired, there are a number of strategies available, taking into account four major interactions within a protein; covalent bonds via disulfide bridges, ionic interactions, hydrogen bonds, and hydrophobic interaction.13) Addition of any of these four types of interactions may be considered in order to enhance the thermostability of a protein. * As the importance of ion pairs toward protein thermostability has been stressed in many cases, addition or removal of an ion pair should have significant effects. In Pf-GDH, there is a large ion pair network comprised of six residues, Arg35, Asp132, Glu138, Arg164, Arg165, and Lys166. Glu138 is located at the center of the network, interacting with Arg165 and Lys166. * Two disulfide bonds were found in the polymerase domain, and these bonds may contribute to the thermostability of the enzyme. * When chaperonin is added into a protein solution in vitro, it prevents the inactivation and aggregation of protein at high temperature. These proteins can support the growth of hyperthermophiles at high temperatures. * High temperature plays a pivotal role (heat maturation) in the proper folding and oligomerization of thermostable enzymes. * High concentration of potassium ion and polyamines (positively charged aliphatic compounds) such as spermine and spermidine can stabilize the DNA. * T. kodakarensis KOD1 possesses two histones (basic proteins, HpkA & HpkB) that are essential for

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