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Molecular Aspects of the Interaction of Organic Solvents and Proteinase K: Kinetics and Docking Studies

  • E. Yadollahi
  • B. Shareghi
  • R. Eslami farsani
Research Paper
  • 49 Downloads

Abstract

Recently, the number of studies dealing with nonaqueous enzymology has increased. Proteases are enzymes that catalyze the hydrolysis of peptide bonds in other proteins. The 279-residue serine protease proteinase K (EC 3.4.21.14) from the fungus Tritirachium album limber belongs to the subtilisin family of enzymes. The enzyme is extensively applied for protein-related studies due to its stability at high temperature and ability to remain active in a wide range of pH (3.0–7.0). The effect of organic solvents (1,4-butanediol and butanol) on the activity of native proteinase K was studied by ultraviolet–visible (UV–Vis) spectroscopy and molecular docking. The results of spectroscopy show that 1,4-butanediol and butanol lead to increase in Vmax and decrease in Km values at low concentrations. Furthermore, they indicated that butanol is a slightly better enzyme activator in comparison with 1,4-butanediol. Molecular docking data illustrate interaction between organic solvents and PK, where hydrogen bonds and hydrophobic interactions play a major role in the PK-organic solvents complex formation. Therefore, we could conclude that these interactions lead to change in the native conformation of PK and increased enzyme activity.

Keywords

Kinetics reaction enzyme Molecular docking Organic solvents Proteinase K 

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Copyright information

© Shiraz University 2018

Authors and Affiliations

  1. 1.Department of BiologyUniversity of ShahrekordShahrekordIslamic Republic of Iran

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