Improvement of steroid biotransformation with hydroxypropyl-beta-cyclodextrin induced complexation

Appl Biochem Biotechnol. 2009 Dec;159(3):642-54. doi: 10.1007/s12010-008-8499-2. Epub 2009 Feb 3.

Abstract

The inclusion complexes induced by cyclodextrins and its derivates have been shown previously to enhance the biotransformation of hydrophobic compounds. Using hydroxypropyl-beta-cyclodextrin (HP-beta-CD; 20% w/v), the water solubility of cortisone acetate increased from 0.039 to 7.382 g L(-1) at 32 degrees C. The solubilization effect of HP-beta-CD was far superior to dimethylformamide (DMF) and ethanol. The dissolution rate also significantly increased in the presence of HP-beta-CD. The enzymatic stability of Delta(1)-dehydrogenase from Arthrobacter simplex TCCC 11037 was not influenced by the increasing concentrations of HP-beta-CD contrary to the organic cosolvents which negatively influenced in the order DMF > ethanol. The activity inhibition effect caused by HP-beta-CD was not so conspicuous as ethanol and DMF. Inactivation constants of ethanol, DMF, and HP-beta-CD were 5.832, 4.541, and 1.216, respectively. The inactivation energy (E (a)) was in the order of HP-beta-CD (55.1 kJ mol(-1)) > ethanol (39.9 kJ mol(-1)) > DMF (37.1 kJ mol(-1)).

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 2-Hydroxypropyl-beta-cyclodextrin
  • Arthrobacter / enzymology
  • Arthrobacter / metabolism*
  • Dimethylformamide / pharmacology
  • Enzyme Stability / drug effects
  • Ethanol / pharmacology
  • Oxidoreductases / metabolism
  • Steroids / chemistry*
  • Steroids / metabolism*
  • beta-Cyclodextrins / pharmacology*

Substances

  • Steroids
  • beta-Cyclodextrins
  • 2-Hydroxypropyl-beta-cyclodextrin
  • Ethanol
  • Dimethylformamide
  • Oxidoreductases
  • 3-oxosteroid delta(1) dehydrogenase