Penicillin acylase catalyzed synthesis of penicillin-G from substrates anchored in cyclodextrins

Abstract

<span style="font-size:14.0pt;font-family:" times="" new="" roman";="" mso-fareast-font-family:"times="" roman";mso-ansi-language:en-us;mso-fareast-language:="" en-us;mso-bidi-language:ar-sa"="">Penicillin acylase (EC 3.5.1.11 ) catalyses the condensation of phenylacetic acid (PAA) and 6-aminopenicillanic acid (6-A A) to form benzylpenicillin (BP). Both PAA and 6-APA were found to form host-guest complexes with β-methylcyclodextrin (βm-CD) and γ-cyclodextrin (γ -CD) respectively. The rate of the reaction catalyzed by the enzyme remained unaffected if one of the substrates used was in the cyclodextrin complexed form. However, in this case, the reaction lasted longer and yielded about 20 per cent more products compared to the condensation reaction involving only uncomplexed substrates. There was a distinct increase in the rate of formation of the antibiotic, if both substrates used are in CD-complexed form .</span>