TY - JOUR
T1 - Penicillin acylase catalyzed synthesis of penicillin-G from substrates anchored in cyclodextrins
AU - Prabhu, Kumble Sandeep
AU - Ramadoss, Candadai S.
PY - 2000/2/1
Y1 - 2000/2/1
N2 - Penicillin acylase (EC 3.5.1.11) catalyses the condensation of phenylacetic acid (PAA) and 6-aminopenicillanic acid (6-APA) 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.
AB - Penicillin acylase (EC 3.5.1.11) catalyses the condensation of phenylacetic acid (PAA) and 6-aminopenicillanic acid (6-APA) 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.
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M3 - Article
C2 - 10983407
AN - SCOPUS:0034138154
SN - 0301-1208
VL - 37
SP - 6
EP - 12
JO - Indian Journal of Biochemistry and Biophysics
JF - Indian Journal of Biochemistry and Biophysics
IS - 1
ER -