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

Kumble Sandeep Prabhu, Candadai S. Ramadoss

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

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.

Original languageEnglish (US)
Pages (from-to)6-12
Number of pages7
JournalIndian Journal of Biochemistry and Biophysics
Volume37
Issue number1
StatePublished - Feb 1 2000

Fingerprint

Penicillin Amidase
Penicillin G
Cyclodextrins
Substrates
Condensation reactions
Anti-Bacterial Agents
Condensation
Enzymes
G-substrate
phenylacetic acid
aminopenicillanic acid

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry

Cite this

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abstract = "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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Penicillin acylase catalyzed synthesis of penicillin-G from substrates anchored in cyclodextrins. / Prabhu, Kumble Sandeep; Ramadoss, Candadai S.

In: Indian Journal of Biochemistry and Biophysics, Vol. 37, No. 1, 01.02.2000, p. 6-12.

Research output: Contribution to journalArticle

TY - JOUR

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AU - Ramadoss, Candadai S.

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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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