Improved activity and pH stability of E. coli ATCC 11105 penicillin acylase by error-prone PCR

Penicillin G acylase is the key enzyme used in the industrial production of β-lactam antibiotics. This enzyme hydrolyzes penicillin G and related β-lactam antibiotics releasing 6-aminopenicillanic acid, which is an intermediate in the production of semisynthetic penicillins. To improve the enzymatic...

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Published in:Applied microbiology and biotechnology 2014-05, Vol.98 (10), p.4467-4477
Main Authors: Balci, Huseyin, Ozturk, Merve Tuzlakoglu, Pijning, Tjaard, Ozturk, Saliha Issever, Gumusel, Fusun
Format: Article
Language:English
Subjects:
amidase
Amino Acid Substitution
Amino acids
Antibiotics
benzylpenicillin
Beta lactamases
Biocatalysts
Biomedical and Life Sciences
Biotechnologically Relevant Enzymes and Proteins
Biotechnology
Chemical properties
Cloning
DNA polymerase
E coli
Enzymatic activity
enzyme activity
Enzyme kinetics
Enzyme Stability
Enzymes
Escherichia coli
Escherichia coli - enzymology
Escherichia coli - genetics
Escherichia coli Proteins - chemistry
Escherichia coli Proteins - genetics
Escherichia coli Proteins - metabolism
evolution
Gene expression
genes
Genetic engineering
High-throughput screening (Biochemical assaying)
Hydrogen-Ion Concentration
Industrial production
Life Sciences
Microbial Genetics and Genomics
Microbiology
Mutagenesis
Mutation, Missense
nucleotide sequences
Penicillin
Penicillin Amidase - chemistry
Penicillin Amidase - genetics
Penicillin Amidase - metabolism
Peptides
Plasmids
Point Mutation
Polymerase chain reaction
Polymerase Chain Reaction - methods
Protein Engineering - methods
sequence analysis
Sequence Analysis, DNA
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Ozturk, Merve Tuzlakoglu
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Gumusel, Fusun
description Penicillin G acylase is the key enzyme used in the industrial production of β-lactam antibiotics. This enzyme hydrolyzes penicillin G and related β-lactam antibiotics releasing 6-aminopenicillanic acid, which is an intermediate in the production of semisynthetic penicillins. To improve the enzymatic activity of Escherichia coli penicillin acylase, sequential rounds of error-prone polymerase chain reaction were applied to the E. coli pac gene. After the second round of evolution, the best mutant M2234 with enhanced activity was selected and analyzed. DNA sequence analyses of M2234 revealed that one amino acid residue (K297I), located far from the center of the catalytic pocket, was changed. This mutant (M2234) has a specific activity 4.0 times higher than the parent enzyme and also displayed higher stability at pH 10.
doi_str_mv 10.1007/s00253-013-5476-7
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This enzyme hydrolyzes penicillin G and related β-lactam antibiotics releasing 6-aminopenicillanic acid, which is an intermediate in the production of semisynthetic penicillins. To improve the enzymatic activity of Escherichia coli penicillin acylase, sequential rounds of error-prone polymerase chain reaction were applied to the E. coli pac gene. After the second round of evolution, the best mutant M2234 with enhanced activity was selected and analyzed. DNA sequence analyses of M2234 revealed that one amino acid residue (K297I), located far from the center of the catalytic pocket, was changed. 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This enzyme hydrolyzes penicillin G and related β-lactam antibiotics releasing 6-aminopenicillanic acid, which is an intermediate in the production of semisynthetic penicillins. To improve the enzymatic activity of Escherichia coli penicillin acylase, sequential rounds of error-prone polymerase chain reaction were applied to the E. coli pac gene. After the second round of evolution, the best mutant M2234 with enhanced activity was selected and analyzed. DNA sequence analyses of M2234 revealed that one amino acid residue (K297I), located far from the center of the catalytic pocket, was changed. 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This enzyme hydrolyzes penicillin G and related β-lactam antibiotics releasing 6-aminopenicillanic acid, which is an intermediate in the production of semisynthetic penicillins. To improve the enzymatic activity of Escherichia coli penicillin acylase, sequential rounds of error-prone polymerase chain reaction were applied to the E. coli pac gene. After the second round of evolution, the best mutant M2234 with enhanced activity was selected and analyzed. DNA sequence analyses of M2234 revealed that one amino acid residue (K297I), located far from the center of the catalytic pocket, was changed. This mutant (M2234) has a specific activity 4.0 times higher than the parent enzyme and also displayed higher stability at pH 10.</abstract><cop>Berlin/Heidelberg</cop><pub>Springer-Verlag</pub><pmid>24389703</pmid><doi>10.1007/s00253-013-5476-7</doi><tpages>11</tpages></addata></record>
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subjects amidase
Amino Acid Substitution
Amino acids
Antibiotics
benzylpenicillin
Beta lactamases
Biocatalysts
Biomedical and Life Sciences
Biotechnologically Relevant Enzymes and Proteins
Biotechnology
Chemical properties
Cloning
DNA polymerase
E coli
Enzymatic activity
enzyme activity
Enzyme kinetics
Enzyme Stability
Enzymes
Escherichia coli
Escherichia coli - enzymology
Escherichia coli - genetics
Escherichia coli Proteins - chemistry
Escherichia coli Proteins - genetics
Escherichia coli Proteins - metabolism
evolution
Gene expression
genes
Genetic engineering
High-throughput screening (Biochemical assaying)
Hydrogen-Ion Concentration
Industrial production
Life Sciences
Microbial Genetics and Genomics
Microbiology
Mutagenesis
Mutation, Missense
nucleotide sequences
Penicillin
Penicillin Amidase - chemistry
Penicillin Amidase - genetics
Penicillin Amidase - metabolism
Peptides
Plasmids
Point Mutation
Polymerase chain reaction
Polymerase Chain Reaction - methods
Protein Engineering - methods
sequence analysis
Sequence Analysis, DNA
title Improved activity and pH stability of E. coli ATCC 11105 penicillin acylase by error-prone PCR
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