Use of high acyl donor concentrations leads to penicillin acylase inactivation in the course of peptide synthesis

Tatyana A. Shcherbakova; Alexei V. Korennykh; Luuk M.Van Langen; Roger A. Sheldon; Vytas K. Švedas

doi:10.1016/j.molcatb.2004.07.006

Use of high acyl donor concentrations leads to penicillin acylase inactivation in the course of peptide synthesis

Tatyana A. Shcherbakova
, Alexei V. Korennykh
, Luuk M.Van Langen
, Roger A. Sheldon
, Vytas K. Švedas

Research output: Contribution to journal › Article › peer-review

4 Scopus citations

Abstract

Enzyme inactivation has been observed in the course of penicillin acylase-catalyzed hydrolysis and aminolysis of d-phenylglycine amide. Inactivation was very sensitive to the d-phenylglycine amide concentration: at pH 9.5, 25°C and 400 mM substrate, penicillin acylase lost more than 90% of its initial catalytic activity in half an hour, in the presence of 100 mM substrate, 50% of the initial activity in two hours, whereas in the absence of substrate, no significant enzyme inactivation was observed in three hours. Observed enzyme inactivation limits use of high acyl donor concentrations at penicillin acylase-catalyzed peptide synthesis.

Original language	English (US)
Pages (from-to)	63-65
Number of pages	3
Journal	Journal of Molecular Catalysis B: Enzymatic
Volume	31
Issue number	1-3
DOIs	https://doi.org/10.1016/j.molcatb.2004.07.006
State	Published - Oct 15 2004
Externally published	Yes

All Science Journal Classification (ASJC) codes

Catalysis
Bioengineering
Biochemistry
Process Chemistry and Technology

Keywords

Enzyme stability
Inactivation by substrate
Penicillin acylase

Access to Document

10.1016/j.molcatb.2004.07.006

Cite this

@article{f6760a25b27e41f884313460afd6519f,

title = "Use of high acyl donor concentrations leads to penicillin acylase inactivation in the course of peptide synthesis",

abstract = "Enzyme inactivation has been observed in the course of penicillin acylase-catalyzed hydrolysis and aminolysis of d-phenylglycine amide. Inactivation was very sensitive to the d-phenylglycine amide concentration: at pH 9.5, 25°C and 400 mM substrate, penicillin acylase lost more than 90\% of its initial catalytic activity in half an hour, in the presence of 100 mM substrate, 50\% of the initial activity in two hours, whereas in the absence of substrate, no significant enzyme inactivation was observed in three hours. Observed enzyme inactivation limits use of high acyl donor concentrations at penicillin acylase-catalyzed peptide synthesis.",

keywords = "Enzyme stability, Inactivation by substrate, Penicillin acylase",

author = "Shcherbakova, \{Tatyana A.\} and Korennykh, \{Alexei V.\} and Langen, \{Luuk M.Van\} and Sheldon, \{Roger A.\} and {\v S}vedas, \{Vytas K.\}",

note = "Funding Information: This work was supported by the Russian Foundation for Basic Research (Grant 03-04-48472) and INTAS 2001-0673. Financial support by DSM Life Sciences and the Dutch Ministry of Economic Affairs is gratefully acknowledged. ",

year = "2004",

month = oct,

day = "15",

doi = "10.1016/j.molcatb.2004.07.006",

language = "English (US)",

volume = "31",

pages = "63--65",

journal = "Journal of Molecular Catalysis B: Enzymatic",

issn = "1381-1177",

publisher = "Elsevier",

number = "1-3",

}

TY - JOUR

T1 - Use of high acyl donor concentrations leads to penicillin acylase inactivation in the course of peptide synthesis

AU - Shcherbakova, Tatyana A.

AU - Korennykh, Alexei V.

AU - Langen, Luuk M.Van

AU - Sheldon, Roger A.

AU - Švedas, Vytas K.

N1 - Funding Information: This work was supported by the Russian Foundation for Basic Research (Grant 03-04-48472) and INTAS 2001-0673. Financial support by DSM Life Sciences and the Dutch Ministry of Economic Affairs is gratefully acknowledged.

PY - 2004/10/15

Y1 - 2004/10/15

N2 - Enzyme inactivation has been observed in the course of penicillin acylase-catalyzed hydrolysis and aminolysis of d-phenylglycine amide. Inactivation was very sensitive to the d-phenylglycine amide concentration: at pH 9.5, 25°C and 400 mM substrate, penicillin acylase lost more than 90% of its initial catalytic activity in half an hour, in the presence of 100 mM substrate, 50% of the initial activity in two hours, whereas in the absence of substrate, no significant enzyme inactivation was observed in three hours. Observed enzyme inactivation limits use of high acyl donor concentrations at penicillin acylase-catalyzed peptide synthesis.

AB - Enzyme inactivation has been observed in the course of penicillin acylase-catalyzed hydrolysis and aminolysis of d-phenylglycine amide. Inactivation was very sensitive to the d-phenylglycine amide concentration: at pH 9.5, 25°C and 400 mM substrate, penicillin acylase lost more than 90% of its initial catalytic activity in half an hour, in the presence of 100 mM substrate, 50% of the initial activity in two hours, whereas in the absence of substrate, no significant enzyme inactivation was observed in three hours. Observed enzyme inactivation limits use of high acyl donor concentrations at penicillin acylase-catalyzed peptide synthesis.

KW - Enzyme stability

KW - Inactivation by substrate

KW - Penicillin acylase

UR - https://www.scopus.com/pages/publications/4644226675

UR - https://www.scopus.com/pages/publications/4644226675#tab=citedBy

U2 - 10.1016/j.molcatb.2004.07.006

DO - 10.1016/j.molcatb.2004.07.006

M3 - Article

AN - SCOPUS:4644226675

SN - 1381-1177

VL - 31

SP - 63

EP - 65

JO - Journal of Molecular Catalysis B: Enzymatic

JF - Journal of Molecular Catalysis B: Enzymatic

IS - 1-3

ER -

Use of high acyl donor concentrations leads to penicillin acylase inactivation in the course of peptide synthesis

Abstract

All Science Journal Classification (ASJC) codes

Keywords

Access to Document

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