New Pseudomonas esterases by genetic engineering

A. Schlacher; T. Stanzer; B. Soelkner; E. Klingsbichel; E. Petersen; M. Schmidt; N. Klempier; H. Schwab

doi:10.1016/S1381-1177(96)00034-3

New Pseudomonas esterases by genetic engineering

A. Schlacher, T. Stanzer, B. Soelkner, E. Klingsbichel, E. Petersen, M. Schmidt, N. Klempier, H. Schwab^*

^*Corresponding author for this work

Research output: Contribution to journal › Journal article › Research › peer-review

3 Citations (Scopus)

Abstract

The two new esterases, EP6 and EP10, from Pseudomonas marginata were studied with respect to their substrate specificities and selectivities. Esters of aliphatic and cyclic secondary alcohols were shown to be substrates for EP10, which could be accepted stereoselectively in hydrolysis and transesterification reactions. EP6 showed no selectivity in hydrolysis or the studied substrates.

Original language	English
Journal	Journal of Molecular Catalysis - B Enzymatic
Volume	3
Issue number	1-4
Pages (from-to)	25-27
Number of pages	3
ISSN	1381-1177
DOIs	https://doi.org/10.1016/S1381-1177(96)00034-3
Publication status	Published - 10 Jun 1997

Keywords

Esterase
Hydrolysis
Pseudomonas marginata
Secondary alcohols
Stereoselectivity

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10.1016/S1381-1177(96)00034-3

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@article{97402a42d0174a88ba09ea0731dedfa0,

title = "New Pseudomonas esterases by genetic engineering",

abstract = "The two new esterases, EP6 and EP10, from Pseudomonas marginata were studied with respect to their substrate specificities and selectivities. Esters of aliphatic and cyclic secondary alcohols were shown to be substrates for EP10, which could be accepted stereoselectively in hydrolysis and transesterification reactions. EP6 showed no selectivity in hydrolysis or the studied substrates.",

keywords = "Esterase, Hydrolysis, Pseudomonas marginata, Secondary alcohols, Stereoselectivity",

author = "A. Schlacher and T. Stanzer and B. Soelkner and E. Klingsbichel and E. Petersen and M. Schmidt and N. Klempier and H. Schwab",

note = "Funding Information: We gratefully acknowledge support of this work by the Austrian Fonds zur Fijrderung der wissenschaftlichen Forschung (Spezial-forschungsbereich Biokatalyse Projekt FO 10 1)",

year = "1997",

month = jun,

day = "10",

doi = "10.1016/S1381-1177(96)00034-3",

language = "English",

volume = "3",

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

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TY - JOUR

T1 - New Pseudomonas esterases by genetic engineering

AU - Schlacher, A.

AU - Stanzer, T.

AU - Soelkner, B.

AU - Klingsbichel, E.

AU - Petersen, E.

AU - Schmidt, M.

AU - Klempier, N.

AU - Schwab, H.

N1 - Funding Information: We gratefully acknowledge support of this work by the Austrian Fonds zur Fijrderung der wissenschaftlichen Forschung (Spezial-forschungsbereich Biokatalyse Projekt FO 10 1)

PY - 1997/6/10

Y1 - 1997/6/10

N2 - The two new esterases, EP6 and EP10, from Pseudomonas marginata were studied with respect to their substrate specificities and selectivities. Esters of aliphatic and cyclic secondary alcohols were shown to be substrates for EP10, which could be accepted stereoselectively in hydrolysis and transesterification reactions. EP6 showed no selectivity in hydrolysis or the studied substrates.

AB - The two new esterases, EP6 and EP10, from Pseudomonas marginata were studied with respect to their substrate specificities and selectivities. Esters of aliphatic and cyclic secondary alcohols were shown to be substrates for EP10, which could be accepted stereoselectively in hydrolysis and transesterification reactions. EP6 showed no selectivity in hydrolysis or the studied substrates.

KW - Esterase

KW - Hydrolysis

KW - Pseudomonas marginata

KW - Secondary alcohols

KW - Stereoselectivity

UR - http://www.scopus.com/inward/record.url?scp=0343052033&partnerID=8YFLogxK

U2 - 10.1016/S1381-1177(96)00034-3

DO - 10.1016/S1381-1177(96)00034-3

M3 - Journal article

AN - SCOPUS:0343052033

SN - 1381-1177

VL - 3

SP - 25

EP - 27

JO - Journal of Molecular Catalysis - B Enzymatic

JF - Journal of Molecular Catalysis - B Enzymatic

IS - 1-4

ER -

New Pseudomonas esterases by genetic engineering

Abstract

Keywords

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