An efficient enzymatic synthesis of 5-aminovaleric acid

A. Pukin; C.G. Boeriu; E.L. Scott; J.P.M. Sanders; M.C.R. Franssen

doi:10.1016/j.molcatb.2009.12.006

An efficient enzymatic synthesis of 5-aminovaleric acid

A. Pukin, C.G. Boeriu, E.L. Scott, J.P.M. Sanders, M.C.R. Franssen

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

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Abstract

The title compound was prepared enzymatically from l-lysine in an excellent yield and under buffer-free conditions. l-Lysine was oxidized by the action of l-lysine a-oxidase from Trichoderma viride followed by spontaneous oxidative decarboxylation of the intermediate 6-amino-2-oxocaproic acid in the reaction medium. l-Lysine a-oxidase was immobilized on an epoxy-activated solid support (Sepabeads EC-EP) and the activity of both solution-based and immobilized enzyme in this reaction was determined.

Original language	English
Pages (from-to)	58-62
Journal	Journal of Molecular Catalysis. B, Enzymatic
Volume	65
Issue number	1-4
DOIs	https://doi.org/10.1016/j.molcatb.2009.12.006
Publication status	Published - 2010

Keywords

lysine alpha-oxidase
amperometric biosensor
amino-acids
immobilization
electrode
sepabeads
stability
proteins

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10.1016/j.molcatb.2009.12.006

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title = "An efficient enzymatic synthesis of 5-aminovaleric acid",

abstract = "The title compound was prepared enzymatically from l-lysine in an excellent yield and under buffer-free conditions. l-Lysine was oxidized by the action of l-lysine a-oxidase from Trichoderma viride followed by spontaneous oxidative decarboxylation of the intermediate 6-amino-2-oxocaproic acid in the reaction medium. l-Lysine a-oxidase was immobilized on an epoxy-activated solid support (Sepabeads EC-EP) and the activity of both solution-based and immobilized enzyme in this reaction was determined.",

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author = "A. Pukin and C.G. Boeriu and E.L. Scott and J.P.M. Sanders and M.C.R. Franssen",

year = "2010",

doi = "10.1016/j.molcatb.2009.12.006",

language = "English",

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pages = "58--62",

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

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T1 - An efficient enzymatic synthesis of 5-aminovaleric acid

AU - Pukin, A.

AU - Boeriu, C.G.

AU - Scott, E.L.

AU - Sanders, J.P.M.

AU - Franssen, M.C.R.

PY - 2010

Y1 - 2010

N2 - The title compound was prepared enzymatically from l-lysine in an excellent yield and under buffer-free conditions. l-Lysine was oxidized by the action of l-lysine a-oxidase from Trichoderma viride followed by spontaneous oxidative decarboxylation of the intermediate 6-amino-2-oxocaproic acid in the reaction medium. l-Lysine a-oxidase was immobilized on an epoxy-activated solid support (Sepabeads EC-EP) and the activity of both solution-based and immobilized enzyme in this reaction was determined.

AB - The title compound was prepared enzymatically from l-lysine in an excellent yield and under buffer-free conditions. l-Lysine was oxidized by the action of l-lysine a-oxidase from Trichoderma viride followed by spontaneous oxidative decarboxylation of the intermediate 6-amino-2-oxocaproic acid in the reaction medium. l-Lysine a-oxidase was immobilized on an epoxy-activated solid support (Sepabeads EC-EP) and the activity of both solution-based and immobilized enzyme in this reaction was determined.

KW - lysine alpha-oxidase

KW - amperometric biosensor

KW - amino-acids

KW - immobilization

KW - electrode

KW - sepabeads

KW - stability

KW - proteins

U2 - 10.1016/j.molcatb.2009.12.006

DO - 10.1016/j.molcatb.2009.12.006

M3 - Article

SN - 1381-1177

VL - 65

SP - 58

EP - 62

JO - Journal of Molecular Catalysis. B, Enzymatic

JF - Journal of Molecular Catalysis. B, Enzymatic

IS - 1-4

ER -

An efficient enzymatic synthesis of 5-aminovaleric acid

Abstract

Keywords

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