Sensitive amperometric biosensor for the determination of
biogenic and synthetic amines using pea seedling amine oxidase:
a novel approach for enzyme immobilisation

J 1999

Sensitive amperometric biosensor for the determination of biogenic and synthetic amines using pea seedling amine oxidase: a novel approach for enzyme immobilisation

WIMMEROVÁ, Michaela and Lumír MACHOLÁN

Basic information

Original name

Sensitive amperometric biosensor for the determination of biogenic and synthetic amines using pea seedling amine oxidase: a novel approach for enzyme immobilisation

Authors

WIMMEROVÁ, Michaela (203 Czech Republic, guarantor) and Lumír MACHOLÁN (203 Czech Republic)

Edition

Biosensors & Bioelectronics, Oxford, Elsevier Advanced Technology, 1999, 0956-5663

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10600 1.6 Biological sciences

Country of publisher

United Kingdom of Great Britain and Northern Ireland

Confidentiality degree

není předmětem státního či obchodního tajemství

Impact factor

Impact factor: 2.020

RIV identification code

RIV/00216224:14310/99:00008547

Organization unit

Faculty of Science

Keywords in English

biosensor; amine oxidase; immobilisation

Abstract

V originále

We prepared a new inorganic sorbent based on modified triazine (2-[4,6-bis (aminoethylamine)-1,3,5-triazine]-Silasorb; BAT-Silasorb) which binds pea seedlings amine oxidase (PSAO) very tightly without loss of its catalytic activity. This unique feature as well as the wide substrate specificity of PSAO was successfully utilised in the construction of an amperometric biosensor based on a carbon paste electrode for the fast and sensitive detection of various amines at a formal potential 0 mV versus Ag:AgCl reference electrode. The reaction layer of the biosensor is created by the direct immobilisation of PSAO at the electrode surface via affinity carrier BAT-Silasorb. Used arrangement facilitates a simple restoration of the inactive biosensor. An amperometric signal results from horseradish peroxidase catalysed reduction of H2O2, a secondary product of the oxidative deamination of amines, catalysed by PSAO. The sensor was used for the basic characterisation of 55 biogenic and synthetic amines, from numerous mono-, di- and polyamines to various hydroxy-, thio-, benzyl- and aromatic derivatives in order to establish its suitability as a postcolumn detector. Its high sensitivity to putrescine, a limit of detection of 10 nmol/l (determined with respect to a signal-to-noise ratio 3:1), a linear range of current response to 0.01-100 mmol/l concentration of substrate and good reproducibility all indicate that the sensor could be applied to future industrial and clinical analyses.

Links

MSM 143100005, plan (intention)

Name: Strukturně-funkční vztahy biomolekul a jejich role v metabolismu

Investor: Ministry of Education, Youth and Sports of the CR, Biomolecular Structure-function Relationships and their role in the Metabolism

Citovat

WIMMEROVÁ, Michaela and Lumír MACHOLÁN. Sensitive amperometric biosensor for the determination of biogenic and synthetic amines using pea seedling amine oxidase: a novel approach for enzyme immobilisation. Biosensors & Bioelectronics. Oxford: Elsevier Advanced Technology, 1999, vol. 14, 8-9, p. 695-702. ISSN 0956-5663.

@article{214772,
   author = {Wimmerová, Michaela and Macholán, Lumír},
   article_location = {Oxford},
   article_number = {8-9},
   keywords = {biosensor; amine oxidase; immobilisation},
   language = {eng},
   issn = {0956-5663},
   journal = {Biosensors & Bioelectronics},
   title = {Sensitive amperometric biosensor for the determination of biogenic and synthetic amines using pea seedling amine oxidase: a novel approach for enzyme immobilisation},
   volume = {14},
   year = {1999}
}

TY  - JOUR
ID  - 214772
AU  - Wimmerová, Michaela - Macholán, Lumír
PY  - 1999
TI  - Sensitive amperometric biosensor for the determination of biogenic and synthetic amines using pea seedling amine oxidase: a novel approach for enzyme immobilisation
JF  - Biosensors & Bioelectronics
VL  - 14
IS  - 8-9
SP  - 695
EP  - 695
PB  - Elsevier Advanced Technology
SN  - 09565663
KW  - biosensor
KW  - amine oxidase
KW  - immobilisation
N2  - We prepared a new inorganic sorbent based on modified triazine (2-[4,6-bis (aminoethylamine)-1,3,5-triazine]-Silasorb; BAT-Silasorb) which binds pea seedlings amine oxidase (PSAO) very tightly without loss of its catalytic activity. This unique feature as well as the wide substrate specificity of PSAO was successfully utilised in the construction of an amperometric biosensor based on a carbon paste electrode for the fast and sensitive detection of various amines at a formal potential 0 mV versus Ag:AgCl reference electrode. The reaction layer of the biosensor is created by the direct immobilisation of PSAO at the electrode surface via affinity carrier BAT-Silasorb. Used arrangement facilitates a simple restoration of the inactive biosensor. An amperometric signal results from horseradish peroxidase catalysed reduction of H2O2, a secondary product of the oxidative deamination of amines, catalysed by PSAO. The sensor was used for the basic characterisation of 55 biogenic and synthetic amines, from numerous mono-, di- and polyamines to various hydroxy-, thio-, benzyl- and aromatic derivatives in order to establish its suitability as a postcolumn detector. Its high sensitivity to putrescine, a limit of detection of 10 nmol/l (determined with respect to a signal-to-noise ratio 3:1), a linear range of current response to 0.01-100 mmol/l concentration of substrate and good reproducibility all indicate that the sensor could be applied to future industrial and clinical analyses.
ER  -

WIMMEROVÁ, Michaela and Lumír MACHOLÁN. Sensitive amperometric biosensor for the determination of biogenic and synthetic amines using pea seedling amine oxidase: a novel approach for enzyme immobilisation. \textit{Biosensors \&{} Bioelectronics}. Oxford: Elsevier Advanced Technology, 1999, vol.~14, 8-9, p.~695-702. ISSN~0956-5663.

Detailed Information on Publication Record