A flow-through enzyme analyzer for determination of L-lysine concentration

Simonian, Aleksandr; Khachatrian, G. E.; Tatikian, S.; Авакян, Ц. М.; Badalian, I. E.

doi:10.1016/0956-5663(91)87032-7

Cited by 28 publications

(15 citation statements)

References 6 publications

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“…Various approaches have been made to develop potentiometric , , amperometric and optical , biosensing systems for L‐lysine determination. In L‐lysine biosensors L‐lysine dehydrogenase , L‐lysine‐2‐monooxygenase , L‐lysine‐decarboxylase and L‐lysine‐(α)‐oxidase enzymes have been used as biological recognition element for biosensor fabrication. L‐lysine‐decarboxylase catalyzes the formation of cadeverine and CO 2 from L‐lysine.…”

Section: Introductionmentioning

confidence: 99%

Graphene/Poly(vinylferrocene) Composite Based Amperometric Biosensor for L‐lysine Determination

2017

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A novel and sensitive amperometric biosensor for L‐lysine determination based on a glassy carbon electrode (GCE) modified with graphene (GR) and redox polymer poly(vinylferrocene) (PVF) was constructed. L‐lysine‐α‐oxidase was immobilized onto the modified GCE by a glutaraldehyde/bovine serum albumin cross‐linking procedure. SEM, CV and EIS were used for the characterization of the surface morphology and stepwise fabrication processes of PVF/GR composite. Optimal composition of the biosensor and experimental conditions that affect the performance of the biosensor are discussed. The effect of buffer pH on biosensor response was studied in detail over a wide pH range. L‐lysine biosensor displayed a linear range of 9.9×10−7 ‐ 3.1×10−4 M with a low detection limit of 2.3×10−7 M and KMapp value of 0.4 mM. The L‐lysine biosensor was tested using pharmaceutical sample and cheese with satisfactory results.

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Section: Introductionmentioning

confidence: 99%

Graphene/Poly(vinylferrocene) Composite Based Amperometric Biosensor for L‐lysine Determination

2017

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“…Different lysine selective enzymes have been used as biological recognition element for sensor construction: L ‐lysine dehydrogenase (LDH, EC 1.4.1.15) 7, L ‐lysine‐2‐monooxygenase (LMO, EC 4.13.12.2) 8, L ‐lysine‐decarboxylase (LDC, EC 4.1.1.18) 9,10 and L ‐lysine‐(α)‐oxidase (LOX, EC 1.4.3.14) 2,3,11–25. A summary of L ‐lysine biosensors is presented in Table 1.…”

Section: Introductionmentioning

confidence: 99%

Novel Amperometric Tri‐Enzyme Biosensor for Lysine Determination in Pharmaceutical Products and Food Samples

et al. 2015

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An enzyme‐based amperometric biosensor was developed for the determination of the lysine content of pharmaceutical products, food and feed samples. Lysine decarboxylase (EC 4.1.1.18) from Bacterium cadaveris was coupled with diamine oxidase (EC 1.4.3.6) from Pisum sativum and horseradish peroxidase (EC 1.11.1.7). The enzymes were co‐immobilized on a graphite electrode with an Os polymer. The biosensor worked in flow injection analysis system (FIA). Optimal working conditions were pH 7.0 and −50 mV potential vs. Ag/AgCl. The linear measuring range was 0.005–0.500 mM. Different pharmaceutical products and feed samples were analysed by the lysine biosensor and by HPLC method for validation.

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“…Total amino acids are commonly measured by time consuming chemical methods. Enzyme electrodes for amino acids have been developed by coupling an enzyme to a membrane (Simonian et al 1991;Johansson et al 1976). Immobilized L-amino acid oxidase (LAAO) degrades L-amino acids to 2-0x0 acid, ammonia and hydrogen peroxide.…”

Section: Introductionmentioning

confidence: 99%

Development of a Biosensor With Immobilized L-Amino Acid Oxidase for Determination of L-Amino Acids

Lee¹,

Huh²

1999

J Food Biochemistry

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The objectives of this research were to investigate conditions for immobilization of L‐amino acid oxidase (LAAO) on a preactivated nylon membrane, and to develop an enzyme sensor which can detect ammonia. LAAO was immobilized onto a preactivated nylon membrane. Optimal immobilization conditions were 0.3% glutaraldehyde, 1 mg bovine serum albumin, and 1.6 units of enzyme with 2 h coupling time. The enzymic membrane and an ammonium selective nonactin membrane were attached to an ammonia electrode to fabricate an L‐amino acid sensor. L‐amino acids were enzymatically degraded by immobilized LAAO, and the ammonia generated was measured by a potentiometric electrode at pH 8.5 and 45C. The sensor showed high relative activities for L‐amino acids, and the responses of the sensor for phenylalanine and isoleucine were linear to 10 mM with a detection limit of 0.05 mM. The L‐amino acid sensor was applied for monitoring increases in amino acids levels, expressed as L‐isoleucine equivalents, during yeast autolysis. Determination of L‐amino acids was complete in 3 min. Moreover, the activity of the enzymic membrane was stable for at least 260 assays, and did not noticeably decline for 2 months.

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A flow-through enzyme analyzer for determination of L-lysine concentration

Cited by 28 publications

References 6 publications

Graphene/Poly(vinylferrocene) Composite Based Amperometric Biosensor for L‐lysine Determination

Graphene/Poly(vinylferrocene) Composite Based Amperometric Biosensor for L‐lysine Determination

Novel Amperometric Tri‐Enzyme Biosensor for Lysine Determination in Pharmaceutical Products and Food Samples

Development of a Biosensor With Immobilized L-Amino Acid Oxidase for Determination of L-Amino Acids

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