Development of an Enzyme Sensor Utilizing a Novel Fructosyl Amine Oxidase from a Marine Yeast

Tsugawa, Wakako; Ishimura, Fumimasa; Ogawa, Kinuko; Sode, Koji

doi:10.5796/electrochemistry.68.869

Cited by 36 publications

(7 citation statements)

References 13 publications

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“…N1-1 (N1-1 FAOD), and have succeeded in its cloning and recombinant production in Escherichia coli (Ferri et al, 2004). We have also reported FAOD-based biosensor systems capable of effectively measuring f-a Val (Ogawa et al, 2002;Sakaguchi et al, 2003;Tsugawa et al, 2000Tsugawa et al, , 2001.…”

Section: Introductionmentioning

confidence: 99%

Motif‐based search for a novel fructosyl peptide oxidase from genome databases

Kim

Ferri

Tsugawa

et al. 2010

Biotech & Bioengineering

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The measurement of glycated hemoglobin A1c (HbA1c) has important implications for diagnosis of diabetes and assessment of treatment effectiveness. We proposed specific sequence motifs to identify enzymes that oxidize glycated compounds from genome database searches. The gene encoding a putative fructosyl amino acid oxidase was found in the Phaeosphaeria nodorum SN15 genome and successfully expressed in Escherichia coli. The recombinant protein (XP_001798711) was confirmed to be a novel fructosyl peptide oxidase (FPOX) with high specificity for alpha-glycated compounds, such as HbA1c model compounds fructosyl-(alpha)N-valine (f-(alpha)Val) and fructosyl-(alpha)N-valyl-histidine (f-(alpha)Val-His). Unlike previously reported FPOXs, the P. nodorum FPOX has a K(m) value for f-(alpha)Val-His (0.185 mM) that is considerably lower than that for f-(alpha)Val (0.458 mM). Based on amino acid sequence alignment, three dimensional structural modeling, and site-directed mutagenesis, Gly60 was found to be a determining residue for the activity towards f-(alpha)Val-His. A flexible surface loop region was also found to likely play an important role in accepting f-(alpha)Val-His.

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Section: Introductionmentioning

confidence: 99%

Motif‐based search for a novel fructosyl peptide oxidase from genome databases

Kim

Ferri

Tsugawa

et al. 2010

Biotech & Bioengineering

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“…Our group has been engaged in the development of a variety of molecules and principles for glycated protein biosensing. [12][13][14][15][16][17][18] Especially, recent engineering studies succeeded in converting FAOX and FPOX into fructosyl amino acid dehydrogenase and fructosyl peptide dehydrogenase, respectively, by introducing mutations. 19,20 However, the FAOXs/FPOXs and the corresponding engineered dehydrogenases show relatively high K m values (10 -3 to 10 -2 M) and cannot react with intact glycated proteins.…”

mentioning

confidence: 99%

Advancing the Development of Glycated Protein Biosensing Technology

Kameya

Sakaguchi-Mikami

Ferri

et al. 2015

J Diabetes Sci Technol

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Research advances in biochemical molecules have led to the development of convenient and reproducible biosensing molecules for glycated proteins, such as those based on the enzymes fructosyl amino acid oxidase (FAOX) or fructosyl peptide oxidase (FPOX). Recently, more attractive biosensing molecules with potential applications in next-generation biosensing of glycated proteins have been aggressively reported. We review 2 such molecules, fructosamine 6-kinase (FN6K) and fructosyl amino acid-binding protein, as well as their recent applications in the development of glycated protein biosensing systems. Research on FN6K and fructosyl amino acid-binding protein has been opening up new possibilities for the development of highly sensitive and proteolytic-digestion-free biosensing systems for glycated proteins.

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“…When used for quantification of HbA1c in the presence of the redox mediator methoxy phenazine methosulfate, this sensor exhibited a detection range of 0.05–1.8 mM and a sensitivity of 0.42 μAmM −1 . When FAO was immobilized in a carbon paste electrode and crosslinked using 1% glutaraldehyde, the sensing range obtained for HbA1c in the presence of the redox mediator was between 0.2 and 2.7 mM, with a sensitivity of 1.1 μAmM −1 [ 71 ]. Other redox mediators, such as ferrocene with peroxidase and Prussian blue, were also investigated for quantification of HbA1c on the PVA-SbQ/Pt electrode.…”

Section: Biosensors Based On Fv Detectionmentioning

confidence: 99%

Trends in Quantification of HbA1c Using Electrochemical and Point-of-Care Analyzers

Mandali

Prabakaran

Annadurai

et al. 2023

Sensors

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Glycated hemoglobin (HbA1c), one of the many variants of hemoglobin (Hb), serves as a standard biomarker of diabetes, as it assesses the long-term glycemic status of the individual for the previous 90–120 days. HbA1c levels in blood are stable and do not fluctuate when compared to the random blood glucose levels. The normal level of HbA1c is 4–6.0%, while concentrations > 6.5% denote diabetes. Conventionally, HbA1c is measured using techniques such as chromatography, spectroscopy, immunoassays, capillary electrophoresis, fluorometry, etc., that are time-consuming, expensive, and involve complex procedures and skilled personnel. These limitations have spurred development of sensors incorporating nanostructured materials that can aid in specific and accurate quantification of HbA1c. Various chemical and biological sensing elements with and without nanoparticle interfaces have been explored for HbA1c detection. Attempts are underway to improve the detection speed, increase accuracy, and reduce sample volumes and detection costs through different combinations of nanomaterials, interfaces, capture elements, and measurement techniques. This review elaborates on the recent advances in the realm of electrochemical detection for HbA1c detection. It also discusses the emerging trends and challenges in the fabrication of effective, accurate, and cost-effective point-of-care (PoC) devices for HbA1c and the potential way forward.

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Development of an Enzyme Sensor Utilizing a Novel Fructosyl Amine Oxidase from a Marine Yeast

Cited by 36 publications

References 13 publications

Motif‐based search for a novel fructosyl peptide oxidase from genome databases

Motif‐based search for a novel fructosyl peptide oxidase from genome databases

Advancing the Development of Glycated Protein Biosensing Technology

Trends in Quantification of HbA1c Using Electrochemical and Point-of-Care Analyzers

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