Preliminary study of a microbeads based histamine detection for food analysis using thermostable recombinant histamine oxidase from Arthrobacter crystallopoietes KAIT-B-007

Ito, Tetsuo; Hiroi, Tetsuya; Amaya, Tsutomu; Kaneko, Satoru; Araki, Mayumi; Ohsawa, Toshiyuki; Yamamura, Akira; Matsumoto, Kunio

doi:10.1016/j.talanta.2008.08.018

Cited by 18 publications

(6 citation statements)

References 14 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Among BAs, histamine is the most biochemically active amines and has been widely addressed as one of the fundamental primary amines in food analysis, especially in fishery industries (Ito et al 2009 ). Scombroid and non-scombroid fish have been shown to have a high concentration of free l -histidine (histamine precursor) in their skeletal muscles (Biji et al 2016 ).…”

Section: Introductionmentioning

confidence: 99%

A novel thermostable alkaline histamine oxidase from Glutamicibacter sp. N1A3101, induced by histamine and its analogue betahistine

et al. 2020

View full text Add to dashboard Cite

Biogenic amines (BAs) are low molecular weight organic bases formed by natural amino acids decarboxylation and trigger an array of toxicological effects in humans and animals. Bacterial amine oxidases enzymes are determined as practical tools to implement the rapid quantification of BAs in foods. Our study set out to obtain a new efficient, amine oxidase enzyme for developing new enzyme-based quantification of histamine. The soils from different sources were screened using histamine as sole carbon and nitrogen sources, and histamine oxidase producing bacteria were selected and identified using specific primers for histamine oxidase (HOD) gene. The HOD gene of six strains, out of 26 isolated histamine-utilizing bacteria, were amplified using our designed primers. The HOD enzyme from Glutamicibacter sp. N1A3101, isolated from nettle soil, was found to be thermostable and showed the highest substrate specificity toward the histamine and with no detected activity in the presence of putrescine, cadaverine, spermine, and spermidine. Its oxidation activity toward tyramine was lower than other HOD reported so far. The isolated enzyme was stable at 60 °C for 30 min and showed pH stability ranging from 6 to 9. Furthermore, we indicated the induction of identified HOD activity in the presence of betahistine as well, with nearly equal efficiency and without the consumption of the substrate.

show abstract

Section: Introductionmentioning

confidence: 99%

A novel thermostable alkaline histamine oxidase from Glutamicibacter sp. N1A3101, induced by histamine and its analogue betahistine

et al. 2020

View full text Add to dashboard Cite

show abstract

“…Among BAs, histamine is the most biochemically active amines and has been widely addressed as one of the fundamental primary amines in food analysis, especially in shery industries (Ito et al 2009).…”

Section: Introductionmentioning

confidence: 99%

A novel thermostable alkaline histamine oxidase from Glutamicibacter sp. N1A310, induced by histamine and its analogue betahistine

Sadeghi

Arjmand

Siadat

et al. 2020

Preprint

View full text Add to dashboard Cite

Biogenic amines (BAs) are low molecular weight organic bases formed by natural amino acids decarboxylation and trigger an array of toxicological effects in humans and animals. Bacterial amine oxidases enzymes are determined as practical tools to implement the rapid quantification of BAs in foods. Our study set out to obtain a new efficient, amine oxidase enzyme for developing new enzyme-based quantification of histamine. The soils from different sources were screened using histamine as sole carbon and nitrogen sources, and histamine oxidase producing bacteria were selected and identified using specific primers for histamine oxidase (HOD) gene. The HOD gene of six strains, out of 26 isolated histamine-utilizing bacteria, were amplified using our designed primers. The HOD enzyme from Glutamicibacter sp. N1A3101, isolated from nettle soil, was found to be thermostable and showed the highest substrate specificity toward the histamine and with no detected activity in the presence of putrescine, cadaverine, spermine, and spermidine. Its oxidation activity toward tyramine was lower than other HOD reported so far. The isolated enzyme was stable at 60 °C for 30 min and showed pH stability ranging from 6–9. Furthermore, we indicated the induction of identified HOD activity in the presence of betahistine as well, with nearly equal efficiency and without the consumption of the substrate.

show abstract

“…BAs are non-volatile, low molecular weight nitrogenous organic bases which are formed through decarboxylation of amino acids by amino acid-speci c decarboxylases These amines are naturally produced and degraded in humans, animals, plants, and microorganisms and result in numerous biological functions ( Among BAs, histamine is the most biochemically active amines and has been widely addressed as one of the fundamental primary amines in food analysis, especially in shery industries (Ito et al 2009). Scombroid and non-scombroid sh have been shown to have a high concentration of free L-histidine (histamine precursor) in their skeletal muscles (Biji et al 2016).…”

Section: Introductionmentioning

confidence: 99%

A novel thermostable alkaline histamine oxidase from Glutamicibacter sp. N1A310, induced by histamine and its analogue betahistine

Sadeghi

Arjmand

Siadat

et al. 2020

Preprint

View full text Add to dashboard Cite

Biogenic amines (BAs) are low molecular weight organic bases formed by natural amino acids decarboxylation and trigger an array of toxicological effects in humans and animals. Bacterial amine oxidases enzymes are determined as practical tools to implement the rapid quantification of BAs in foods. Our study set out to obtain a new efficient, amine oxidase enzyme for developing new enzyme-based quantification of histamine. The soils from different sources were screened using histamine as sole carbon and nitrogen sources, and histamine oxidase producing bacteria were selected and identified using specific primers for histamine oxidase (HOD) gene. The HOD gene of six strains, out of 26 isolated histamine-utilizing bacteria, were amplified using our designed primers. The HOD enzyme from Glutamicibacter sp. N1A3101, isolated from nettle soil, was found to be thermostable and showed the highest substrate specificity toward the histamine and with no detected activity in the presence of putrescine, cadaverine, spermine, and spermidine. Its oxidation activity toward tyramine was lower than other HOD reported so far. The isolated enzyme was stable at 60 °C for 30 min and showed pH stability ranging from 6-9. Furthermore, we indicated the induction of identified HOD activity in the presence of betahistine as well, with nearly equal efficiency and without the consumption of the substrate.

show abstract

Preliminary study of a microbeads based histamine detection for food analysis using thermostable recombinant histamine oxidase from Arthrobacter crystallopoietes KAIT-B-007

Cited by 18 publications

References 14 publications

A novel thermostable alkaline histamine oxidase from Glutamicibacter sp. N1A3101, induced by histamine and its analogue betahistine

A novel thermostable alkaline histamine oxidase from Glutamicibacter sp. N1A3101, induced by histamine and its analogue betahistine

A novel thermostable alkaline histamine oxidase from Glutamicibacter sp. N1A310, induced by histamine and its analogue betahistine

A novel thermostable alkaline histamine oxidase from Glutamicibacter sp. N1A310, induced by histamine and its analogue betahistine

Contact Info

Product

Resources

About