Details

Autor(en) / Beteiligte

• Xu, Yaqin
• Zhang, Zhuyuan
• Ali, M. Monsur
• Sauder, Joanna
• Deng, Xudong
• Giang, Karen
• Aguirre, Sergio D.
• Pelton, Robert
• Li, Yingfu
• Filipe, Carlos D. M.

Titel

Turning Tryptophanase into Odor-Generating Biosensors

Ist Teil von

• Angewandte Chemie International Edition, 2014-03, Vol.53 (10), p.2620-2622

Auflage

International ed. in English

Ort / Verlag

Weinheim: WILEY-VCH Verlag

Erscheinungsjahr

2014

Quelle

MEDLINE

Beschreibungen/Notizen

• An odor‐based sensor system that exploits the metabolic enzyme tryptophanase (TPase) as the key component is reported. This enzyme is able to convert an odorless substrate like S‐methyl‐L‐cysteine or L‐tryptophan into the odorous products methyl mercaptan or indole. To make a biosensor, TPase was biotinylated so that it could be coupled with a molecular recognition element, such as an antibody, to develop an ELISA‐like assay. This method was used for the detection of an antibody present in nM concentrations by the human nose. TPase can also be combined with the enzyme pyridoxal kinase (PKase) for use in a coupled assay to detect adenosine 5′‐triphosphate (ATP). When ATP is present in the low μM concentration range, the coupled enzymatic system generates an odor that is easily detectable by the human nose. Biotinylated TPase can be combined with various biotin‐labeled molecular recognition elements, thereby enabling a broad range of applications for this odor‐based reporting system. The nose knows: Tryptophanase (TPase), which converts S‐methyl‐L‐cysteine into methyl mercaptan (smelly), was coupled to a molecular recognition element (such as an antibody) to create an odor‐based biosensor. Biotinylated TPase could be combined with various biotin‐labeled molecular recognition elements, thereby enabling a broad range of applications for this odor‐based reporting system.