Premium
Turning Tryptophanase into Odor‐Generating Biosensors
Author(s) -
Xu Yaqin,
Zhang Zhuyuan,
Ali M. Monsur,
Sauder Joanna,
Deng Xudong,
Giang Karen,
Aguirre Sergio D.,
Pelton Robert,
Li Yingfu,
Filipe Carlos D. M.
Publication year - 2014
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201309684
Subject(s) - biotinylation , tryptophanase , odor , biochemistry , chemistry , biosensor , enzyme , analyte , chromatography , tryptophan , amino acid , organic chemistry
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 n M 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 μ M 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.