.
The application of an odorant binding protein for
odour control and fragrance delayed release from a textile
surface was first explored in this work. Pig
OBP-1
gene was
cloned and expressed in
Escherichia coli
, and the purified
protein was biochemically characterized. The IC
50
values
(concentrations of competitor that caused a decay of fluores-
cence to half-maximal intensity) were determined for four
distinct fragrances, namely, citronellol, benzyl benzoate,
citronellyl valerate and ethyl valerate. The results showed a
strong binding of citronellyl valerate, citronellol and benzyl
benzoate to the recombinant protein, while ethyl valerate
displayed weaker binding. Cationized cotton substrates were
coated with porcine odorant binding protein and tested for
their capacity to retain citronellol and to mask the smell of
cigarette smoke. The immobilized protein delayed the release
of citronellol when compared to the untreated cotton.
According to a blind evaluation of 30 assessors, the smell of
cigarette smoke, trapped onto the fabrics
’
surface, was suc-
cessfully attenuated by porcine odorant binding protein (more
than 60 % identified the weakest smell intensity after protein
exposure compared to
β
-cyclodextrin-treated and untreated