ENZYMATIC DEGRADATION OF GLIADIN BY NIGELLA SATIVA SEEDS PROTEASE: IMPLICATIONS FOR NEW TREATMENT OF CELIAC DISEASE
Nousseiba Bellir*, Mohamed Nacer Bellir, Leila Rouabah
ABSTRACT
The protease was extracted from Nigella sativa seeds with 0,1 M
citrate/phosphate buffer (pH 7,5), the crude enzyme extract
showed maximum protease activity at pH 1,5 ,and optimal
temperature at 50°C. After the partially purification of enzyme
and analyses of RP-HPLC and SDS-PAGE results it appeared
that Nigella sativa seeds protease degrade Triticum aestivum
gliadin more efficiently than Triticum durum gliadin after 24h of
incubation. The activity of Nigella sativa seeds protease with gliadin as
substrate, in pH 7,5 at 37°C after 2h of incubation, before and after
partial enzymatic purification prove that the crude enzyme extract
have a low activity with Triticum durum gliadin however it was
important with Triticum aestivum gliadin, this protease activity was
increased in the same conditions using partially purified enzyme and it
persist always higer with Triticum durum gliadin comparing with Triticum aestivum gliadin.
On the bases of these results, Nigella sativa seeds protease represent the alternative means of
treating celiac disease in the future using the detoxification of gliadin to eliminate the
immunogenicity of gluten.
Keywords: Gliadin, Celiac disease, Nigella sativa, Protease.
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