Skip to Content
Merck
CN
  • Protein purification from Arachis hypogaea in one step: stability studies and anticarcinogenic analysis.

Protein purification from Arachis hypogaea in one step: stability studies and anticarcinogenic analysis.

Food science and biotechnology (2020-01-25)
Afaque Ahmad, Hirday N Verma, Prahalad Bharti, Kamlesh Pandey, Shahbaz Khan, Kapil Dev
ABSTRACT

The study involved purification of trypsin inhibitor from the seeds of Indian peanuts (Arachis hypogaea), a member of leguminosae family. The inhibitor was purified to homogeneity via three sequential step procedure i.e., salt precipitation to anion-exchange chromatography. The purity and molecular mass was detected using SDS PAGE analysis i.e. ~ 16 kDa. The purified inhibitor termed as Peanut Trypsin Inhibitor (PTI) which inhibits trypsin belonging to serpins family. Anti- neoplastic potential on breast cancer cells (MCF-7) and normal Human Embryonic Kidney cells (HEK) was determined using MTT assay. PTI exhibited IC50 value of ~ 18.412 µg/mL in HEK cells compared to ~ 9.635 µg/mL in MCF-7 cells. The values were quite comparable to curcumin, the standard anticancer drug demonstrating IC50 values of ~ 21.581 µg/mL and ~ 7.135 µg/mL in HEK and MCF-7 respectively. Therefore, we conclude that PTI may be used as supplement along with the conventional drugs for increased efficacy in the treatment of cancer.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Nα-Benzoyl-DL-arginine 4-nitroanilide hydrochloride, ≥98%