Open AccessProtein purification from Arachis hypogaea in one step: stability studies and anticarcinogenic analysis
Author(s) -
Afaque Ahmad,
H. N. Verma,
Prahalad Singh Bharti,
Kamlesh Kumar Pandey,
Samiya Khan,
Kapil Dev
Publication year - 2019
Publication title -
food science and biotechnology/food science and biotechnology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.595
H-Index - 38
eISSN - 2092-6456
pISSN - 1226-7708
DOI - 10.1007/s10068-019-00638-0
Subject(s) - arachis hypogaea , trypsin inhibitor , hek 293 cells , ic50 , trypsin , chemistry , microbiology and biotechnology , chromatography , biochemistry , biology , in vitro , receptor , enzyme , botany
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 IC 50 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 IC 50 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.