No abstract

Online) Journal homepage: https://www.tandfonline.com/loi/ljfp20 Antioxidant activity and DNA protection against oxidative damage of bambara groundnut seeds (Vigna subterranea (L.) Verdc.) as affected by processing methods Dutsadee ChinnapunTo cite this article: Dutsadee Chinnapun (2018) Antioxidant activity and DNA protection against oxidative damage of bambara groundnut seeds (Vignasubterranea (L.) Verdc.) as affected by processing methodsABSTRACT This research investigated the effects of processing by dry heating, boiling, and steaming on the antioxidant activity and DNA protection against oxidative damage of bambara groundnut seeds (Vigna subterranea (L.) Verdc.). Comparing raw and processed samples of bambara groundnut seeds, dry heating caused a significant (P < 0.05) reduction of ferric-reducing antioxidant power (FRAP), metal chelating activity, DPPH • and ABTS •+ radical scavenging activity. The boiling process did not cause a significant difference in FRAP and metal chelating activity and caused smaller losses in DPPH • and ABTS •+ radical scavenging activity than the dry heating and steaming processes. The steaming process caused a significant (P < 0.05) reduction of FRAP, DPPH • and ABTS •+ radical scavenging activity. For DNA protection against oxidative damage, boiled and steamed bambara groundnut seed samples were more effective with a lower minimum concentration (50 µg/mL) than raw and dry heated samples. These results indicated that the boiling process caused smaller losses antioxidant activity than dry heating and steaming. Therefore, boiling was recommended as processing method for bambara groundnut seeds to preserve antioxidant components and antioxidant activity. ARTICLE HISTORY

A novel serine protease inhibitor gene was isolated from Hevea brasiliensis leaves, a RRIT251 cultivar and designated RRIT251 H. brasiliensis protease inhibitor (251Hbpi). Reverse transcription polymerase chain reaction (RT-PCR) and rapid amplification of cDNA ends (RACE) were used to isolate 251Hbpi. A full-length cDNA of 251Hbpi encoded a 70 amino acid protein. 251HbPI is a member of the potato inhibitor I (PI-I) family of serine protease inhibitors. The amino acid residues at the active site of 251HbPI were predicted as Met 46-Glu 47. Multiple alignments of the homologous PI-I family revealed one motif WPELVG of 251HbPI conserved across the family. 251Hbpi was cloned into expression vector pFLAG-ATS and expressed in Escherichia coli strain BL21. Molecular weight of the recombinant 251HbPI (r251HbPI) was approximately 11 kDa. Protease inhibition analysis revealed that r251HbPI inhibited the activity of chymotrypsin and subtilisin A but did not trypsin protease. Moreover, purified r251HbPI protein inhibited Trichophyton rubrum with a minimum inhibitory concentration of 0.7 mg/ml and a minimum fungicidal concentration of 1.4 mg/ml. The specific T. rubrum protease targets of r251HbPI were analyzed by co-immunoprecipitation. r251HbPI interacted with approximate 27 and 61 kDa T. rubrum proteins, suggesting a role in the inhibition of T. rubrum growth. These results suggest that 251HbPI could be a candidate for the development of a novel drug to treat T. rubrum infection.

No abstract