Active recombinant thioredoxin h protein with antioxidant activities from sweet potato (Ipomoea batatas [L.] Lam Tainong 57) storage roots

Dong Jiann Huang, Hsien Jung Chen, Wen Chi Hou, Chun Der Lin, Yaw Huei Lin

Research output: Contribution to journalArticle

33 Citations (Scopus)

Abstract

Recombinant thioredoxin h (Trx2) overproduced in Escherichia colI (M 15) was purified by Ni2+-chelated affinity chromatography. The molecular mass of Trx2 is ∼1.4 kDa as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Total antioxidant status, 1,1-diphenyl-2-picrylhydrazyl (DPPH) staining, reducing power method, Fe 2+-chelating ability, ferric thiocyanate (FTC) method, and protection of calf thymus DNA against hydroxyl radical-induced damage were studied. The thioredoxin h protein with a concentration of 12.5 mg/mL exhibited the highest activity (expressed as 0.37 ± 0.012 mM ABTS radical cation being cleared) in a total antioxidant status test. In the DPPH staining thioredoxin h appeared as white spots when it was diluted to 50 mg/mL (a final amount of 15 μg). Like the total antioxidant status, the reducing power, Fe2+-chelating ability, FTC activity, and protection against hydroxyl radical-induced calf thymus DNA damage were found with the thioredoxin h protein. It was suggested that thioredoxin h might contribute to its antioxidant activities against hydroxyl and peroxyl radicals.

Original languageEnglish
Pages (from-to)4720-4724
Number of pages5
JournalJournal of Agricultural and Food Chemistry
Volume52
Issue number15
DOIs
Publication statusPublished - Jul 28 2004

Keywords

  • Antioxidant
  • CDNA sequence
  • Gene expression
  • Recombinant protein
  • Sweet potato
  • Thioredoxin h

ASJC Scopus subject areas

  • Agricultural and Biological Sciences (miscellaneous)
  • Food Science
  • Chemistry (miscellaneous)

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