An aspartic type protease degrades trypsin inhibitors, the major root storage proteins of sweet potato (Ipomoea batatas (L.) Lam cv. Tainong 57)

Wen C. Hou, Dong Jiann Huang, Yaw Huei Lin

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

Roots of sprouted sweet potato (Ipomoea batatas [L.] Lam) were used as materials to purify proteases which degraded trypsin inhibitors (TIs), the root storage proteins of sweet potato (SP). The commercial pepstatinagarose (crosslinked, 6%) was chosen as an affinity column for purification. The purified protease has a molecular mass of about 64 kDa on the gelatin-SDS-PAGE gel and was inhibited by pepstatin but not by E-64 on the gelatin-SDS-PAGE gel. Therefore, it might belong to the aspartic type. Using the trypsin inhibitor activity staining method as a criterion for TI degradations, we found that this aspartic type protease could degrade purified TIs in the presence or absence of 5 mM DTT and the hydrolysis was complete in the former condition. The physiological role of aspartic type protease in the degradation of SPTIs is discussed.

Original languageEnglish
Pages (from-to)271-276
Number of pages6
JournalBotanical Bulletin of Academia Sinica
Volume43
Issue number4
Publication statusPublished - Oct 2002
Externally publishedYes

Keywords

  • Aspartic type protease
  • Degradation
  • Physiological role
  • Sweet potato
  • Trypsin inhibitor

ASJC Scopus subject areas

  • Plant Science

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