Enzyme hydrolysate of silk protein suppresses tert-butyl hydroperoxide-induced hepatotoxicity by enhancing antioxidant activity in rats

Hyung Joo Suh, Bobin Kang, Chae Young Kim, Hyeon Son Choi

Research output: Contribution to journalArticle


The purpose of current study is to investigate the beneficial effect of enzyme (Alcalase) hydrolysates of silk protein in rat. Alcalase-treated silk protein hydrolysate (ATSH) itself did not show any cytotoxicity on the hepatic tissues and blood biochemistry, similar to the normal condition. ATSH played a protective role in tert-butyl hydroperoxide (t-BHP)-induced hepatotoxicity and liver damage. The values of AST (aspartate aminotransferase) and ALT (alanine aminotransferase), which are the indicators of the liver function, were effectively alleviated with the ATSH treatment in a dose dependent manner. The level of Lactate dehydrogenase (LDH) and Malondialdehyde (MDA), which were increased with t-BHP treatment, were significantly reduced by ATSH. High dose of ATSH (2 g/kg) reduced the t-BHP-induced LDH release by 48%. Antioxidant and antioxidant enzymes in liver cells were significantly increased by ATSH treatment in their level and activities. ATSH (2 g/kg) increased glutathione (GSH), an intracelluar antioxidant, by 2.5-fold compared with the t-BHP treated group. The activities of glutathione-s-transferase (GST), superoxide dismutase (SOD), and catalase were also elevated by 38%, 60%, and 45%, respectively, with ATSH (2 g/kg) treatment. The antioxidative effect of ATSH was recapitulated to the protection from t-BHP induced liver damages in hematoxylin and eosin (H&E) staining. Thus, ATSH might be used as a hepatoprotective agent.

Original languageEnglish
Pages (from-to)550-558
Number of pages9
JournalKorean Journal of Food Preservation
Issue number4
Publication statusPublished - 2017 Jul 1



  • Antioxidant enzymes
  • Hepatoprotective effect
  • Liver damage
  • Silk proteins hydrolysate
  • Tert-butyl hydroperoxide

ASJC Scopus subject areas

  • Food Science

Cite this