Characterization of the proteases involved in gel weakening of beef heart surimi

Baowu Wang, Youling L. Xiong

Research output: Contribution to journalArticlepeer-review

6 Scopus citations

Abstract

The goal of this study was to elucidate the nature and characteristics of the proteases involved in gel weakening of beef heart surimi. Acidic (E1) and neutral (E2) protease extracts were prepared from the surimi. The major active components in E1 were found to be cathepsins B and L. E1 exhibited optimum activity to hydrolyze substrates specific to cathepsins B and B+L at 50 °C and pH 5.5. At pH 6.0, it retained ~50% of its maximum activity. The catheptic activity of E1 was inhibited almost completely by E-64 and leupeptin. The active component in E2 was unidentified and was not inhibited by cysteine or serine protease inhibitors. However, beef plasma powder effectively inhibited the hydrolysis of FITC-casein and myosin heavy chain by E2.

Original languageEnglish
Pages (from-to)887-892
Number of pages6
JournalJournal of Agricultural and Food Chemistry
Volume47
Issue number3
DOIs
StatePublished - Mar 1999

Keywords

  • Beef heart
  • Cathepsin
  • Protease
  • Protease inhibitor
  • Surimi

ASJC Scopus subject areas

  • General Chemistry
  • General Agricultural and Biological Sciences

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