Covalent binding of 4-hydroxy-2-nonenal to lactate dehydrogenase decreases nadh formation and metmyoglobin reducing activity

Ranjith Ramanathan, Richard A. Mancini, Surendranath P. Suman, Carol M. Beach

Research output: Contribution to journalArticlepeer-review

31 Scopus citations

Abstract

Lactate dehydrogenase (LDH) activity can regenerate NADH, which is a critical component in metmyoglobin reduction. However, limited research has determined the effects of lipid oxidation products on LDH activity. The overall objective of this study was to determine the effects of 4-hydroxy-2-nonenal (HNE) on LDH activity. LDH was reacted with HNE at pH 5.6 and 7.4, and LDH activity was measured as NADH formation following the addition of lactate and NAD. The effects of HNE on NADH-dependent metmyoglobin reduction also were analyzed. Mass spectrometric examination revealed that HNE adducts to LDH at both pH 5.6 and 7.4. More specifically, HNE binds with cysteine and histidine residues of LDH at pH 5.6 and 7.4. Covalent binding of HNE decreased NADH formation and metmyoglobin reduction (P < 0.05). These results indicate that secondary lipid oxidation products can inactivate enzymes involved in metmyoglobin reduction and have the potential to increase beef discoloration.

Original languageEnglish
Pages (from-to)2112-2117
Number of pages6
JournalJournal of Agricultural and Food Chemistry
Volume62
Issue number9
DOIs
StatePublished - Mar 5 2014

Keywords

  • beef color
  • LDH
  • lipid oxidation
  • mass spectrometry
  • metmyoglobin reduction
  • NADH-dependent cytochrome b5 reductase

ASJC Scopus subject areas

  • Chemistry (all)
  • Agricultural and Biological Sciences (all)

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