Kinetics of Myoglobin Redox Form Stabilization by Malate Dehydrogenase

This study reports the reduction of metmyoglobin (MMb) via oxidation of malate to oxaloacetate and the regeneration of reduced nicotinamide adenine dinucleotide (NADH) via malate dehydrogenase (MDH). Two experiments were conducted to evaluate a malate−MDH−NADH system as a possible mechanism for MMb...

Full description

Saved in:
Bibliographic Details
Published in:Journal of agricultural and food chemistry 2010-06, Vol.58 (11), p.6994-7000
Main Authors: Mohan, Anand, Muthukrishnan, S, Hunt, Melvin C, Barstow, Thomas J, Houser, Terry A
Format: Article
Language:English
Subjects:
animal tissue extracts
Animals
beef
Biological and medical sciences
Cattle
chemical concentration
enzyme activity
Enzyme Stability
Food Chemistry/Biochemistry
Food industries
Fundamental and applied biological sciences. Psychology
Horses
Kinetics
malate dehydrogenase
Malate Dehydrogenase - chemistry
Malates - chemistry
malic acid
Meat and meat product industries
metmyoglobin
muscle tissues
Myocardium - enzymology
myoglobin
Myoglobin - chemistry
NAD (coenzyme)
oxaloacetic acid
Oxaloacetic Acid - chemistry
oxidation
Oxidation-Reduction
reduction
temperature
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:This study reports the reduction of metmyoglobin (MMb) via oxidation of malate to oxaloacetate and the regeneration of reduced nicotinamide adenine dinucleotide (NADH) via malate dehydrogenase (MDH). Two experiments were conducted to evaluate a malate−MDH−NADH system as a possible mechanism for MMb reduction. In experiment 1, kinetics of MDH and MMb reduction were determined, and the results showed that increasing concentrations of oxidized nicotinamide adenine dinucleotide (NAD+) and l-malate also increased (p < 0.05) MMb reduction in vitro. Experiment 2 assessed the reducing activity of beef muscle extracts with different concentrations of malate and NAD+ added. Reduction of MMb in the muscle extracts via MDH was NAD+, malate, and extract concentration dependent (p < 0.05). A new mechanism is described for the nonspecific and specific enzymatic reduction of MMb, which supports the hypothesis that malate can replenish NADH via MDH activity in post-mortem muscle, ultimately resulting in a more functional meat color.
ISSN:0021-8561
1520-5118
DOI:10.1021/jf100639n