Myofibrillar protein oxidation affects filament charges, aggregation and water-holding

Yulong Bao, Sjef Boeren, Per Ertbjerg*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

23 Citations (Scopus)

Abstract

Hypochlorous acid (HClO) is a strong oxidant that is able to mediate protein oxidation. In order to study the effect of oxidation on charges, aggregation and water-holding of myofibrillar proteins, extracted myofibrils were oxidized by incubation with different concentrations of HClO (0, 1, 5, and 10 mM). Loss of free thiols, loss of histidine and formation of carbonyls were greater with increasing oxidation level and the particle size increased. Water-holding in the 5 and 10 mM HClO groups were greater than in the non-oxidized control. Isoelectric focusing (IEF) showed that the isoelectric point (pI) of oxidized proteins were lower compared to non-oxidized ones. The lower pI values of oxidized proteins suggests that oxidation increased the overall net negative charge of myofibrillar proteins solubilized for IEF. Here we propose a hypothesis that oxidation-induced increase in net negative charges is the driving force for improved water-holding in myofibrils, whereas protein cross-linking and aggregation have an opposing effect by decreasing the water-holding.

Original languageEnglish
Pages (from-to)102-108
JournalMeat Science
Volume135
DOIs
Publication statusPublished - 2018

Fingerprint

myofibrillar proteins
oxidation
Hypochlorous Acid
Water
myofibrils
isoelectric focusing
Proteins
Myofibrils
water
Isoelectric Focusing
acids
proteins
protein value
isoelectric point
thiols
crosslinking
histidine
oxidants
Isoelectric Point
particle size

Keywords

  • Carbonyls
  • Free thiols
  • Histidine
  • Isoelectric point
  • Particle size

Cite this

@article{b19d4eec1dd04d3cad44e3369e88a2ee,
title = "Myofibrillar protein oxidation affects filament charges, aggregation and water-holding",
abstract = "Hypochlorous acid (HClO) is a strong oxidant that is able to mediate protein oxidation. In order to study the effect of oxidation on charges, aggregation and water-holding of myofibrillar proteins, extracted myofibrils were oxidized by incubation with different concentrations of HClO (0, 1, 5, and 10 mM). Loss of free thiols, loss of histidine and formation of carbonyls were greater with increasing oxidation level and the particle size increased. Water-holding in the 5 and 10 mM HClO groups were greater than in the non-oxidized control. Isoelectric focusing (IEF) showed that the isoelectric point (pI) of oxidized proteins were lower compared to non-oxidized ones. The lower pI values of oxidized proteins suggests that oxidation increased the overall net negative charge of myofibrillar proteins solubilized for IEF. Here we propose a hypothesis that oxidation-induced increase in net negative charges is the driving force for improved water-holding in myofibrils, whereas protein cross-linking and aggregation have an opposing effect by decreasing the water-holding.",
keywords = "Carbonyls, Free thiols, Histidine, Isoelectric point, Particle size",
author = "Yulong Bao and Sjef Boeren and Per Ertbjerg",
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language = "English",
volume = "135",
pages = "102--108",
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publisher = "Elsevier",

}

Myofibrillar protein oxidation affects filament charges, aggregation and water-holding. / Bao, Yulong; Boeren, Sjef; Ertbjerg, Per.

In: Meat Science, Vol. 135, 2018, p. 102-108.

Research output: Contribution to journalArticleAcademicpeer-review

TY - JOUR

T1 - Myofibrillar protein oxidation affects filament charges, aggregation and water-holding

AU - Bao, Yulong

AU - Boeren, Sjef

AU - Ertbjerg, Per

PY - 2018

Y1 - 2018

N2 - Hypochlorous acid (HClO) is a strong oxidant that is able to mediate protein oxidation. In order to study the effect of oxidation on charges, aggregation and water-holding of myofibrillar proteins, extracted myofibrils were oxidized by incubation with different concentrations of HClO (0, 1, 5, and 10 mM). Loss of free thiols, loss of histidine and formation of carbonyls were greater with increasing oxidation level and the particle size increased. Water-holding in the 5 and 10 mM HClO groups were greater than in the non-oxidized control. Isoelectric focusing (IEF) showed that the isoelectric point (pI) of oxidized proteins were lower compared to non-oxidized ones. The lower pI values of oxidized proteins suggests that oxidation increased the overall net negative charge of myofibrillar proteins solubilized for IEF. Here we propose a hypothesis that oxidation-induced increase in net negative charges is the driving force for improved water-holding in myofibrils, whereas protein cross-linking and aggregation have an opposing effect by decreasing the water-holding.

AB - Hypochlorous acid (HClO) is a strong oxidant that is able to mediate protein oxidation. In order to study the effect of oxidation on charges, aggregation and water-holding of myofibrillar proteins, extracted myofibrils were oxidized by incubation with different concentrations of HClO (0, 1, 5, and 10 mM). Loss of free thiols, loss of histidine and formation of carbonyls were greater with increasing oxidation level and the particle size increased. Water-holding in the 5 and 10 mM HClO groups were greater than in the non-oxidized control. Isoelectric focusing (IEF) showed that the isoelectric point (pI) of oxidized proteins were lower compared to non-oxidized ones. The lower pI values of oxidized proteins suggests that oxidation increased the overall net negative charge of myofibrillar proteins solubilized for IEF. Here we propose a hypothesis that oxidation-induced increase in net negative charges is the driving force for improved water-holding in myofibrils, whereas protein cross-linking and aggregation have an opposing effect by decreasing the water-holding.

KW - Carbonyls

KW - Free thiols

KW - Histidine

KW - Isoelectric point

KW - Particle size

U2 - 10.1016/j.meatsci.2017.09.011

DO - 10.1016/j.meatsci.2017.09.011

M3 - Article

VL - 135

SP - 102

EP - 108

JO - Meat Science

JF - Meat Science

SN - 0309-1740

ER -