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

Yulong Bao, Sjef Boeren, Per Ertbjerg

Forskningsoutput: TidskriftsbidragArtikelVetenskapligPeer review

Sammanfattning

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.
Originalspråkengelska
TidskriftMeat Science
Volym135
Sidor (från-till)102-108
Antal sidor7
ISSN0309-1740
DOI
StatusPublicerad - jan 2018
MoE-publikationstypA1 Tidskriftsartikel-refererad

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  • 416 Livsmedelsvetenskap

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

I: Meat Science, Vol. 135, 01.2018, s. 102-108.

Forskningsoutput: TidskriftsbidragArtikelVetenskapligPeer review

TY - JOUR

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

AU - Bao, Yulong

AU - Boeren, Sjef

AU - Ertbjerg, Per

PY - 2018/1

Y1 - 2018/1

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 - 416 Food Science

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

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