On the origin of thaw loss

Relationship between freezing rate and protein denaturation

Tutkimustuotos: ArtikkelijulkaisuArtikkeliTieteellinenvertaisarvioitu

Kuvaus

The role of protein denaturation in formation of thaw loss is currently not well understood. This study investigated denaturation of myofibrillar and sarcoplasmic proteins of pork loins caused by freezing-thawing in relation to freezing rate. Compared to fast freezing, slow freezing caused 28% larger thaw loss, decreased water-holding capacity of myofibrils and increased surface hydrophobicity, indicating more pronounced denaturation of myofibrillar proteins. We here propose a model: In slow freezing protons are concentrated in the unfrozen water resulting in reduced pH in proximity of structural proteins causing protein denaturation. In parallel, large ice crystals are formed outside of muscle fibers resulting in transversal shrinkage. In fast freezing small ice crystals trap protons and cause less severe protein denaturation and reduced thaw loss. Differential scanning calorimetry and tryptophan fluorescence spectra indicated sarcoplasmic protein denaturation in drip due to freezing-thawing. However, sarcoplasmic protein denaturation was independent of freezing rate.
Alkuperäiskielienglanti
Artikkeli125104
LehtiFood Chemistry
Vuosikerta299
ISSN0308-8146
DOI - pysyväislinkit
TilaJulkaistu - 29 kesäkuuta 2019
OKM-julkaisutyyppiA1 Alkuperäisartikkeli tieteellisessä aikakauslehdessä, vertaisarvioitu

Tieteenalat

  • 416 Elintarviketieteet

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title = "On the origin of thaw loss: Relationship between freezing rate and protein denaturation",
abstract = "The role of protein denaturation in formation of thaw loss is currently not well understood. This study investigated denaturation of myofibrillar and sarcoplasmic proteins of pork loins caused by freezing-thawing in relation to freezing rate. Compared to fast freezing, slow freezing caused 28{\%} larger thaw loss, decreased water-holding capacity of myofibrils and increased surface hydrophobicity, indicating more pronounced denaturation of myofibrillar proteins. We here propose a model: In slow freezing protons are concentrated in the unfrozen water resulting in reduced pH in proximity of structural proteins causing protein denaturation. In parallel, large ice crystals are formed outside of muscle fibers resulting in transversal shrinkage. In fast freezing small ice crystals trap protons and cause less severe protein denaturation and reduced thaw loss. Differential scanning calorimetry and tryptophan fluorescence spectra indicated sarcoplasmic protein denaturation in drip due to freezing-thawing. However, sarcoplasmic protein denaturation was independent of freezing rate.",
keywords = "Meat, Ice crystal formation, Purge loss, Myofibril structure, DSC, 416 Food Science",
author = "Yuemei Zhang and Per Ertbjerg",
year = "2019",
month = "6",
day = "29",
doi = "10.1016/j.foodchem.2019.125104",
language = "English",
volume = "299",
journal = "Food Chemistry",
issn = "0308-8146",
publisher = "ELSEVIER SCI IRELAND LTD",

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On the origin of thaw loss : Relationship between freezing rate and protein denaturation. / Zhang, Yuemei; Ertbjerg, Per.

julkaisussa: Food Chemistry, Vuosikerta 299, 125104, 29.06.2019.

Tutkimustuotos: ArtikkelijulkaisuArtikkeliTieteellinenvertaisarvioitu

TY - JOUR

T1 - On the origin of thaw loss

T2 - Relationship between freezing rate and protein denaturation

AU - Zhang, Yuemei

AU - Ertbjerg, Per

PY - 2019/6/29

Y1 - 2019/6/29

N2 - The role of protein denaturation in formation of thaw loss is currently not well understood. This study investigated denaturation of myofibrillar and sarcoplasmic proteins of pork loins caused by freezing-thawing in relation to freezing rate. Compared to fast freezing, slow freezing caused 28% larger thaw loss, decreased water-holding capacity of myofibrils and increased surface hydrophobicity, indicating more pronounced denaturation of myofibrillar proteins. We here propose a model: In slow freezing protons are concentrated in the unfrozen water resulting in reduced pH in proximity of structural proteins causing protein denaturation. In parallel, large ice crystals are formed outside of muscle fibers resulting in transversal shrinkage. In fast freezing small ice crystals trap protons and cause less severe protein denaturation and reduced thaw loss. Differential scanning calorimetry and tryptophan fluorescence spectra indicated sarcoplasmic protein denaturation in drip due to freezing-thawing. However, sarcoplasmic protein denaturation was independent of freezing rate.

AB - The role of protein denaturation in formation of thaw loss is currently not well understood. This study investigated denaturation of myofibrillar and sarcoplasmic proteins of pork loins caused by freezing-thawing in relation to freezing rate. Compared to fast freezing, slow freezing caused 28% larger thaw loss, decreased water-holding capacity of myofibrils and increased surface hydrophobicity, indicating more pronounced denaturation of myofibrillar proteins. We here propose a model: In slow freezing protons are concentrated in the unfrozen water resulting in reduced pH in proximity of structural proteins causing protein denaturation. In parallel, large ice crystals are formed outside of muscle fibers resulting in transversal shrinkage. In fast freezing small ice crystals trap protons and cause less severe protein denaturation and reduced thaw loss. Differential scanning calorimetry and tryptophan fluorescence spectra indicated sarcoplasmic protein denaturation in drip due to freezing-thawing. However, sarcoplasmic protein denaturation was independent of freezing rate.

KW - Meat

KW - Ice crystal formation

KW - Purge loss

KW - Myofibril structure

KW - DSC

KW - 416 Food Science

U2 - 10.1016/j.foodchem.2019.125104

DO - 10.1016/j.foodchem.2019.125104

M3 - Article

VL - 299

JO - Food Chemistry

JF - Food Chemistry

SN - 0308-8146

M1 - 125104

ER -