Denaturation of myofibrillar and sarcoplasmic proteins in pale, soft and exudative-like meat : effects on water-holding

The aim of the thesis was to investigate the interaction between sarcoplasmic proteins and myofibrillar proteins, considering the effects on the loss of water-holding in mild heat induced denaturation such as occurring in pale, soft and exudative (PSE) condition. Porcine longissimus thoracis et lumborum muscles were incubated at temperature 0, 10, 20, 30 or 40 ˚C to 6 h post mortem. Incubation at 40 ˚C reduced the water-holding of meat compared to the lower temperatures (P < 0.001). SDS-PAGE and Western blot analyses indicated that glycogen phosphorylase and creatine kinase precipitated with the myofilaments, which was already accomplished at 6 h post mortem. Substantial meat tenderization was measured after incubation at 40 ˚C, but with less activity of extracted μ- and m- calpains compared to lower temperatures (P < 0.001), which suggests that an early activation of calpains at the highest incubation temperature could have been the reason for the tenderization. Surface hydrophobicity of myofilanments was higher after the pre-rigor incubation at 40 ˚C compared to lower temperatures (P < 0.001). Less myosin subfragment-1 (S1) units were released by chymotryptic cleavage simultaneously with the loss of Ca2+ ATPase activity after incubation at 40 ˚C than at lower incubation temperatures (P < 0.001). The results suggest that the high temperature incubation induce microstructural alterations on the myosin head (S1) region, which may in turn have been related to the loss of water-holding. The roles of the denaturation of sarcoplasmic proteins and myofibrillar proteins were compared. Sarcoplasm not-incubated or incubated at 44 ˚C were mixed with protein-depleted sarcoplasm in different rations and the mixtures were combined with myofibrils and subjected to PSE-like condition pH 5.6/44 ˚C for 1 h . Water-holding was the poorest without the incubated sarcoplasmic proteins. Precipitated sarcoplasmic proteins shrank the myofilamental lattice spacing by 6.3%, compared to protein-free sarcoplasm, during post-rigor incubation at 44 ˚C, shown by X-ray diffraction. These results challenge the current understanding of the role of the denaturation of different proteins in water-holding, and therefore, a new hypothesis is proposed in this thesis: 1) in the intramyofibrillar space, the presence of precipitating sarcoplasmic proteins is associated with the filamental lattice compression that expels water; 2) in the space outside the myofibrils (intermyofibrillar space) within fiber and up to the extracellular space, the coagulated sarcoplasmic proteins form a network that traps water expelled from the intramyofibrillar space.

Grantor dc:publisher

Helsingin yliopisto

Year dc:date.issued

2016

Author dc:creator

• Liu, Jiao

• Meat Science

Statement dc:rights

• Julkaisu on tekijänoikeussäännösten alainen. Teosta voi lukea ja tulostaa henkilökohtaista käyttöä varten. Käyttö kaupallisiin tarkoituksiin on kielletty.
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• Publikationen är skyddad av upphovsrätten. Den får läsas och skrivas ut för personligt bruk. Användning i kommersiellt syfte är förbjuden.

Language dc:language.iso

eng

Handle dc:identifier.uri

http://hdl.handle.net/10138/163547

OAI record oai:identifier

https://helda.helsinki.fi/server/oai/request?verb=GetRecord&metadataPrefix=dim&identifier=oai%3Ahelda.helsinki.fi%3A10138%2F163547