This study aimed to investigate the effect of storage at− 3° C on myofibrillar protein in fast or
slow frozen pork. Five pork loins at 48 h post-mortem were subjected to either fast (cold …

Abstract Changes in thermal stability and structure of myofibrillar protein from pork patties
with different fat addition (0%, 5%, 10%, 15% and 20%) under freeze-thaw (FT) cycles were …

This study aims at providing new insight on protein denaturation in freezing-thawing.
Freezing-thawing minced pork reduced water-holding of myofibrils and increased surface …

The myofibrillar protein (MP) degradation and in vitro digestive properties of porcine
longissimus during freezing at− 8,− 18,− 25 and− 40° C for 1, 3, 6, 9 and 12 months were …

Freezing is commonly used to extend the shelf life of meat and meat products but may
impact the overall quality of those products by inducing structural changes in myofibrillar …

This study was performed to examine the changes in myofibrils, proteins and peptides
during postmortem conditioning of vacuum-packed pork loins at 4° C for 30 days. The …

This study aimed to determine the effect of frozen-then-chilled storage on free Ca 2+,
proteolytic enzyme activity of calpains and the proteasome, water-holding capacity and …

Uniform design was adopted, and three factors, ie, freezing rates with two levels, thawing
rates with six levels and individual (six pork M. Longissimus dorsi from three pigs), were …

The effect of frozen time and the temperature on myofibril degradation and the structure of
myofibrillar proteins of porcine longissimus muscles were investigated. With extended frozen …

This study aimed to address the effects of frozen storage temperature and duration on the
changes in physicochemical properties of beef myofibrillar protein. The beef was stored at …