Effects of aging and freezing/thawing sequence on quality attributes of bovine Mm. gluteus medius and biceps femoris

Abstract

ObjectiveThe effects of aging and freezing/thawing sequence on color, physicochemical, and enzymatic characteristics of two beef muscles (Mm. gluteus medius, GM and biceps femoris, BF) were evaluated.MethodsBeef muscles at 3 d postmortem were assigned to four different combinations of aging and freezing/thawing sequence as follows; aging at 2°C for 3 wk (A3, never-frozen control), freezing at −28°C for 2 wk then thawing (F2, frozen/thawed-only), aging at 2°C for 3 wk, freezing at −28°C for 2 wk then thawing (A3F2), and freezing at −28°C for 2 wk, thawing then further aging at 2°C for 3 wk (F2A3).ResultsNo significant interactions between different aging/freezing/thawing treatments and muscle type on all measurements were found. Postmortem aging, regardless of aging/freezing/thawing sequence, had no impact on color stability of frozen/thawed beef muscles (p<0.05). F2A3 resulted in higher purge loss than F2 and A3F2 treatments (p<0.05). A3F2 and F2A3 treatments resulted in lower shear force of beef muscles compared to F2 (p<0.05). Although there was no significant difference in glutathione peroxidase (GSH-Px) activity, F2A3 had the highest β-N-acetyl glucominidase (BNAG) activity in purge, but the lowest BNAG activity in muscle (p<0.05). GM muscle exhibited higher total color changes and purge loss, and lower GSH-Px activity than BF muscle.ConclusionThe results from this present study indicate that different combinations of aging/freezing/thawing sequence would result in considerable impacts on meat quality attributes, particularly thaw/purge loss and tenderness. Developing a novel freezing strategy combined with postmortem aging will be beneficial for the food/meat industry to maximize its positive impacts on tenderness, while minimizing thaw/purge loss of frozen/thawed meat.

Effects of Aging and Aging Method on Physicochemical and Sensory Traits of Different Beef Cuts

“…For each beef cut, both wet and dry aging processes led to reduction in shear force (p<0.05). Meat is tenderized by proteolytic enzymes, which degrade myofibrillar and cytoskeletal proteins that weaken the muscle structure and increase tenderness during wet and dry aging ( Kim et al, 2017 ; Oh et al, 2017 ).…”

“…The a* and b* values of the rump were not significantly affected by aging or the aging method. Color stability can be affected by muscle types, which have different oxygen consumption rates and metmyoglobin reductase activities ( Kim et al, 2017 ). In the present study, color change was dependent on aging method.…”

“…The aging process is used for the improvement in the eating quality of fresh meat such as tenderness, flavor, and/or juiciness ( Kim and Kim, 2017 ). The process is divided into two types, wet and dry aging ( Lee et al, 2017 ).…”

Changes in oxidation and secondary structure of myofibrilla protein, water distribution, and quality of vacuum packaged Tan mutton during storage at different temperatures

“…In addition, the results showed that the decrease of WHC among the three groups was significantly different in the same storage period. Different formation rate of ice crystal and level of protein oxidation caused by various temperature might explain these differences (Kim & Kim, 2017). Therefore, storage temperature, storage time, and their interaction had a significant effect on WHC (p < .05).…”

Physicochemical and microbial characteristics of longissimus lumborum and biceps femoris muscles in Korean native black goat with wet-aging time

“…Wet-aging improves the tenderness of meat as a part of the proteolytic degradation of the myofibrillar protein and increases the flavor of aged meat because of the changing sequence of peptides and amino acids [ 8 , 9 ]. It also increases the eating quality of meat at different storage times and processes [ 10 ]. On the other hand, the taste, flavor, texture, and other physicochemical characteristics of aged-meat varies according to the different meat cuts because of the different contents of collagen, free amino acids, fatty acids, and nucleotides [ 11 ].…”