Tenderization and fragmentation of myofibrillar proteins in bovine longissimus dorsi muscle using proteolytic extract from Sarcodon aspratus

Shin, H.G.; Choi, Young Min; Kim, Ho Kyoung; Ryu, Youn-Chul; Lee, Sang Hoon; Kim, Byoung Chul

doi:10.1016/j.lwt.2007.08.019

Cited by 48 publications

(34 citation statements)

References 41 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The increase in MFI from day 0 to day 14 (Table ) may be due to the breaking of myofibrillar proteins into segments at, or near, the Z‐disk during post mortem storage (Shin et al . ). Hou et al .…”

Section: Resultsmentioning

confidence: 97%

Changes of microbial spoilage, lipid-protein oxidation and physicochemical properties during post mortem refrigerated storage of goat meat

et al. 2016

View full text Add to dashboard Cite

Examined was the effect of post mortem refrigerated storage on microbial spoilage, lipid-protein oxidation and physicochemical traits of goat meat. Seven Boer bucks were slaughtered, eviscerated and aged for 24 h. The Longissimus lumborum (LL) and Semitendinosus (ST) muscles were excised and subjected to 13 days post mortem refrigerated storage. The pH, lipid and protein oxidation, tenderness, color and drip loss were determined in LL while microbiological analysis was performed on ST. Bacterial counts generally increased with increasing aging time and the limit for fresh meat was reached at day 14 post mortem. Significant differences were observed in malondialdehyde (MDA) content at day 7 of storage. The thiol concentration significantly reduced as aging time increased. The band intensities of myosin heavy chain (MHC) and troponin-T significantly decreased as storage progressed, while actin remained relatively stable. After 14 days of aging, tenderness showed significant improvement while muscle pH and drip loss reduced with increase in storage time. Samples aged for 14 days had higher lightness (P < 0.05) and lower (P < 0.05) yellowness and redness. Post mortem refrigerated storage influenced oxidative and microbial stability and physico-chemical properties of goat meat.

show abstract

Section: Resultsmentioning

confidence: 97%

Changes of microbial spoilage, lipid-protein oxidation and physicochemical properties during post mortem refrigerated storage of goat meat

et al. 2016

View full text Add to dashboard Cite

show abstract

“…In postmortem muscle, activating μ ‐calpain and initiating the proteolytic degradation of Z‐disc related myofibrillar proteins lead to myofibril fragmentation and MFI, which is based on the myofibril fragmentation and is regarded as an index of meat tenderness . In the control group, MFI increased during 48 h of incubation.…”

Section: Resultsmentioning

confidence: 99%

Effect of inhibition of μ‐calpain on the myofibril structure and myofibrillar protein degradation in postmortem ovine muscle

Gao

et al. 2016

J Sci Food Agric

View full text Add to dashboard Cite

show abstract

“…Measurement of myofibril fragmentation has been widely used to determine post‐mortem proteolysis in meat,25–27 and myofibrillar fragmentation is a useful indicator of the extent of myofibrillar protein degradation 25. Marination of bovine longissimus dorsi with Sarcodon aspratus proteases was observed to increase myofibrillar fragmentation 28. Multi‐angle light scattering has been used to determine differences in particle size distributions between unaged and aged samples of pork 12.…”

Section: Discussionmentioning

confidence: 99%

Injection of marinade with actinidin increases tenderness of porcine M. biceps femoris and affects myofibrils and connective tissue

et al. 2009

View full text Add to dashboard Cite

BACKGROUND: Marination of beef muscles with brine solutions containing proteolytic enzymes from fruit extracts has been shown to tenderize meat. However, the effect of marination with actinidin on tenderness of pork muscles has not been investigated. Tenderness and eating quality of porcine M. biceps femoris was investigated by Warner-Bratzler (WB) shear test and sensory evaluation after injection of brine containing up to 11 g L −1 actinidin-containing kiwi fruit powder and 2, 5 or 9 days of storage.

show abstract

Tenderization and fragmentation of myofibrillar proteins in bovine longissimus dorsi muscle using proteolytic extract from Sarcodon aspratus

Cited by 48 publications

References 41 publications

Changes of microbial spoilage, lipid-protein oxidation and physicochemical properties during post mortem refrigerated storage of goat meat

Changes of microbial spoilage, lipid-protein oxidation and physicochemical properties during post mortem refrigerated storage of goat meat

Effect of inhibition of μ‐calpain on the myofibril structure and myofibrillar protein degradation in postmortem ovine muscle

Injection of marinade with actinidin increases tenderness of porcine M. biceps femoris and affects myofibrils and connective tissue

Contact Info

Product

Resources

About