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• W3022210526 abstract "Postmortem aging has beenextensively practiced as value-adding process due to the beneficial impacts onmeat palatability. Meat tenderization occurred through proteolyticfragmentation of myofibrillar structural proteins via endogenous proteasesystems, which is considered as the primary drive to enhance major palatabilityattributes including tenderness, juiciness, and flavor. Recent theoreticalframework proposes apoptosis, or programmed cell death, as the preceding stepthat initiates postmortem proteolysis. Whereas small heat shock proteins havebeen consistently recognized as meat quality biomarkers, probably due to theirprotective activities against proteolysis through anti-stress, anti-apoptotic,and chaperoning functionalities. To shed light on detailed mechanismscontrolling postmortem proteolysis and consequential impacts on the developmentof fresh meat quality characteristics, postmortem proteolytic changes of smallheat shock proteins, apoptotic factors, and myofibrillar structural proteinswere profiled in postmortem skeletal muscles under different metabolicbackgrounds and across species. In beef, three muscles, longissimuslumborum (LL), semimembranosus (SM), and psoas major (PM),have been selected to represent glycolytic, intermediate, and oxidative muscletypes. Tenderness and water - holding capacity were determined, andproteolysis, apoptotic features, and small heat shock proteins were measured in8 beef carcasses at 1, 2, 9, 16, and 23 days of aging. PM exhibited limitedaging potential in quality developments shown by lower extents of shear force,water-holding capacity, and proteolytic changes, including calpain 1 autolysis,troponin T, and HSP27 compared to LL and SM. Conversely, LL had an increase intenderization and water-holding capacity, which was accompanied with moreextended calpain 1 autolysis, proteolysis and HSP27 degradation, compared withother muscles. The results of this study suggest that postmortem proteolyticchanges of myofibrillar proteins, small HSPs and apoptotic factors occur in amuscle-specific manner, which is likely attributed to different rate and extentof meat quality developments of each muscle during aging. Callipyge lambs are a uniquegenetic background showing calpastatin over-expression, muscle hypertrophy inloin and hindquarter area, substantially compromised meat tenderizationpotential, and a shift of muscle fiber composition towards fast-glycolyticdirections. Proteome and metabolome changes in muscles from callipyge mutation(+/C) and non-callipyge phenotype (+/+, C/+, and C/C) lambs were profiled toprovide insight into the biochemical changes affecting meat quality attributes.M. longissimus thoracis from lambs with all four possible callipyge genotype (n= 4, C/+, C/C, +/C, and +/+) were collected after 3d aging and analyzed usingmass-spectrometry based platforms. Among identified proteomes, cytochrome c (pro-apoptoticprotein) was detected with significantly lower abundances in +/C.Anti-apoptotic HSP70, BAG3, and PARK7 were over-abundant in +/C, which couldresult in delayed apoptosis and possibly attributed to tougher meat incallipyge lambs. Eight glycolysis enzymes were overabundant in +/C lambs,whereas 3 enzymes involved in TCA cycle were overabundant in non-callipyge ones(C/C and/or C/+). Twenty-five metabolites were affected by genotypes (P <0.05), including metabolic co-factors, polyphenols, and AA/short peptides.Pig production is facing increasedpublic pressure regarding antibiotic usage restriction. Recently, dietaryL-glutamine at cost effective level (0.2%) was identified as an effective antibioticalternative in post-transport nursery pig diets. To evaluate carcass and meatquality characteristics in market-ready pigs when 0.2% dietary L-glutamine wasapplied as for early-life post-weaning and transport recovery, pigs (N=480)were weaned and transported in two replication trials in SPRING (April of 2017)vs. SUMMER (July of 2016), fed 3 different diets (Non: no antibiotic, Anti: 441ppm chlortetracycline and + 38.6 ppm tiamulin, Gln: 0.20% L-glutamine) for 14days after transport, and fed basal diet until reaching market weight. Pairs oflongissimus dorsi (LD) and psoas major (PM) muscles from eachcarcass (n=10/diet/trial) were separated at 1 d and 7 d postmortem,respectively. Carcass yield and meat physical and quality attributes wereevaluated. Overall impacts of Gln on physical attributes of carcasses andporcine muscles were minimal. No dietary effects were found in carcass,proximate composition, water-holding capacity, or shear force. Significantdifference between trials were found in terms of productivity and pork/carcassqualities, where SPRING replicates showed increased body weight, faster pHdecline, paler surface color, higher intra-muscular fat deposition, andimproved tenderness and water-holding capacity as indicated by lower shearforce values, thaw-purge loss, and cooking loss (P < 0.05).The pork and carcass qualityresults give rise to a postulation that different metabolism and animal growthmight have been occured between the two production trials, consequentiallydifferentiated meat quality development. In this regard, myofibrillarproteolysis, small heat shock proteins, and apoptotic factors were characterizedduring 7 d postmortem aging in porcine LD and PM muscles from both seasonaltrials, combined with metabolomics profiles of 1d samples using theGC-TOF-MS/MS platform. Compared to SUMMER counterparts, SPRING muscles showedconcurrence of more extended apoptosis, further calpain 1 autolysis, andincreased structural protein degradation (P<0.05). SPRING muscles showedmore ATP catabolism compounds and increase in carbohydrates, branched-chainamino acids, and 16-18 carbon fatty acids, which could be chemistryfingerprints of increased cellular oxidative stress, consequentially favoringonset of apoptosis and proteolysis. Meanwhile, SUMMER pigs showed increasedstress-defending metabolites, such as ascorbic acid, antioxidant amino acids,and decreased inhibitory neuro-transmitter GABA, which may indicate elevatedstress-defending activity in SUMMER pigs that possibly inhibited apoptosis andproteolysis." @default.
• W3022210526 created "2020-05-13" @default.
• W3022210526 creator A5073836103 @default.
• W3022210526 date "2020-04-28" @default.
• W3022210526 modified "2023-09-27" @default.
• W3022210526 title "Unlocking the role of small heat shock proteins and apoptosis in postmortem proteolysis and meat quality characteristics of skeletal muscles under different conditions" @default.
• W3022210526 doi "https://doi.org/10.25394/pgs.12196857.v1" @default.
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