Effects of chopping temperature on the gel quality of silver carp (Hypophthalmichthys molitrix) surimi: insight from gel-based proteomics.

BACKGROUND: Morden advanced analytical tools offer valuable information into the understanding of molecular mechanism of traditional food processing. Chopping temperature is well-known to affect the surimi gel quality of silver carp, but the detailed molecular mechanism is not very clear. In this study, a gel-based proteomics was performed on the extracted surimi proteins under different chopping temperatures (0, 5, 10, and 25 °C) along with other physicochemical characterization of surimi proteins and gels. RESULTS: With increased chopping temperature, protein extractability (in 3% sodium chloride) generally decreased, while the extracted protein generally exhibited larger surface hydrophobicity, reduced intrinsic fluorescence intensity, lower sulfhydryl content. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) profile of extracted protein showed a clear difference at 25 °C when compared with the other three temperatures, and more protein fragmentation occurred. Proteomic analysis of selected bands indicated that major myofibrillar proteins react differently with chopping temperatures, especially at 25 °C. The selected bands contained a variety of other proteins or their fragments, including adenosine triphosphate (ATP) synthase, glyceraldehyde-3-phosphate dehydrogenase, glucose-6-phosphate isomerase, heat shock protein, parvalbumin, collagen, and so forth. For the surimi gel, water-holding capacity and gel strength generally decreased with increased chopping temperature. CONCLUSION: Our results suggested that chopping at 0-10 °C is acceptable for the production of silver carp surimi in terms of gel strength and water-holding capacity. However, a chopping temperature near 0 °C led to less protein oxidation and denaturation. The inferior gel quality at 25 °C is linked to a decreased concentration of extracted protein and degradation of major myofibrillar protein, the latter is likely crosslinked with sarcoplasmic proteins. © 2024 Society of Chemical Industry.

Hydrolysis of Beef Sarcoplasmic Protein by Dry-Aged Beef-Isolated Penicillium oxalicum and Its Associated Metabolic Pathways.

Yanbian cattle have a unique meat flavor, and high-grade meat is in short supply. Therefore, in this study, we aimed to improve the added value of Yanbian cattle low-fat meat and provide a theoretical reference for the subsequent development of an excellent starter. Rump meat from Yanbian cattle was dry-aged and then screened for protease-producing fungi. Three protease-producing fungi (Yarrowia hollandica (D4 and D11), Penicillium oxalicum (D5), and Meesziomyces ophidis (D20)) were isolated from 40 d dry-aged beef samples, and their ability to hydrolyze proteins was determined using bovine sarcoplasmic protein extract. SDS-PAGE showed that the ability of Penicillium oxalicum (D5) to degrade proteins was stronger than the other two fungi. In addition, the volatile component content of sarcoplasmic proteins in the D5 group was the highest (45.47%) and comprised the most species (26 types). Metabolic pathway analysis of the fermentation broth showed that phenylalanine, tyrosine, and tryptophan biosynthesis was the most closely related metabolic pathway in sarcoplasmic protein fermentation by Penicillium oxalicum (D5). Dry-aged beef-isolated Penicillium oxalicum serves as a potential starter culture for the fermentation of meat products.

Effect of Sarcoplasmic Protein Solutions Dried at Different Times and Rates on Water Migration in Lamb Myofibril In Vitro.

To determine whether sarcoplasmic proteins affected water migration in myofibrils during air-drying, with protein denaturation as an indicator of sarcoplasmic protein changes, the extent of sarcoplasmic protein changes in lamb during air-drying was first studied. The results showed that sarcoplasmic protein's thermal stability decreased and secondary structure changed, indicating sarcoplasmic protein denatured in lamb during air-drying (35 °C, 60% RH, 3 m/s wind speed). Subsequently, the effect of sarcoplasmic protein solutions, dried at different times and rates, on myofibril protein-water interaction was studied in vitro. Two sets of sarcoplasmic protein solutions were dried for 0, 3, 6, and 9 h in a drying oven, resulting in different degrees of change. These two sets with higher or lower drying rates were achieved by controlling the contact area between sarcoplasmic protein solution and air. These dried sarcoplasmic protein solutions were then mixed with extracted myofibril and incubated for 2 h. The results showed a significant increase in T21 relaxation time of the incubation system when sarcoplasmic protein solution was dried at 35 °C for 3 h. This indicated that myofibrillar protein-water interaction was weakened, facilitating water migration from the inside to the outside of myofibrils. The denaturation degree of sarcoplasmic proteins was slowed by a higher drying rate, thereby alleviating the increase in the amount of immobile water within myofibrils when dried for 6 h. In conclusion, the properties of sarcoplasmic proteins were influenced by both drying rate and time, thereby influencing the water migration within myofibrils during air-drying.

Evaluation of sono-physico-chemical and processing effects in the mixed sarcoplasmic protein/soy protein isolate system.

Since it may be employed to guide the production of high-quality plant protein as a partial substitute for animal protein using sono-physico-chemical effects, it is important to investigate the mixing of animal and plant protein in ultrasound (UID)-assisted processing systems. A study group of sono-physico-chemical processing with five distinct soy protein isolate (SPI)/ sarcoplasmic protein (SPN) ratios was developed in this work. The results showed that adding additional SPN to the mixed protein can increase its sono-physico-chemical impact, and this effect is greatest when the ratio of SPI to SPN is 1:3. The high SPN group's grafting rate rose from 39.13% to 55.26% in comparison to the high SPI content group. Quercetin (Que) may more readily modify SPN than SPI in the "dual protein" system used in this work, highlighting the critical function of plant protein in controlling the effects of UID-assisted processing in the "dual protein" system. Changes in apparent viscosity and microstructure are the primary parameters that affect the severity of sono-physico-chemical effects in SPI/SPN mixed protein systems, in addition to structural variables.

Binding of Selected Aroma Compounds to Myofibrillar Protein, Sarcoplasmic Protein, and Collagen during Thermal Treatment: Role of Conformational Changes and Degradation of Proteins.

To investigate the effects of conformational changes and thermal degradation of myofibrillar protein (MP), sarcoplasmic protein (SP), and collagen (CO) on the binding ability for aroma compounds during heating. Using SDS-PAGE, HPLC, and LC-MS/MS, a consistent rise in the total concentration of peptides and free amino acids formed by the thermal degradation of proteins was observed. The surface hydrophobicity, total sulfhydryl content, particle size, and secondary structure content of proteins changed significantly over time. Furthermore, the aroma binding ability of proteins was determined by gas chromatography-mass spectrometry. The results revealed an increase in binding ability during 5 or 10 min of heating due to protein unfolding and the accumulation of degradation products. However, the binding ability decreased due to protein aggregation with prolonged heating. Notably, all proteins exhibited strong affinity toward (E)-2-octenal, (E,E)-2,4-decadienal, 2-methyl-3-furanthiol, and dimethyl trisulfide. The binding ability of MP and SP was similar but differed significantly from that of CO, which had lower binding ability for hexanal, (E)-2-octenal, (E,E)-2,4-decadienal, and dimethyl trisulfide compared to MP and SP.

Evaluation of protein degradation and flavor compounds during the processing of Xuan'en ham.

Protein degradation occurs during the processing of dry-cured ham, which has important influences on the flavor and quality of products. The aim of this work was to study the degradation kinetics of myofibrillar proteins (MPs) and sarcoplasmic proteins (SPs) extracted from the biceps femoris muscle during the processing of Xuan'en ham. A relationship between protein degradation and the flavor formation was found. During the processing of Xuan'en ham, MPs and SPs were mainly degraded in the salting stage and incipient fermentation. Accompanied by protein degradation, the content of carbonyl group in SPs increased gradually, but in MPs, it first increased and then decreased. Interconversion between sulfhydryl and disulfide bonds was investigated during this processing. Oxidation, degradation, and thermal effects significantly affected the surface hydrophobicity of proteins. More than one hundred volatile compounds have been identified at each stage of ham preparation. Among them, organic acids were the predominant group, followed by hydrocarbons, aldehydes, alcohols, ketones, and esters.

Capture and identification of bacteria from fish muscle based on immunomagnetic beads and MALDI-TOF MS.

In the present study, E. coli was taken as a model bacterium, anti-E. coli functionalized magnetic beads were constructed and used to capture E. coli from aqueous extracts of fish sarcoplasmic protein (FSP) and fish muscle protein of sablefish. The excellency of the reproducibility of the present protocol was demonstrated by capturing E. coli from sablefish FSP extracts. The presence of 10 CFU/mL E. coli is still detectable. A microbial safety test on the surface of fish muscle was successfully performed. The bacterial identification accuracy from samples with different matrices was found to be excellent with RSD = 3%. High specific detection of target bacteria in complex biological samples was testified by spiking Staphylococcus aureus and Klebsiella pneumoniae in samples as interference. Ten biomarker ions were discovered for E. coli's recognition. It is promising to apply the present protocol in bacterial analysis in muscle food samples to ensure their safety.

Release mechanism between sarcoplasmic protein-bound and free heterocyclic amines and the effects of dietary additives using an in-vitro digestion model.

In this study, the release mechanism between free and sarcoplasmic protein-bound heterocyclic amines (HAs) in an in-vitro digestion model were investigated by comparing changes in the amount of HAs between groups with different enzyme dosages and at different digestion stages. The effects of the addition of onions, peppers, and apples on the release mechanism were also studied. We found that bound HAs cannot be completely converted to free HAs under normal enzyme dosages and that a significant increase in HAs occurred in the intestines. The release rate of bound HAs was 5.99%-43.84%, and the total release rate of HAs was 36.67%. Furthermore, the release rate of ß-carbolines was the highest (34.41%-43.84%). The addition of onions, peppers, and apples significantly increased the number of free HAs, with growth rates reaching 56.06%, 43.43%, and 54.44%, respectively. These additives mainly promoted the generation of free harman and norharman.

Investigation of the effect of pork compositions on freezing points in different pork cuts by measuring thermal properties and water mobility and distribution.

This work was to compare the difference of freezing point in the four pork cuts (chuck roll, picnic shoulder, loin, and topside) and evaluate the effect of pork compositions on the freezing points. Loin exhibited lower freezing points and accompanied by higher content of unfreezable water, lower relaxation times, and higher proportions of bound water, compared with other pork cuts. Low freezing points of pork may be attributed to high sarcoplasmic protein solubility, due to high sarcoplasmic protein solubility related to increase of bound water proportion and decrease of NMR T2 relaxometry. In addition, correlation analysis revealed that sarcoplasmic protein solubility and ash content were negatively related to the freezing point, which was verified by a quadratic polynomial correlation between the sarcoplasmic protein solubility and the freezing point in vitro. These results could help to better understand the freezing point of pork and provide more theories for improving superchilled storage.

Regulation of protein oxidation in Cantonese sausages by rutin, quercetin and caffeic acid.

The effects of rutin, quercetin, and caffeic acid on protein oxidation in Cantonese sausage during 60 days of storage at room temperature (25 ± 1 °C) were investigated. The results showed that the three phenolic compounds played different roles in inhibiting the oxidation of sarcoplasmic and myofibrillar protein. All of them inhibited sarcoplasmic protein oxidation by retarding carbonylation, the conversion of SH to S-S groups, and the formation of dimeric tyrosine and Schiff bases, of which rutin is the most effective. For myofibrillar protein, all of them suppressed the conversion of SH to S-S groups, only caffeic acid inhibited the accumulation of Schiff bases instead of carbonyls while both quercetin and caffeic acid inhibited the formation of dimeric tyrosine. In addition, quercetin had an inverse dosage effect on the oxidation regulation of MP, 0.16 g/kg quercetin had better inhibit effect on protein oxidation than 0.32 g/kg quercetin.

Quantitative changes in peptides derived from proteins in beef tenderloin (psoas major muscle) and striploin (longissimus lumborum muscle) during cold storage.

Peptides derived from whole proteins in beef tenderloin (M. psoas major, PM) and striploin (M. longissimus lumborum, LL) associated with meat quality and muscle fiber composition were identified and quantified during 21 days of aging. Peptide quantification revealed 40-43 proteins to be significantly degraded during all aging time, and these were mostly sarcoplasmic proteins. Cooking loss of both muscles was not changed by aging (P > 0.05), whereas Warner-Bratzler shear force and meat color were affected by aging. Sensory tenderness increased in PM after 14 days of aging (P < 0.05). PM had a higher type I fiber content, whereas LL had a higher type IIX fiber content (P < 0.05), resulting in differences in proteolysis during all aging periods tested. These findings improve our understanding of different biochemical and physicochemical changes in aged meat according to the muscle type.

Effects of Farm Management Practices and Transport Time on Post-Mortem Changes of Longissimus lumborum Muscle Proteins in Suckling Goat Kids.

The combined effect of farm management practices, transport time, and ageing time on the electrophoretic changes of sarcoplasmic (SPP) and myofibrillar (MFP) protein fractions of goat kids was studied. A total of 64 suckling goat kids were withdrawn from two farms with "high" (GW) and "low" (DW) welfare-friendly management practices, and they were transported for 2 or 6 h immediately before slaughtering. Longissimus lumborum samples were obtained at 3, 8, and 21 days post-mortem, and muscle proteins were separated by sodium dodecyl sulfate polyacrylamide gel electrophoresis SDS-PAGE. Both protein extracts displayed significant changes attributable to meat maturation. Managing conditions of kids in DW farms increased the post-mortem susceptibility of muscle proteins. Some MFP of Longissimus lumborum muscle, such as troponin T, as well as 26-30 and 35-37 kDa fractions were influenced significantly by deficient on-farm management, and therefore, these protein fragments might be considered as indicators of low-welfare on-farm management in goat kids.

Impact of methylglyoxal modification of chicken sarcoplasmic protein emulsions on emulsifying properties, rheological behavior and advanced glycation end products.

BACKGROUND: Protein modification is used to improve emulsion properties. However, there are limited reports on the effect of methylglyoxal (MGO) modification on emulsifying properties and on the production of advanced glycation end-products (AGEs) in chicken sarcoplasmic protein emulsion (SPE). In this study, MGO solution was dispersed into prepared emulsion (17 mg mL-1 sarcoplasmic-soybean oil (v/v 5:1)) at 0, 0.5, 5, 10, 30 and 50 mmol L-1 concentrations. Emulsifying activity index (EAI), emulsifying stability index (ESI), Z-average diameter, polydispersity index (PDI), zeta potential, rheological behavior (thermal condensation characteristics and fluidity) and AGEs in different concentrations of MGO SPE were measured. In addition, the effect of MGO on the levels of AGEs, lipid and protein oxidation of the emulsion as well as their relationship has also been analyzed. RESULTS: Our findings showed that ESI had the lowest value when MGO was added at a concentration of 10 mmol L-1 , while Z-average, PDI, carbonyl and AGEs had the highest value at the same concentration. Also, 10 mmol L-1 MGO played an important role in affecting the rheology of the emulsion. Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) results showed that the presence of myofibrillar proteins (MPs) in SPE was the main reason for the crosslinking of polymers which could be damaged by high concentration of MGO (>10 mmol L-1 ). CONCLUSION: Different concentration of MGO showed varying effects on emulsion properties and on the formation of AGEs in chicken SPE. Pearson's correlation analysis concluded that protein oxidation played a significant positive role during MGO modification. © 2020 Society of Chemical Industry.

Effect of malondialdehyde on oil-in-water emulsifying behavior and Maillard reaction of chicken sarcoplasmic protein in emulsion.

The purpose of this study was to investigate the effect of malondialdehyde (MDA) on emulsifying properties, rheological behavior and advanced glycation end products (AGEs) in chicken sarcoplasmic protein emulsion (CSPE). The CSPE preparation (17 mg/mL sarcoplasmic: soybean oil (v : v = 5:1) was dispersed into MDA emulsions at 0 mM, 0.5 mM, 5 mM, 10 mM, 30 mM, and 50 mM concentrations. Our hypothesis and main conclusions were summarized at three points: (1) Levels of AGEs increased when MDA concentrations were at 0.5-10 mM for the dispersive system and were aggregated by the disulfide bond. (2) Levels of AGEs decreased at 10-30 mM MDA concentrations, which could be attributed to protein structure changes. (3) Covalent bonding of non-disulfide bond played an important role at 30-50 mM MDA concentration. In sum, it was concluded that MDA not only changed the emulsifying properties but also induced AGEs formation in CSPE.

The coordination of dietary valine and isoleucine on water holding capacity, pH value and protein solubility of fresh meat in finishing pigs.

To investigate coordination of dietary levels of valine (Val) and isoleucine (Ile) on carcass traits and meat quality in pigs, 72 of 73.8 ± 1.6 kg crossbred barrows were randomly divided into a 2 (0.31% vs. 0.65% standard ileum digestible (SID) Val) × 2 (0.25% vs. 0.53% SID Ile) factorial arrangement. As a result, high dietary valine decreased myosin heavy-chain (MyHC)-I mRNA expression, pH24 h value, bound water amount (T21 peak area ratio), sarcoplasmic protein solubility and water holding capacity (WHC) of meat (P < .05). Meanwhile, high dietary isoleucine increased pH24 h value, sarcomere length (P < .05) and tend to decrease drip loss (P = .07). The significant interactions between valine and isoleucine were observed on backfat thickness, water distribution forms and myofibrillar protein solubility (P < .05) of pork. High valine diets undermined WHC of meat probably through decreasing pH24 h value and sarcoplasmic protein solubility considering their significant correlations with drip loss.

Skeletal Muscle Myofibrillar Protein Abundance Is Higher in Resistance-Trained Men, and Aging in the Absence of Training May Have an Opposite Effect.

Resistance training generally increases skeletal muscle hypertrophy, whereas aging is associated with a loss in muscle mass. Interestingly, select studies suggest that aging, as well as resistance training, may lead to a reduction in the abundance of skeletal muscle myofibrillar (or contractile) protein (per mg tissue). Proteomic interrogations have also demonstrated that aging, as well as weeks to months of resistance training, lead to appreciable alterations in the muscle proteome. Given this evidence, the purpose of this small pilot study was to examine total myofibrillar as well as total sarcoplasmic protein concentrations (per mg wet muscle) from the vastus lateralis muscle of males who were younger and resistance-trained (denoted as YT, n = 6, 25 ± 4 years old, 10 ± 3 self-reported years of training), younger and untrained (denoted as YU, n = 6, 21 ± 1 years old), and older and untrained (denoted as OU, n = 6, 62 ± 8 years old). The relative abundances of actin and myosin heavy chain (per mg tissue) were also examined using SDS-PAGE and Coomassie staining, and shotgun proteomics was used to interrogate the abundances of individual sarcoplasmic and myofibrillar proteins between cohorts. Whole-body fat-free mass (YT > YU = OU), VL thickness (YT > YU = OU), and leg extensor peak torque (YT > YU = OU) differed between groups (p < 0.05). Total myofibrillar protein concentrations were greater in YT versus OU (p = 0.005), but were not different between YT versus YU (p = 0.325). The abundances of actin and myosin heavy chain were greater in YT versus YU (p < 0.05) and OU (p < 0.001). Total sarcoplasmic protein concentrations were not different between groups. While proteomics indicated that marginal differences existed for individual myofibrillar and sarcoplasmic proteins between YT versus other groups, age-related differences were more prominent for myofibrillar proteins (YT = YU > OU, p < 0.05: 7 proteins; OU > YT = YU, p < 0.05: 11 proteins) and sarcoplasmic proteins (YT = YU > OU, p < 0.05: 8 proteins; OU > YT&YU, p < 0.05: 29 proteins). In summary, our data suggest that modest (~9%) myofibrillar protein packing (on a per mg muscle basis) was evident in the YT group. This study also provides further evidence to suggest that notable skeletal muscle proteome differences exist between younger and older humans. However, given that our n-sizes are low, these results only provide a preliminary phenotyping of the reported protein and proteomic variables.

Controlled Release of Metformin Hydrochloride from Core-Shell Nanofibers with Fish Sarcoplasmic Protein.

Background and Objectives: A coaxial electrospinning technique was used to produce core/shell nanofibers of a polylactic acid (PLA) as a shell and a polyvinyl alcohol (PVA) containing metformin hydrochloride (MH) as a core. Materials and Methods: Fish sarcoplasmic protein (FSP) was extracted from fresh bonito and incorporated into nanofiber at various concentrations to investigate the influence on properties of the coaxial nanofibers. The morphology, chemical structure and thermal properties of the nanofibers were studied. Results: The results show that uniform and bead-free structured nanofibers with diameters ranging from 621 nm to 681 nm were obtained. A differential scanning calorimetry (DSC) analysis shows that FSP had a reducing effect on the crystallinity of the nanofibers. Furthermore, the drug release profile of electrospun fibers was analyzed using the spectrophotometric method. Conclusions: The nanofibers showed prolonged and sustained release and the first order kinetic seems to be more suitable to describe the release. MTT assay suggests that the produced drug and protein loaded coaxial nanofibers are non-toxic and enhance cell attachment. Thus, these results demonstrate that the produced nanofibers had the potential to be used for diabetic wound healing applications.

A Critical Evaluation of the Biological Construct Skeletal Muscle Hypertrophy: Size Matters but So Does the Measurement.

Skeletal muscle is highly adaptable and has consistently been shown to morphologically respond to exercise training. Skeletal muscle growth during periods of resistance training has traditionally been referred to as skeletal muscle hypertrophy, and this manifests as increases in muscle mass, muscle thickness, muscle area, muscle volume, and muscle fiber cross-sectional area (fCSA). Delicate electron microscopy and biochemical techniques have also been used to demonstrate that resistance exercise promotes ultrastructural adaptations within muscle fibers. Decades of research in this area of exercise physiology have promulgated a widespread hypothetical model of training-induced skeletal muscle hypertrophy; specifically, fCSA increases are accompanied by proportional increases in myofibrillar protein, leading to an expansion in the number of sarcomeres in parallel and/or an increase in myofibril number. However, there is ample evidence to suggest that myofibrillar protein concentration may be diluted through sarcoplasmic expansion as fCSA increases occur. Furthermore, and perhaps more problematic, are numerous investigations reporting that pre-to-post training change scores in macroscopic, microscopic, and molecular variables supporting this model are often poorly associated with one another. The current review first provides a brief description of skeletal muscle composition and structure. We then provide a historical overview of muscle hypertrophy assessment. Next, current-day methods commonly used to assess skeletal muscle hypertrophy at the biochemical, ultramicroscopic, microscopic, macroscopic, and whole-body levels in response to training are examined. Data from our laboratory, and others, demonstrating correlations (or the lack thereof) between these variables are also presented, and reasons for comparative discrepancies are discussed with particular attention directed to studies reporting ultrastructural and muscle protein concentration alterations. Finally, we critically evaluate the biological construct of skeletal muscle hypertrophy, propose potential operational definitions, and provide suggestions for consideration in hopes of guiding future research in this area.

Isoelectric solubilization/precipitation processing modified sarcoplasmic protein from pale, soft, exudative-like chicken meat.

The sarcoplasmic protein from pale, soft and exudative -like chicken breast meat was modified using an isoelectric solubilization/precipitation process. After the modification, the sarcoplasmic protein obtained a larger particle distribution than the nontreated sample, indicating a severe aggregation. The isoelectric solubilization/precipitation-treated sarcoplasmic protein aggregates exhibited a flocculated and amorphous shape stabilized by the hydrophobic interactions. The hydrophobic interactions of alkali-treated sarcoplasmic proteins were relatively constant during heating, while they dramatically increased in nontreated sample. The alkali-treated sarcoplasmic protein could promote myofibrillar protein gelation properties, as proved by the higher breaking force and lower cooking loss. According to our results, it is hypothesized that the alkali-treated sarcoplasmic protein likely does not interfere in the gelation behavior of myofibrillar protein but does fill in the pores of the three-dimensional network, thereby strengthening its gelation elasticity. Overall, the alkali-treated sarcoplasmic protein exhibits the potential to improve the myofibrillar protein gelation properties.

Differences in light scattering between pale and dark beef longissimus thoracis muscles are primarily caused by differences in the myofilament lattice, myofibril and muscle fibre transverse spacings.

Beef colour is essential to consumer acceptability with dark muscle colours being problematic. Dark meat has less light scattering but the mechanisms are unknown. We hypothesise that three mechanisms are responsible for decreased light scattering in dark meat, namely (i) larger lateral separation of myofilaments, (ii) decreased optical protein density in the I-band and (iii) decreased denaturation of sarcoplasmic proteins. Nineteen beef longissimus thoracis muscles, divided into 'light', 'medium' and 'dark' colour groups, were assessed for light scattering by reflectance confocal microscopy, sarcomere length, and myofilament lattice spacing by small-angle X-ray diffraction. Dark muscles had a longer lattice spacing, shorter sarcomeres and wider muscle fibre diameters compared to lighter colour groups, indicating that the transverse spacing of muscle fibres that occurs post-mortem, with pH decline, is central to light scattering development. Dark muscles also had more degradation of the Z-disc and higher sarcoplasmic protein activities, which could impact on the optical density and contribute to lower light scattering.