scholarly journals Assessment of RNAlater® as a Potential Method to Preserve Bovine Muscle Proteins Compared with Dry Ice in a Proteomic Study

Foods ◽  
2019 ◽  
Vol 8 (2) ◽  
pp. 60 ◽  
Author(s):  
Yao Zhu ◽  
Anne Mullen ◽  
Dilip Rai ◽  
Alan Kelly ◽  
David Sheehan ◽  
...  
Keyword(s):  
Shear Force ◽  
Muscle Protein ◽  
Potential Method ◽  
Post Mortem ◽  
Muscle Proteins ◽  
Dry Ice ◽  
Bovine Muscle ◽  
Preservation Method ◽  
Liquid Chromatography Tandem Mass ◽  
Proteomic Study

RNAlater® is regarded as a potential preservation method for proteins, while its effect on bovine muscle proteins has rarely been evaluated. Bovine muscle protein samples (n = 12) collected from three tender (Warner–Bratzler shear force: 30.02–31.74 N) and three tough (Warner–Bratzler shear force: 54.12–66.25 N) Longissimus thoracis et lumborum (LTL) samples, preserved using two different sampling preservation methods (RNAlater® and dry ice), at two post mortem time points (day 0 and day 14), were characterized using one-dimensional electrophoresis. Fourteen bands with molecular weights ranging from 15 to 250 kDa were verified, both in the dry ice and RNAlater® storage groups, at each time point, using image analysis. A shift from high to low molecular weight fragments, between day 0 and day 14, indicated proteolysis of the muscle proteins during post mortem storage. Liquid chromatography-tandem mass spectrometry (LC-MS/MS) analyses and database searching resulted in the identification of 10 proteins in four bands. Protein profiles of muscle preserved in RNAlater® were similar to those of muscle frozen on dry ice storage, both at day 0 and day 14. The results demonstrate that RNAlater® could be a simple and efficient way to preserve bovine muscle proteins for bovine muscle proteomic studies.

In vitro study to evaluate the degradation of bovine muscle proteins post-mortem by proteasome and μ-calpain

Meat Science ◽  
2008 ◽  
Vol 79 (1) ◽  
pp. 77-85 ◽  
Author(s):  
Malene Bergh Houbak ◽  
Per Ertbjerg ◽  
Margrethe Therkildsen
Keyword(s):  
In Vitro Study ◽  
Vitro Study ◽  
Post Mortem ◽  
Muscle Proteins ◽  
Bovine Muscle

scholarly journals Influence of high pre-rigor temperature and fast pH fall on muscle proteins and meat quality: a review

2014 ◽  
Vol 54 (4) ◽  
pp. 375 ◽  
Author(s):  
Yuan H. Brad Kim ◽  
Robyn D. Warner ◽  
Katja Rosenvold
Keyword(s):  
Meat Quality ◽  
Protein Denaturation ◽  
Current Knowledge ◽  
Muscle Protein ◽  
Muscle Metabolism ◽  
Quality Attributes ◽  
Post Mortem ◽  
Muscle Proteins ◽  
Chilling Temperatures ◽  
Stress Susceptibility

The impacts of accelerated pH decline combined with high muscle temperature on post-mortem muscle metabolism and subsequent meat quality attributes have been extensively studied. Traditionally, this phenomenon has been observed in pork muscles, primarily due to the relatively fast post-mortem glycolysis rate and its relationships to stress susceptibility of pigs before slaughter. However, the protein-denaturing condition of high temperature/rapid pH fall and subsequent PSE (pale, soft and exudative)-like abnormal meat quality characteristics have been observed in muscles from other species such as beef, lamb, venison and even poultry. Various pre-rigor conditions including the application of electrical stimulation, hot-boning, and/or pre-rigor carcass chilling temperatures in various muscles, in conjunction with carcass stretching/hanging methods, can also contribute to muscle-protein denaturation pre-rigor. This review considers the influence of a faster than normal pH fall at a higher than normal pre-rigor temperature on glycolysis, post-mortem muscle proteins and subsequently meat quality attributes. Gaps in current knowledge are identified and recommendations made for additional research.

Bovine muscle proteins IV. Preparation of myosin and actomyosin

1963 ◽  
Vol 19 (9) ◽  
pp. 493-494 ◽  
Author(s):  
A. J. Fryar ◽  
R. J. Gibbs
Keyword(s):  
Muscle Proteins ◽  
Bovine Muscle

Effects of sugars on post-mortem glycolysis in bovine muscle mince

Meat Science ◽  
1988 ◽  
Vol 23 (3) ◽  
pp. 211-225 ◽  
Author(s):  
O.A. Young ◽  
S.M. Humphrey ◽  
D.J.C. Wild
Keyword(s):  
Post Mortem ◽  
Bovine Muscle

scholarly journals The effect of extended post-mortem ageing on the Warner–Brazler shear force of longissimus thoracis from beef heifers from two sire breeds, slaughtered at 20 or 25 mo of age

2020 ◽  
Author(s):  
A.P. Moloney ◽  
B. Picard ◽  
L. Moran
Keyword(s):  
Chemical Analysis ◽  
Consumer Satisfaction ◽  
Shear Force ◽  
Muscle Fibres ◽  
Type I ◽  
Post Mortem ◽  
Beef Heifers ◽  
Holstein Friesian ◽  
Main Effects ◽  
Sire Breed

The effects on tenderness of extended ageing of longissimus thoracis (LT, striploin) muscle that differed in structure and composition were examined. Spring-born Angus × Holstein-Friesian heifers (n = 48) and Belgian Blue × Holstein-Friesian heifers (n = 48) were slaughtered, within sire breed, at 20 or 25 mo of age. Approximately 48 h post-mortem, LT steaks (2.5 cm) were removed, and either stored at −20°C for chemical analysis or vacuum-packed, stored at 2°C for 7, 14 or 28 d post-mortem and then at −20°C pending Warner–Bratzler shear force (WBSF) analysis. Muscle from Angus-sired heifers had higher (P < 0.001) intramuscular fat (IMF) concentration, lower (P < 0.001) proportion of type IIX muscle fibres and higher (P < 0.001) proportion of type IIA and type I muscle fibres compared to muscle from Belgian Blue-sired heifers. Collagen characteristics did not differ between sire breeds. Later slaughter increased (P < 0.001) IMF concentration and decreased (P < 0.001) total and insoluble concentrations and collagen solubility. There were no interactions between the main effects for WBSF and no difference between sire breeds. Later slaughter and increasing the duration of ageing decreased (P < 0.05) WBSF. Based on threshold WBSF values in the literature, all samples would be considered tender (<39 N) after 7 d ageing. Untrained consumers are likely to detect the decrease in WBSF from 7 to 14 d ageing but not due to further ageing. Within the production system examined and based on WBSF data, extending LT ageing to 28 d is not necessary to ensure consumer satisfaction.

Changes in the Solubility of Bovine Muscle Proteins during Growth

1970 ◽  
Vol 30 (1) ◽  
pp. 10-14 ◽  
Author(s):  
B. A. Link ◽  
R. G. Cassens ◽  
R. G. Kauffman ◽  
R. W. Bray
Keyword(s):  
Muscle Proteins ◽  
Bovine Muscle

scholarly journals Human Muscle Protein Synthesis Rates after Intake of Hydrolyzed Porcine-Derived and Cows’ Milk Whey Proteins—A Randomized Controlled Trial

Nutrients ◽  
2019 ◽  
Vol 11 (5) ◽  
pp. 989 ◽  
Author(s):  
Bendtsen ◽  
Thorning ◽  
Reitelseder ◽  
Ritz ◽  
Hansen ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
G Protein ◽  
Whey Protein ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Synthesis Rate ◽  
Protein Synthesis Rate ◽  
Muscle Proteins ◽  
Mixed Meal ◽  
The Impact

Abstract: Background: Whey protein has been shown to be one of the best proteins to stimulate muscle protein synthesis rate (MPS), but other high quality proteins, e.g., animal/porcine-derived, could have similar effects. Objective: To investigate the effects of hydrolyzed porcine proteins from blood (HPB) and muscle (HPM), in comparison to hydrolyzed whey protein (HW), on MPS after intake of 15 g alone or 30 g protein as part of a mixed meal. We hypothesized that the postprandial MPS would be similar for porcine proteins and whey protein. Design: Eighteen men (mean ± SD age: 24 ± 1 year; BMI: 21.7 ± 0.4 kg/m2) participated in the randomized, double-blind, three-way cross-over study. Subjects consumed the three test products (HPB, HPM and HW) in a random order in two servings at each test day. Serving 1 consisted of a drink with 15 g protein and serving 2 of a drink with 30 g protein together with a mixed meal. A flood-primed continuous infusion of (ring-13C6) phenylalanine was performed and muscle biopsies, blood and urine samples were collected for determination of MPS, muscle free leucine, plasma amino acid concentrations and urea excretion. Results: There were no statistical differences between the MPS measured after consuming 15 g protein alone or 30 g with a mixed meal (p = 0.53) of HPB (0.048 ± 0.007 vs. 0.049 ± 0.008%/h, resp.), HPM (0.063 ± 0.011 vs. 0.062 ± 0.011 %/h, resp.) and HW (0.058 ± 0.007 vs. 0.071 ± 0.013%/h, resp.). However, the impact of protein type on MPS reached statistical tendency (HPB vs. HPM (p = 0.093) and HPB vs. HW (p = 0.067)) with no difference between HPM and HW (p = 0.88). Plasma leucine, branched-chain, essential and total amino acids were generally higher for HPB and HW than HPM (p < 0.01), which reflected their content in the proteins. Muscle-free leucine was higher for HPB than HW and HPM (p < 0.05). Conclusion: Hydrolyzed porcine proteins from blood and muscle resulted in an MPS similar to that of HW, although with a trend for porcine blood proteins to be inferior to muscle proteins and whey. Consequently, these porcine-derived muscle proteins can be used similarly to whey protein to support maintenance of skeletal muscle as part of supplements and ingredients in foods.

Sign in / Sign up

Export Citation Format

Share Document