scholarly journals Endpoint Temperature Influences Sarcoplasmic Proteome Profile of Cooked Beef Longissimus Lumborum

2019 ◽  
Vol 3 (2) ◽  
Author(s):  
A. P. A. A. Salim ◽  
S. P. Suman ◽  
S. Li ◽  
Y. Wang ◽  
J. Chen ◽  
...  
Keyword(s):  
Color Stability ◽  
Fructose Bisphosphate ◽  
Cooking Temperature ◽  
Longissimus Lumborum ◽  
Fructose Bisphosphate Aldolase ◽  
C 71 ◽  
Proteome Profile ◽  
Aldolase B ◽  
Differentially Abundant Proteins ◽  
Cooked Color

ObjectivesCooking ensures safety and enhances the palatability attributes of meat. Denaturation of myoglobin results in the dull-brown color of cooked meats. The denaturation of sarcoplasmic proteins is influenced by the degree of heat treatment, and their solubility is decreased with an increase in the endpoint cooking temperature. While previous studies examined the relationship between myoglobin denaturation, cooked color, and internal temperature in beef, investigations are yet to be undertaken to characterize the association between endpoint temperature, sarcoplasmic proteome, and color attributes in cooked steaks. Therefore, the objective of the present study was to examine the influence of endpoint cooking temperature (60 and 71°C) on sarcoplasmic proteome and internal color of beef longissimus lumborum (LL) steaks.Materials and MethodsEight (n = 8) beef LL muscles (14 d postmortem; USDA Choice) were obtained from a commercial packing plant. Two 2.5-cm thick steaks were fabricated from the center of the muscles and were cooked to internal endpoint temperature of 60°C (C-60) or 71°C (C-71) in a clam-shell grill. Cooked steaks were immediately cooled in slushed ice, sliced parallel to the grilled surface, and internal redness (a* value) and color stability (R630/580) were evaluated instrumentally. Sarcoplasmic proteome from the interiors of the cooked steaks was analyzed using 2-dimensional electrophoresis, and the gel images were digitally analyzed. The protein spots exhibiting more than 2.5-fold intensity differences (P < 0.05) between C-60 and C-71 were subjected to in-gel tryptic digestion and were identified by tandem mass spectrometry.ResultsThe C-60 steaks demonstrated greater (P < 0.05) a* and R630/580 than their C-71 counterparts. Seven differentially abundant proteins were identified and were over-abundant (P < 0.05) in C-60 compared to C-71. The differentially abundant proteins belong to 6 functional groups, i.e., transport proteins (serum albumin and hemoglobin), energy metabolism (adenylate kinase isoenzyme 1), chaperones (heat shock protein β-1), antioxidant (thioredoxin-dependent peroxide reductase), glycolytic enzymes (fructose-bisphosphate aldolase B), and protease (cytosol aminopeptidase).ConclusionThe findings indicated that the endpoint cooking temperature influences the internal cooked color and the sarcoplasmic proteome profile of beef LL steaks. The overabundant proteins in steaks cooked to 60°C may be utilized as potential biomarkers for undercooked beef, which is a source for foodborne infections.

scholarly journals Proteomic Changes in Sarcoplasmic and Myofibrillar Proteins Associated with Color Stability of Ovine Muscle during Post-Mortem Storage

Foods ◽  
2021 ◽  
Vol 10 (12) ◽  
pp. 2989
Author(s):  
Xiaoguang Gao ◽  
Dandan Zhao ◽  
Lin Wang ◽  
Yue Cui ◽  
Shijie Wang ◽  
...  
Keyword(s):  
Energy Metabolism ◽  
Molecular Mechanisms ◽  
Proteome Analysis ◽  
Color Stability ◽  
Post Mortem ◽  
Theoretical Understanding ◽  
Metabolism Enzymes ◽  
Longissimus Lumborum ◽  
Different Color ◽  
Differentially Abundant Proteins

The objective of this study was to investigate the proteomic characteristics for the sarcoplasmic and myofibrillar proteomes of M. longissimus lumborum (LL) and M. psoasmajor (PM) from Small-tailed Han Sheep. During post-mortem storage periods (1, 3, and 5 days), proteome analysis was applied to elucidate sarcoplasmic and myofibrillar protein changes in skeletal muscles with different color stability. Proteomic results revealed that the identified differentially abundant proteins were glycolytic enzymes, energy metabolism enzymes, chaperone proteins, and structural proteins. Through Pearson’s correlation analysis, a few of those identified proteins (Pyruvate kinase, Adenylate kinase isoenzyme 1, Creatine kinase M-type, and Carbonic anhydrase 3) were closely correlated to representative meat color parameters. Besides, bioinformatics analysis of differentially abundant proteins revealed that the proteins mainly participated in glycolysis and energy metabolism pathways. Some of these proteins may have the potential probability to be predictors of meat discoloration during post-mortem storage. Within the insight of proteomics, these results accumulated some basic theoretical understanding of the molecular mechanisms of meat discoloration.

scholarly journals Tandem Mass Tag Labeling to Identify Proteome Changes in Beef Longissimus Lumborum and Psoas Major Muscles During Early Postmortem Period

2019 ◽  
Vol 3 (2) ◽  
Author(s):  
C. Zhai ◽  
B. A. Djimsa ◽  
J. E. Prenni ◽  
R. J. Delmore ◽  
D. R. Woerner ◽  
...  
Keyword(s):  
Meat Quality ◽  
Color Stability ◽  
Quality Attributes ◽  
Tandem Mass ◽  
Tandem Mass Tag ◽  
Proteome Profile ◽  
Apoptotic Proteins ◽  
Psoas Major ◽  
Differentially Abundant Proteins ◽  
Early Postmortem

ObjectivesLongissimus lumborum (LL) and psoas major (PM) are important muscles in beef hindquarters that exhibit variation in meat quality attributes. Postmortem metabolism (muscle-to-meat conversion) affects biochemical properties of muscles and in turn influence the meat quality. Although previous research has indicated that variation in the proteome profile of LL and PM post-rigor influences meat quality attributes such as tenderness and color stability during retail display, limited research has examined the influence of early postmortem metabolism on meat quality. Tandem mass tag (TMT) labeling is a chemical labeling approach used for accurate mass spectrometry-based quantification and identification of biological macromolecules. Therefore, the objective of this study was to use TMT labeling to examine proteome profile variation between beef LL and PM during the early postmortem period.Materials and MethodsMuscle biopsy samples were collected from carcasses (n = 4) at 45 min, 12 h, and 36 h postmortem from a commercial beef processing facility. Samples were frozen immediately in liquid nitrogen and stored at –80°C until proteomic analysis. Proteome was analyzed using TMT label containing ten different isobaric compounds with the same mass and chemical structure composed of an amine-reactive NHS-ester group, a spacer arm, and a mass reporter. After labeling and peptide fractionation, all the samples were multiplexed and ran through the Orbitrap Velos mass spectrometer equipped with a Nanospray Flex ion source to identify differentially abundant proteins. The proteins exhibiting 1.5-fold or more intensity difference and a statistical difference (P < 0.05) between LL and PM or within the muscles during the postmortem were reported as differentially abundant.ResultsSeventy differentially abundant proteins (P < 0.05) were identified from three comparisons between the muscles (31 proteins in PM 45 min vs. LL 45 min, 41 proteins in PM 12 h vs. LL 12 h, 49 proteins in PM 36 h vs. LL 36 h). However, no difference (P > 0.05) in protein expression within a muscle was observed during these time points. The differentially abundant proteins were mainly involved in oxidative phosphorylation and ATP-related transport, tricarboxylic acid cycle, NADPH regeneration, fatty acid degradation, muscle contraction, calcium signaling, chaperone activity, oxygen transport, as well as degradation of the extracellular matrix. At early postmortem, overabundant anti-apoptotic proteins in LL could cause high metabolic stability, enhanced autophagy, and delayed apoptosis, while overabundant metabolic enzymes and pro-apoptotic proteins in PM could accelerate the reactive oxygen species generation and programmed cell death.ConclusionDifferentially abundant proteins between LL and PM during the early postmortem were primarily associated with cellular metabolism and programmed cell death. The greater oxidative and color stability in LL compared to PM could be related to the increased expression of anti-apoptotic proteins and the decreased expression of metabolic enzymes and proapoptotic proteins in LL.

scholarly journals Epitope-Based Peptide Vaccine Against Fructose-Bisphosphate Aldolase of Madurella mycetomatis Using Immunoinformatics Approaches

2018 ◽  
Vol 12 ◽  
pp. 117793221880970 ◽  
Author(s):  
Arwa A Mohammed ◽  
Ayman MH ALnaby ◽  
Solima M Sabeel ◽  
Fagr M AbdElmarouf ◽  
Amina I Dirar ◽  
...  
Keyword(s):  
B Cell ◽  
Binding Affinity ◽  
Mhc Class Ii ◽  
Bacterial Infections ◽  
Peptide Vaccine ◽  
Fructose Bisphosphate ◽  
Mhc I ◽  
Strong Binding ◽  
Fructose Bisphosphate Aldolase ◽  
Madurella Mycetomatis

Background: Mycetoma is a distinct body tissue destructive and neglected tropical disease. It is endemic in many tropical and subtropical countries. Mycetoma is caused by bacterial infections ( actinomycetoma) such as Streptomyces somaliensis and Nocardiae or true fungi ( eumycetoma) such as Madurella mycetomatis. To date, treatments fail to cure the infection and the available marketed drugs are expensive and toxic upon prolonged usage. Moreover, no vaccine was prepared yet against mycetoma. Aim: The aim of this study is to predict effective epitope-based vaccine against fructose-bisphosphate aldolase enzymes of M. mycetomatis using immunoinformatics approaches. Methods and materials: Fructose-bisphosphate aldolase of M. mycetomatis sequence was retrieved from NCBI. Different prediction tools were used to analyze the nominee’s epitopes in Immune Epitope Database for B-cell, T-cell MHC class II and class I. Then the proposed peptides were docked using Autodock 4.0 software program. Results and conclusions: The proposed and promising peptides KYLQ show a potent binding affinity to B-cell, FEYARKHAF with a very strong binding affinity to MHC I alleles and FFKEHGVPL that shows a very strong binding affinity to MHC II and MHC I alleles. This indicates a strong potential to formulate a new vaccine, especially with the peptide FFKEHGVPL which is likely to be the first proposed epitope-based vaccine against fructose-bisphosphate aldolase of M. mycetomatis. This study recommends an in vivo assessment for the most promising peptides especially FFKEHGVPL.

scholarly journals In Search of Antioxidant Peptides from Porcine Liver Hydrolysates Using Analytical and Peptidomic Approach

Antioxidants ◽  
2021 ◽  
Vol 11 (1) ◽  
pp. 27
Author(s):  
María López-Pedrouso ◽  
José M. Lorenzo ◽  
Paula Borrajo ◽  
Daniel Franco
Keyword(s):  
Antioxidant Capacity ◽  
Amino Acid Residues ◽  
Antioxidant Peptides ◽  
Fructose Bisphosphate ◽  
Porcine Liver ◽  
In Vivo Experiments ◽  
Adequate Quality ◽  
Health Promoting ◽  
Fructose Bisphosphate Aldolase

The search for antioxidant peptides as health-promoting agents is of great scientific interest for their biotechnological applications. Thus, the main goal of this study was to identify antioxidant peptides from pork liver using alcalase, bromelain, flavourzyme, and papain enzymes. All liver hydrolysates proved to be of adequate quality regarding the ratio EAA/NEAA, particularly flavourzyme hydrolysates. The peptidomic profiles were significantly different for each enzyme and their characterizations were performed, resulting in forty-four differentially abundant peptides among the four treatments. Porcine liver hydrolysates from alcalase and bromelain are demonstrated to have the most antioxidant capacity. On the other hand, hydrophobic amino acid residues (serine, threonine, histidine and aspartic acid) might be reducing the hydrolysates antioxidant capacity. Seventeen peptides from collagen, albumin, globin domain-containing protein, cytochrome β, fructose-bisphosphate aldolase, dihydropyrimidinase, argininosuccinate synthase, and ATP synthase seem to be antioxidant. Further studies are necessary to isolate these peptides and test them in in vivo experiments.

scholarly journals Proteomic Analysis of Soybean Leaves in a Compatible and an Incompatible Interaction with Phakopsora Pachyrhizi

2014 ◽  
Vol 1 (1) ◽  
Author(s):  
Mateus Rodrigues Pereira ◽  
Bianca Castro Gouvêa ◽  
Francismar Corrêa Marcelino-Guimarães ◽  
Humberto Josué de Oliveira Ramos ◽  
Maurilio Alves Moreira ◽  
...  
Keyword(s):  
Control Measure ◽  
Production Costs ◽  
Soybean Rust ◽  
Phakopsora Pachyrhizi ◽  
Fructose Bisphosphate ◽  
Soybean Genotypes ◽  
Fructose Bisphosphate Aldolase ◽  
Soybean Leaves ◽  
Dimensional Electrophoresis ◽  
Carbonic Anhydrase 1

AbstractAsian soybean rust (ASR), which is incited by the fungus Phakopsora pachyrhizi, is considered one of the most aggressive diseases to the soybean culture. There are no commercial cultivars immune to the pathogen and the control measure currently used is the application of fungicides that harms the environment and increases production costs. For a better understanding of the host’s response to the pathogen at the molecular level, two soybean genotypes were analyzed (PI561356, resistant to ASR and Embrapa 48, susceptible) at 72 hours and 192 hours after inoculation with spores of P. pachyrhizi. Leaf protein profiles of the plants were compared by two-dimensional electrophoresis associated with mass spectrometry (MS). Twenty-two protein spots presented different levels when the two treatments were compared (inoculated vs. non-inoculated). From those, twelve proteins were identified by MS analysis. Some of them are involved in metabolic pathways related to plant defense against pathogens, as in the case of carbonic anhydrase, 1-deoxy-D-xylulose- 5-phosphate reductoisomerase, fructose-bisphosphate aldolase and glutamine synthetase. The possible biochemical-physiological meanings of our findings are discussed.

scholarly journals Na2CO3-Responsive Photosynthetic and ROS Scavenging Mechanisms in Chloroplasts of Alkaligrass Revealed by Phosphoproteomics

2019 ◽  
Author(s):  
Jinwei Suo ◽  
Heng Zhang ◽  
Qi Zhao ◽  
Nan Zhang ◽  
Yongxue Zhang ◽  
...  
Keyword(s):  
Quantitative Proteomics ◽  
Energy Homeostasis ◽  
Thermal Dissipation ◽  
Wild Type ◽  
Ros Scavenging ◽  
Fructose Bisphosphate ◽  
Ps Ii ◽  
Ros Homeostasis ◽  
Fructose Bisphosphate Aldolase ◽  
Regulation Of Photosynthesis

Alkali-salinity exerts severe osmotic, ionic and high-pH stresses to plants. To understand the alkali-salinity responsive mechanisms underlying photosynthetic modulation and reactive oxygen species (ROS) homeostasis, physiological and diverse quantitative proteomics analyses of alkaligrass (Puccinellia tenuiflora) under Na2CO3 stress were conducted. In addition, Western blot, real-time PCR, and transgenic techniques were applied to validate the proteomic results and test the functions of the Na2CO3-responsive proteins. A total of 104 and 102 Na2CO3-responsive proteins were identified in leaves and chloroplasts, respectively. In addition, 84 Na2CO3-responsive phosphoproteins were identified, including 56 new phosphorylation sites in 56 phosphoproteins from chloroplasts, which are crucial for the regulation of photosynthesis, ion transport, signal transduction and energy homeostasis. A full-length PtFBA encoding an alkaligrass chloroplastic fructose-bisphosphate aldolase (FBA) was overexpressed in wild-type cells of cyanobacterium Synechocystis sp. Strain PCC 6803, leading to enhanced Na2CO3 tolerance. All these results indicate that thermal dissipation, state transition, cyclic electron transport, photorespiration, repair of photosystem (PS) II, PSI activity, and ROS homeostasis were altered in response to Na2CO3 stress, and they have improved our understanding of the Na2CO3-responsive mechanisms in halophytes.

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