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      Comparative Study on Pale, Soft and Exudative (PSE) and Red, Firm and Non-Exudative (RFN) Pork: Protein Changes during Aging and the Differential Protein Expression of the Myofibrillar Fraction at 1 h Postmortem

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          Abstract

          In this paper, the protein changes during aging and the differences in the myofibrillar protein fraction at 1 h postmortem of pale, soft and exudative (PSE), and red, firm and non-exudative (RFN) pork longissimus thoracis (LT) were comparatively studied. The PSE and RFN groups were screened out based on the differences in their pH and lightness ( L*) at 1 h, and their purge loss at 24 h postmortem. Based on the measured MFI, desmin degradation, and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) analysis, PSE meat presented more significant changes in the myofibrillar protein fraction compared to RFN meat during postmortem aging. Through liquid chromatograph-mass spectrometer/mass spectrometer (LC-MS/MS) analysis, a total of 172 differential proteins were identified, among which 151 were up-regulated and 21 were down-regulated in the PSE group. The differential proteins were muscle contraction, motor proteins, microfilaments, microtubules, glycolysis, glycogen metabolism, energy metabolism, molecular chaperones, transport, and enzyme proteins. The AMP activated protein kinase (AMPK) signaling pathway, HIF-1 signaling pathway, calcium signaling pathway, and PI3K-Akt signaling pathway were identified as the significant pathways related to meat quality. This study suggested that the different changes of the myofibrillar protein fraction were involved in the biochemical metabolism in postmortem muscle, which may contribute to the molecular understanding of PSE meat formation.

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          Accurate Proteome-wide Label-free Quantification by Delayed Normalization and Maximal Peptide Ratio Extraction, Termed MaxLFQ *

          Protein quantification without isotopic labels has been a long-standing interest in the proteomics field. However, accurate and robust proteome-wide quantification with label-free approaches remains a challenge. We developed a new intensity determination and normalization procedure called MaxLFQ that is fully compatible with any peptide or protein separation prior to LC-MS analysis. Protein abundance profiles are assembled using the maximum possible information from MS signals, given that the presence of quantifiable peptides varies from sample to sample. For a benchmark dataset with two proteomes mixed at known ratios, we accurately detected the mixing ratio over the entire protein expression range, with greater precision for abundant proteins. The significance of individual label-free quantifications was obtained via a t test approach. For a second benchmark dataset, we accurately quantify fold changes over several orders of magnitude, a task that is challenging with label-based methods. MaxLFQ is a generic label-free quantification technology that is readily applicable to many biological questions; it is compatible with standard statistical analysis workflows, and it has been validated in many and diverse biological projects. Our algorithms can handle very large experiments of 500+ samples in a manageable computing time. It is implemented in the freely available MaxQuant computational proteomics platform and works completely seamlessly at the click of a button.
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            Determination of serum proteins by means of the biuret reaction.

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              Water distribution and mobility in meat during the conversion of muscle to meat and ageing and the impacts on fresh meat quality attributes--a review.

              This paper reviews current knowledge on the distribution and mobility of water in muscle (myowater) ante- and post mortem and factors affecting these in relation to fresh meat quality parameters; water-holding capacity (WHC), tenderness and juiciness. NMR transverse relaxometry (T(2)) using bench-top Low-Field Nuclear Magnetic Resonance (LF-NMR) has characterised myowater distribution and mobility as well as structural features in meat which directly affect WHC. The current literature demonstrates that WHC is correlated to the water located outside the myofibrillar network (extra-myofibrillar). This review identifies the critical stages which affect the translocation of water into the extra-myofibrillar space and thus the potential for decreased WHC during proteolysis (the conversion of muscle to meat). This review discusses how the intrinsic properties of the water held within the meat could contribute to juiciness and tenderness. Tenderness has been shown to correlate to T(2), however breed and species differences made it difficult to draw firm conclusions. Further understanding of the inherent water properties of fresh meat and the factors affecting water distribution and mobility using NMR technologies will increase the understanding of WHC and tenderisation of fresh meat. Copyright © 2011 Elsevier Ltd. All rights reserved.
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                Author and article information

                Contributors
                Role: Academic Editor
                Journal
                Foods
                Foods
                foods
                Foods
                MDPI
                2304-8158
                30 March 2021
                April 2021
                : 10
                : 4
                : 733
                Affiliations
                [1 ]Industrial Engineering Center for Huaiyang Cuisine of Jiangsu Province, College of Food Science and Engineering, Yangzhou University, Yangzhou 225127, China; ruiliu@ 123456yzu.edu.cn (R.L.); MX120180904@ 123456yzu.edu.cn (G.-Y.W.); MX120190932@ 123456yzu.edu.cn (K.-Y.L.); mgwu@ 123456yzu.edu.cn (M.-G.W.); yuhai@ 123456yzu.edu.cn (H.Y.)
                [2 ]Jiangsu Key Laboratory of Animal Genetic Breeding and Molecular Design, College of Animal Science and Technology, Yangzhou University, Yangzhou 225009, China; slwu@ 123456yzu.edu.cn
                Author notes
                [* ]Correspondence: qfge@ 123456yzu.edu.cn (Q.-F.G.); wbbao@ 123456yzu.edu.cn (W.-B.B.); Tel.: +86-0514-89786171 (Q.-F.G.)
                Author information
                https://orcid.org/0000-0001-7776-3709
                https://orcid.org/0000-0001-5486-2253
                Article
                foods-10-00733
                10.3390/foods10040733
                8066169
                33808327
                2bc87475-75b9-4354-8959-20170412f544
                © 2021 by the authors.

                Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license ( http://creativecommons.org/licenses/by/4.0/).

                History
                : 07 February 2021
                : 25 March 2021
                Categories
                Article

                pse meat,rfn meat,myofibrillar protein fraction,postmortem aging,proteomics

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