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      Ultrasound-assisted covalent reaction of myofibrillar protein: The improvement of functional properties and its potential mechanism

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          Highlights

          • •

            Different combined manner of ultrasound and covalent reaction between PPs and MP from chicken were studied.

          • •

            Ultrasound promoted MP structure unfolding, -SH exposure and OH· release simultaneously.

          • •

            Enhanced oxidation process promoted the unfolding of MP, thus contributing to the chemical and non-chemical interactions.

          • •

            Ultrasonic assisted ECG oxidation showed superior MP bio-accessibility and antioxidant activities.

          Abstract

          The effects of the different combined manner of ultrasound and covalent reaction between polyphenol and myofibrillar protein (MP) from chicken were studied. More so, antioxidant activities, digestive properties, and potential mechanism of ultrasound-assisted oxidation system of hydrophilic ((−)-Epicatechin gallate, ECG) and hydrophobic (Baicalein, BN) polyphenols was also analyzed in this study. Among all the combined treatments, surface hydrophobicity (SUH), active sulfhydryl contents (ASC), and specific surface area (SSA) of ultrasonic assisted ECG oxidation group (T6) was relatively apparent, indicating that a more unfolding MP structure was obtained. Furthermore, ultrasonic assisted ECG oxidation group showed the highest antioxidant activities compared with other combined treatments on the basis of the results of DPPH free radical scavenging activities, metal ion chelating activities, and hydroxyl radicals (OH·) scavenging activities. The results of simulated digestion system and kinetic analysis also verified that ultrasonic assisted ECG oxidation had higher MP bio-accessibility than the control group. In contrast, a lower digestibility was displayed in ultrasonic assisted BN oxidation group. In summary, the ultrasound-assisted covalent reaction of MP and ECG might be a desirable approach for industrial production of MP from chicken with better antioxidant activities and digestive properties.

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          Effects of extracellular matrix viscoelasticity on cellular behaviour

          Ovijit Chaudhuri, Justin Cooper-White, Paul A. Janmey … (2020)
          Significant research over the past two decades has established that extracellular matrix (ECM) elasticity, or stiffness, impacts fundamental cell processes including spreading, growth, proliferation, migration, differentiation, and organoid formation. Linearly elastic polyacrylamide hydrogels and polydimethylsiloxane (PDMS) elastomers coated with ECM proteins have become widely-used tools for assessing the role of stiffness, and results from these experiments are often assumed to reproduce the effect of the mechanical environment experienced by cells in vivo . However, tissues and ECMs are not linearly elastic materials – they in fact exhibit far more complex mechanical behaviors, including viscoelasticity, or a time-dependent response to loading or deformation, as well as mechanical plasticity and nonlinear elasticity. Recent work has revealed that matrix viscoelasticity regulates these same fundamental cell processes, and importantly can promote behaviors not observed with elastic hydrogels in both 2D and 3D culture microenvironments. These important findings have provided new insights into cell-matrix interactions and have given context as to how these interactions differentially modulate mechano-sensitive molecular pathways in cells. Moreover, these results indicate new design guidelines for the next generation of biomaterials that better match tissue and ECM mechanics for in vitro tissue models and applications in regenerative medicine.
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            A review on protein–phenolic interactions and associated changes

            Tugba Ozdal, Esra Capanoglu, Filiz Altay (2013)
            Article 0 comments Cited 203 times – based on 0 reviews     Review now
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              Chlorogenic acid-mediated gel formation of oxidatively stressed myofibrillar protein.

              Yungang Cao, Youling Xiong (2015)
              The effect of chlorogenic acid (CA) at different concentration levels (0, 6, 30, and 150 μmol/g protein) on porcine myofibrillar protein (MP) gelling potential in relation to chemical and structural changes was investigated. The results showed that CA generally inhibited protein carbonyl formation but did not prevent sulphydryl and amine losses caused by oxidation. The presence of CA intensified oxidation-initiated loss of α-helix conformation as well as tertiary structure of MP. CA at 150 μmol/g produced the greatest increase in MP surface hydrophobicity and insolubility. The physicochemical changes with 6 and 30 μmol/g CA led to a remarkably enhanced gelling capacity of MP and augmented the positive effect of oxidation in building an elastic gel network. However, CA at 150 μmol/g was detrimental to the MP gelation. The result can explain why processed meats with phenolic-rich spices and herbs often exhibit variable texture-forming properties.
              Article 0 comments Cited 111 times – based on 0 reviews     Review now
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                Author and article information

                Contributors
                Xinglian Xu
                Journal
                Journal ID (nlm-ta): Ultrason Sonochem
                Journal ID (iso-abbrev): Ultrason Sonochem
                Title: Ultrasonics Sonochemistry
                Publisher: Elsevier
                ISSN (Print): 1350-4177
                ISSN (Electronic): 1873-2828
                Publication date PMC-release: 24 June 2021
                Publication date Collection: August 2021
                Publication date (Electronic): 24 June 2021
                Volume: 76
                Electronic Location Identifier: 105652
                Affiliations
                [a ]Key Laboratory of Meat Processing, Ministry of Agriculture, Key Lab of Meat Processing and Quality Control, Ministry of Education, Jiangsu Collaborative Innovation Center of Meat Production and Processing, College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, China
                [b ]Department of Trauma and Reconstructive Surgery, RWTH Aachen University, Aachen 52074, Germany
                [c ]School of Pharmaceutical Sciences, Xuzhou Medical University, Xuzhou 221002, China
                [d ]State Key Laboratory of Food Science and Technology, School of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, China
                Author notes
                [* ]Corresponding author. xlxus@ 123456njau.edu.cn
                [1]

                These authors contributed equally to this work.

                Article
                Publisher Item ID: S1350-4177(21)00194-2 Publisher ID: 105652
                DOI: 10.1016/j.ultsonch.2021.105652
                PMC ID: 8251511
                PubMed ID: 34182317
                SO-VID: bebaae8a-6e30-41d0-b2c9-3aa90bb12942
                Copyright © © 2021 The Author(s)
                License:

                This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).

                History
                Date received : 23 April 2021
                Date revision received : 10 June 2021
                Date accepted : 18 June 2021
                Categories
                Subject: Original Research Article

                Keywords: myofibrillar protein (mp),ultrasound,digestive properties,(−)-epicatechin gallate (ecg),baicalein (bn)
                Data availability:
                Keywords: myofibrillar protein (mp), ultrasound, digestive properties, (−)-epicatechin gallate (ecg), baicalein (bn)

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