{"title":"Ultrasonication Induced Alterations in Physicochemical and Functional Properties of Myosin.","authors":"Rashid Saleem, Riaz Ahmad","doi":"10.2174/0929866530666230124093804","DOIUrl":null,"url":null,"abstract":"<p><strong>Background: </strong>Several reports have indicated that ultrasonication can change the solubility of muscle proteins and improves the functional properties of meat and isolated muscle proteins. Moreover, available literature suggests that ultrasonication can significantly improve the gelling properties of muscle proteins.</p><p><strong>Objectives: </strong>The present study was carried out to investigate the effect of low-frequency ultrasonication on the secondary structure of myosin and the impact of these structural changes on solubility and gelling ability.</p><p><strong>Methods: </strong>Myosin from breast muscles (Pectoralis major) of broiler chicken was extracted and exposed to low-frequency ultrasonication for 30 min. Four aliquots collected at the interval of 5, 10, 20, and 30 min were analysed for change in ATPase activity, sulfhydryl content, surface hydrophobicity, alpha-helicity. The possible impact of these changes on heat-induced gelation was observed through electron micrographs.</p><p><strong>Results: </strong>Ultrasonication reduced the enzymatic activity of myosin and increased the reactive sulfhydryl content. Decreased α-helicity and increased intrinsic fluorescence displayed significant structural changes at the secondary and tertiary levels. Myosin aggregation, as indicated by electron micrographs, showed a marked decrease. The microstructure of myosin gels displayed a distinct correlation with ultrasonication-induced structural changes. Furthermore, improved microstructure led to a significant increase in the water retention capacity of myosin gels.</p><p><strong>Conclusion: </strong>In conclusion, ultrasonication of myosin caused a marked change in structure at the tertiary and secondary levels. Structural changes apparently confined within the globular head region and rod portion of myosin were displayed by reduced enzymatic activity and improved gelation/solubility. Results of our study convincingly showed that ultrasonication improved the microstructure of myosin gels resulting in increased WHC.</p>","PeriodicalId":20736,"journal":{"name":"Protein and Peptide Letters","volume":null,"pages":null},"PeriodicalIF":1.0000,"publicationDate":"2023-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Protein and Peptide Letters","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.2174/0929866530666230124093804","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
引用次数: 0
Abstract
Background: Several reports have indicated that ultrasonication can change the solubility of muscle proteins and improves the functional properties of meat and isolated muscle proteins. Moreover, available literature suggests that ultrasonication can significantly improve the gelling properties of muscle proteins.
Objectives: The present study was carried out to investigate the effect of low-frequency ultrasonication on the secondary structure of myosin and the impact of these structural changes on solubility and gelling ability.
Methods: Myosin from breast muscles (Pectoralis major) of broiler chicken was extracted and exposed to low-frequency ultrasonication for 30 min. Four aliquots collected at the interval of 5, 10, 20, and 30 min were analysed for change in ATPase activity, sulfhydryl content, surface hydrophobicity, alpha-helicity. The possible impact of these changes on heat-induced gelation was observed through electron micrographs.
Results: Ultrasonication reduced the enzymatic activity of myosin and increased the reactive sulfhydryl content. Decreased α-helicity and increased intrinsic fluorescence displayed significant structural changes at the secondary and tertiary levels. Myosin aggregation, as indicated by electron micrographs, showed a marked decrease. The microstructure of myosin gels displayed a distinct correlation with ultrasonication-induced structural changes. Furthermore, improved microstructure led to a significant increase in the water retention capacity of myosin gels.
Conclusion: In conclusion, ultrasonication of myosin caused a marked change in structure at the tertiary and secondary levels. Structural changes apparently confined within the globular head region and rod portion of myosin were displayed by reduced enzymatic activity and improved gelation/solubility. Results of our study convincingly showed that ultrasonication improved the microstructure of myosin gels resulting in increased WHC.
期刊介绍：
Protein & Peptide Letters publishes letters, original research papers, mini-reviews and guest edited issues in all important aspects of protein and peptide research, including structural studies, advances in recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, and drug design. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallization and preliminary structure determination of biologically important proteins are considered only if they include significant new approaches or deal with proteins of immediate importance, and preliminary structure determinations of biologically important proteins. Purely theoretical/review papers should provide new insight into the principles of protein/peptide structure and function. Manuscripts describing computational work should include some experimental data to provide confirmation of the results of calculations.
Protein & Peptide Letters focuses on:
Structure Studies
Advances in Recombinant Expression
Drug Design
Chemical Synthesis
Function
Pharmacology
Enzymology
Conformational Analysis
Immunology
Biotechnology
Protein Engineering
Protein Folding
Sequencing
Molecular Recognition
Purification and Analysis
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