Literature DB >> 32180654

Estimating the structure of sarcoplasmic proteins extracted from pork tenderloin thawed by a high-voltage electrostatic field.

Guoliang Jia1,2,3, Frans van den Berg4, Han Hao5, Haijie Liu1,2.   

Abstract

The application of high-voltage electrostatic field (HVEF) is a novel method of thawing. To determine if HVEF thawing could lead to sarcoplasmic proteins denaturation, and to provide a theoretical estimation of the structure of the sarcoplasmic proteins, pork tenderloin was thawed by traditional and HVEF methods. The results from protein solubility analysis, sodium dodecyl sulfate-polyacrylamide gel electrophoresis, Fourier transform infrared spectroscopy (FTIR) and differential scanning calorimeter showed that HVEF thawing did not result in more protein denaturation than those thawed under air or running water. From the principal component analysis of FTIR raw spectra (1700-1600 cm-1, Amide I region), we observed some separations of samples with different thawing treatments. It was found that the proportions of α-helix (1650-1640 cm-1 spectral bands in the original data) could lead to the differences on the PC2 axis of score plots. © Association of Food Scientists & Technologists (India) 2020.

Entities:  

Keywords:  Denaturation; HVEF; Pork tenderloin; Sarcoplasmic proteins

Year:  2020        PMID: 32180654      PMCID: PMC7054592          DOI: 10.1007/s13197-020-04253-4

Source DB:  PubMed          Journal:  J Food Sci Technol        ISSN: 0022-1155            Impact factor:   2.701


  12 in total

1.  Decreased gelling and emulsifying properties of myofibrillar protein from repeatedly frozen-thawed porcine longissimus muscle are due to protein denaturation and susceptibility to aggregation.

Authors:  Xiufang Xia; Baohua Kong; Youling Xiong; Yanming Ren
Journal:  Meat Sci       Date:  2010-02-20       Impact factor: 5.209

2.  Characterizing salt substitution in beef meat processing by vibrational spectroscopy and sensory analysis.

Authors:  Nebojsa Perisic; Nils Kristian Afseth; Ragni Ofstad; Bjørg Narum; Achim Kohler
Journal:  Meat Sci       Date:  2013-06-05       Impact factor: 5.209

Review 3.  The principles of high voltage electric field and its application in food processing: A review.

Authors:  Mohsen Dalvi-Isfahan; Nasser Hamdami; Alain Le-Bail; Epameinondas Xanthakis
Journal:  Food Res Int       Date:  2016-09-03       Impact factor: 6.475

4.  Physicochemical changes of myofibrillar proteins during processing of Cantonese sausage in relation to their aggregation behaviour and in vitro digestibility.

Authors:  Weizheng Sun; Feibai Zhou; Mouming Zhao; Bao Yang; Chun Cui
Journal:  Food Chem       Date:  2011-05-04       Impact factor: 7.514

Review 5.  What vibrations tell us about proteins.

Authors:  Andreas Barth; Christian Zscherp
Journal:  Q Rev Biophys       Date:  2002-11       Impact factor: 5.318

6.  Physicochemical changes in myofibrillar proteins extracted from pork tenderloin thawed by a high-voltage electrostatic field.

Authors:  Guoliang Jia; Satoru Nirasawa; Xiaohua Ji; Yongkang Luo; Haijie Liu
Journal:  Food Chem       Date:  2017-07-26       Impact factor: 7.514

7.  Tracking hydrophobicity state, aggregation behaviour and structural modifications of pork proteins under the influence of assorted heat treatments.

Authors:  Bhaskar Mitra; Åsmund Rinnan; Jorge Ruiz-Carrascal
Journal:  Food Res Int       Date:  2017-09-09       Impact factor: 6.475

8.  Proteomic study of muscle sarcoplasmic proteins using AUT-PAGE/SDS-PAGE as two-dimensional gel electrophoresis.

Authors:  Gianluca Picariello; Alessandra De Martino; Gianfranco Mamone; Pasquale Ferranti; Francesco Addeo; Michele Faccia; Salvatore Spagnamusso; Aldo Di Luccia
Journal:  J Chromatogr B Analyt Technol Biomed Life Sci       Date:  2006-02-28       Impact factor: 3.205

Review 9.  The use and misuse of FTIR spectroscopy in the determination of protein structure.

Authors:  M Jackson; H H Mantsch
Journal:  Crit Rev Biochem Mol Biol       Date:  1995       Impact factor: 8.250

10.  Structural changes and dynamic rheological properties of sarcoplasmic proteins subjected to pH-shift method.

Authors:  Panchaporn Tadpitchayangkoon; Jae W Park; Steven G Mayer; Jirawat Yongsawatdigul
Journal:  J Agric Food Chem       Date:  2010-04-14       Impact factor: 5.279

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