Literature DB >> 22055084

Conformational changes in the muscle proteins of cured beef during heating.

E F Oreshkin1, M A Borisova, G S Tchubarova, V M Gorbatov, E A Permyakov, V L Shnyrov, E A Burstein.   

Abstract

Structural changes caused by heating in the proteins of cured beef longissimus dorsi muscle were examined by fluorescence and differential scanning calorimetry. Denaturation occurred in four temperature ranges-40-55°C, 55-61°C, 62-70°C and above 70°C, in contrast to the three endothermic transitions reported for non-cured meats.
Copyright © 1986. Published by Elsevier Ltd.

Year:  1986        PMID: 22055084     DOI: 10.1016/0309-1740(86)90040-9

Source DB:  PubMed          Journal:  Meat Sci        ISSN: 0309-1740            Impact factor:   5.209


  1 in total

1.  Differential Scanning Calorimetry - A Method for Assessing the Thermal Stability and Conformation of Protein Antigen.

Authors:  Ibrahim B Durowoju; Kamaljit S Bhandal; Jian Hu; Bruce Carpick; Marina Kirkitadze
Journal:  J Vis Exp       Date:  2017-03-04       Impact factor: 1.355

  1 in total

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