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Effects of heat on meat proteins - Implications on structure and quality of meat products

Tornberg, Eva LU (2005) In Meat Science 70(3). p.493-508
Abstract
Globular and fibrous proteins are compared with regard to structural behaviour on heating, where the former expands and the latter contracts. The meat protein composition and structure is briefly described. The behaviour of the different meat proteins on heating is discussed. Most of the sarcoplasmic proteins aggregate between 40 and 60 ° C, but for some of them the coagulation can extend up to 90 ° C. For myofibrillar proteins in solution unfolding starts at 30-32 ° C, followed by protein-protein association at 36-40 ° C and subsequent gelation at 45-50 ° C (cone. > 0.5% by weight). At temperatures between 53 and 63 ° C the collagen denaturation occurs, followed by collagen fibre... (More)
Globular and fibrous proteins are compared with regard to structural behaviour on heating, where the former expands and the latter contracts. The meat protein composition and structure is briefly described. The behaviour of the different meat proteins on heating is discussed. Most of the sarcoplasmic proteins aggregate between 40 and 60 ° C, but for some of them the coagulation can extend up to 90 ° C. For myofibrillar proteins in solution unfolding starts at 30-32 ° C, followed by protein-protein association at 36-40 ° C and subsequent gelation at 45-50 ° C (cone. > 0.5% by weight). At temperatures between 53 and 63 ° C the collagen denaturation occurs, followed by collagen fibre shrinkage. If the collagen fibres are not stabilised by heat-resistant intermolecular bonds, it dissolves and forms gelatine on further heating. The structural changes on cooking in whole meat and comminuted meat products, and the alterations in water-holding and texture of the meat product that it leads to, are then discussed. © 2005 Elsevier Ltd. All rights reserved. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Meat Science
volume
70
issue
3
pages
493 - 508
publisher
Elsevier
external identifiers
  • wos:000229570200010
  • scopus:33644522736
ISSN
1873-4138
DOI
10.1016/j.meatsci.2004.11.021
language
English
LU publication?
yes
id
88d9a255-499a-4f43-9c40-e452b670f927 (old id 152058)
alternative location
http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B6T9G-4FN76XM-1-15&_cdi=5114&_user=745831&_orig=search&_coverDate=07%2F31%2F2005&_sk=999299996&view=c&wchp=dGLbVzb-zSkWz&md5=ebd487ef84176c960289ab84cd886fb1&ie=/sdarticle.pdf
date added to LUP
2016-04-01 16:21:50
date last changed
2020-12-29 03:58:48
@article{88d9a255-499a-4f43-9c40-e452b670f927,
  abstract     = {Globular and fibrous proteins are compared with regard to structural behaviour on heating, where the former expands and the latter contracts. The meat protein composition and structure is briefly described. The behaviour of the different meat proteins on heating is discussed. Most of the sarcoplasmic proteins aggregate between 40 and 60 ° C, but for some of them the coagulation can extend up to 90 ° C. For myofibrillar proteins in solution unfolding starts at 30-32 ° C, followed by protein-protein association at 36-40 ° C and subsequent gelation at 45-50 ° C (cone. > 0.5% by weight). At temperatures between 53 and 63 ° C the collagen denaturation occurs, followed by collagen fibre shrinkage. If the collagen fibres are not stabilised by heat-resistant intermolecular bonds, it dissolves and forms gelatine on further heating. The structural changes on cooking in whole meat and comminuted meat products, and the alterations in water-holding and texture of the meat product that it leads to, are then discussed. © 2005 Elsevier Ltd. All rights reserved.},
  author       = {Tornberg, Eva},
  issn         = {1873-4138},
  language     = {eng},
  number       = {3},
  pages        = {493--508},
  publisher    = {Elsevier},
  series       = {Meat Science},
  title        = {Effects of heat on meat proteins - Implications on structure and quality of meat products},
  url          = {http://dx.doi.org/10.1016/j.meatsci.2004.11.021},
  doi          = {10.1016/j.meatsci.2004.11.021},
  volume       = {70},
  year         = {2005},
}