Literature DB >> 22060651

Biochemical factors regulating the toughening and tenderization processes of meat.

M Koohmaraie1.   

Abstract

The purpose of this manuscript is to present a brief review of the biochemical basis for longissimus toughening and tenderization processes. Also, to explore the potential technologies that can be developed based on this knowledge to reduce variation in tenderness, thus, improving consumer acceptance of meat. Results suggest that after slaughter longissimus has low to intermediate shear force values (probably tender). Rigor development-induced changes increase its shear force. Maximum toughness is observed between 12 to 24 h post mortem. The toughening process seems to occur equally in all carcasses. Post-mortem storage at refrigerated conditions tenderizes longissimus. Post-mortem tenderization is caused by enzymatic degradation of key myofibrillar and associated proteins. The function of these proteins is to maintain the structural integrity of myofibrils. Current data indicates that μ-calpain is responsible for degradation of these proteins. Unlike the toughening process, there exists a large variation in the rate and extent of tenderization which is responsible for variation in tenderness at the consumer level. Potential strategies for the control of the variation in meat tenderness are discussed.

Year:  1996        PMID: 22060651     DOI: 10.1016/0309-1740(96)00065-4

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


  30 in total

Review 1.  A critical analysis of production-associated DNA polymorphisms in the genes of cattle, goat, sheep, and pig.

Authors:  Eveline M Ibeagha-Awemu; Patrick Kgwatalala; Xin Zhao
Journal:  Mamm Genome       Date:  2008-10-04       Impact factor: 2.957

2.  Kinetics of colour and texture changes of beef during storage.

Authors:  Daniela F Olivera; Ruth Bambicha; Gladys Laporte; Fernanda Coll Cárdenas; Nora Mestorino
Journal:  J Food Sci Technol       Date:  2012-11-06       Impact factor: 2.701

3.  A novel polymorphisms in intron 12 of the bovine calpastatin gene.

Authors:  Edyta Juszczuk-Kubiak; Joanna Wyszyńska-Koko; Krystyna Wicińska; Stanisław Rosochacki
Journal:  Mol Biol Rep       Date:  2007-01-09       Impact factor: 2.316

4.  Wet bone-in ageing and effect on beef quality technological parameters.

Authors:  Francesca Crivelli; Erica Tirloni; Cristian Bernardi; Carlo Angelo Sgoifo Rossi; Simone Stella
Journal:  J Food Sci Technol       Date:  2019-08-10       Impact factor: 2.701

5.  Effects of genetic variants for the bovine calpain gene on meat tenderness.

Authors:  Hoyoung Chung; Sungchul Shin; Euiryong Chung
Journal:  Mol Biol Rep       Date:  2014-01-28       Impact factor: 2.316

6.  Effect of mung bean and sprouted mung bean (Vigna radiata) powder on chicken breast meat tenderness, microbial and sensory characteristics.

Authors:  K Yogesh; Jamshed Ali
Journal:  J Food Sci Technol       Date:  2012-02-21       Impact factor: 2.701

7.  Association of CAST gene polymorphisms with carcass and meat quality traits in Yanbian cattle of China.

Authors:  Y X Li; H G Jin; C G Yan; K S Seo; L C Zhang; C Y Ren; X Jin
Journal:  Mol Biol Rep       Date:  2012-10-21       Impact factor: 2.316

8.  Epistasis between calpain 1 and its inhibitor calpastatin within breeds of cattle.

Authors:  W Barendse; B E Harrison; R J Hawken; D M Ferguson; J M Thompson; M B Thomas; R J Bunch
Journal:  Genetics       Date:  2007-07-01       Impact factor: 4.562

9.  Sexual Dimorphism of Metabolite Profiles in Pigs Depends on the Genetic Background.

Authors:  Manuela Peukert; Sebastian Zimmermann; Björn Egert; Christoph H Weinert; Thomas Schwarzmann; Dagmar A Brüggemann
Journal:  Metabolites       Date:  2021-04-22

10.  Monitoring post mortem changes in porcine muscle through 2-D DIGE proteome analysis of Longissimus muscle exudate.

Authors:  Alessio Di Luca; Giuliano Elia; Anne Maria Mullen; Ruth M Hamill
Journal:  Proteome Sci       Date:  2013-03-20       Impact factor: 2.480

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