Calpain Activity and Proteolytic Effects on Longissimus Lumborum Muscle from Hanwoo Cows and Heifers

D.E. Aguayo; D. Dashdorj; M.N. Uddin; Ch. Ochirbat; J.S. Lee; Duhak Yoon; I.H. Hwang

Calpain Activity and Proteolytic Effects on Longissimus Lumborum Muscle from Hanwoo Cows and Heifers

In: 63rd International Congress of Meat Science and Technology

Authors:

D.E. Aguayo

D.E. Aguayo ¹Department of Animal Science, Chonbuk National University, Republic of Korea

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D. Dashdorj

D. Dashdorj ¹Department of Animal Science, Chonbuk National University, Republic of Korea
²Department of Livestock Production, Mongolian University of Life Sciences, Ulaanbaatar, Mongolia

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M.N. Uddin

M.N. Uddin ¹Department of Animal Science, Chonbuk National University, Republic of Korea

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Ch. Ochirbat

Ch. Ochirbat ¹Department of Animal Science, Chonbuk National University, Republic of Korea

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J.S. Lee

J.S. Lee ¹Department of Animal Science, Chonbuk National University, Republic of Korea

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Duhak Yoon

Duhak Yoon ³Department of Animal Science, Kyungpook National University, Daegu 41566, Republic of Korea; inho.hwang@jbnu.ac.kr

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, and

I.H. Hwang

I.H. Hwang ¹Department of Animal Science, Chonbuk National University, Republic of Korea

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Type:: Chapter

Pages:: 394–395

DOI:: https://doi.org/10.3920/9789086868605_173

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Calpain activity has been categorized as the most important factor causing proteolysis on structural muscle proteins. Casein Zymogramy is a good technique to study calpain activity with no need to separate calpain and calpastatin from meat samples. Enzymatic activity between cows and heifers did not differ significantly between the two age groups during aging. Decline activities as normally expected were obtained from µ-calpain (P<0.001) and m-calpain (P<0.05). Regarding to µ-calpain, several events mediated by its activity (autolysis) were evident allowing to measure µ-calpain activity through its products of degradation. Meat from cow and heifer animals significantly differed (P<0.001) due to aging effects and at 14 d cow’s meat samples were tougher (P<0.01) than heifers’ samples. Lightness and yellowness of meat significantly increased (P<0.01), as well as cooking loss percent (P<0.01). The degradation of troponin-t bands (37 kDa) also suggested robust µ-calpain activity on myofibrillar muscle proteins along the storage period.

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63rd International Congress of Meat Science and Technology

Nurturing locally, growing globally

E-Book ISBN:: 9789086868605

Publisher:: Wageningen Academic

Print Publication Date:: 15 Nov 2017

Subjects
- Life Sciences

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Calpain Activity and Proteolytic Effects on Longissimus Lumborum Muscle from Hanwoo Cows and Heifers

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63rd International Congress of Meat Science and Technology

Nurturing locally, growing globally

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