Free amino acids, collagen solubility, and meat quality in pork (Longissimus muscle of Yorkshire) as a function of chiller temperature and aging
2008
Park, B.Y. (National Livestock Research Institute, RDA, Suwon, Republic of Korea) | Park, K.M. (Chonbuk National University, Jeonju, Republic of Korea) | Kim, J.H. (National Livestock Research Institute, RDA, Suwon, Republic of Korea) | Cho, S.H. (National Livestock Research Institute, RDA, Suwon, Republic of Korea) | Kim, N.K. (Konkuk University, Chungju, Republic of Korea) | Song, M.J. (Konkuk University, Chungju, Republic of Korea) | Lee, C.S. (Konkuk University, Chungju, Republic of Korea) | Cho, I.K. (Nambu University, Gwangju, Republic of Korea) | Choe, H.S. (Chonbuk National University, Jeonju, Republic of Korea) | Ryu, K.S. (Chonbuk National University, Jeonju, Republic of Korea) | Hwang, I.H. (Chonbuk National University, Jeonju, Republic of Korea), E-mail: [email protected]
This study was conducted to identify the effect of chilling temperature (-3 and 6℃) and aging (1- and 7-day) on objective meat quality, collagen solubility, and free amino acids in pork (longissimus muscle of Yorkshire). Warner-Bratzler (WB)-shear force indicated that variation in chilling temperature had no detectable effect on meat tenderness and tenderization during the 7-day aging period. Among the 13 detected free amino acids, only 3 amino acids (histidine, valine, leucine) were significantly affected by the temperature treatment (p less than 0.05). Collagen solubility was significantly increased at 6℃ treatment (p less than 0.05). There was a significant linear relationship (r = 0.67, p less than 0.05) between changes in free amino acids and WB-shear force during the 7-day aging period. These results confirmed that chilling conditions had significantly affected collagen solubility, and meat tenderization occurred in direct proportion to an increase in free amino acids.
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