On the water-holding of myofibrils: Effect of sarcoplasmic protein denaturation

被引：62
作者：
Liu, Jiao [1 ]
Arner, Anders [2 ]
Puolanne, Eero [1 ]
Ertbjerg, Per [1 ]
机构：
[1] Univ Helsinki, Dept Food & Environm Sci, FIN-00014 Helsinki, Finland
[2] Karolinska Inst, Dept Physiol & Pharmacol, SE-17177 Stockholm, Sweden
来源：
MEAT SCIENCE | 2016年 / 119卷
基金：
瑞典研究理事会;
关键词：
PSE; Heat denaturation; Protein aggregation; Water-holding capacity; X-ray diffraction; X-RAY-DIFFRACTION; PRE-RIGOR TEMPERATURE; CYTOSKELETAL PROTEINS; MYOFILAMENT LATTICE; QUALITY ATTRIBUTES; MUSCLE PROTEINS; MEAT QUALITY; POST-MORTEM; DRIP LOSS; PORK;
D O I：
10.1016/j.meatsci.2016.04.020
中图分类号：
TS2 [食品工业];
学科分类号：
0832 ;
摘要：
The role of heat-denatured sarcoplasmic proteins in water-holding is not well understood. Here we propose a new hypothesis that in PSE-like conditions denatured sarcoplasmic proteins aggregate within and outside myofilaments, improving the water-holding of denatured myofibrils. The process is compartmentalized: 1) within the filaments the denatured sarcoplasmic proteins shrink the lattice space and water is expelled; and 2) between the myofibrils and in the extracellular space, the coagulated sarcoplasmic proteins trap the expelled water from interfilamental space. The effect of sarcoplasmic proteins on the water-holding of myofibrils following incubation for 1 h at 21 to 44 degrees C was investigated. Our results were consistent with the new hypothesis. Myofibrils without sarcoplasm had the poorest water-holding. With increasing amount of denatured sarcoplasmic proteins, the water-holding of heat-denatured myofibrils improved proportionally. X-ray diffraction was used to measure the lattice space between the filaments. Precipitated sarcoplasmic proteins shrank (P < 0.001) the lattice spacing by 63% at 44 degrees C. (C) 2016 Elsevier Ltd. All rights reserved.
引用
收藏
页码：32 / 40
页数：9
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