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

被引：64

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

页码：32 / 40

页数：9

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