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

共 48 条

[31] THE MECHANISM OF DRIP PRODUCTION - FORMATION OF 2 COMPARTMENTS OF EXTRACELLULAR-SPACE IN MUSCLE POSTMORTEM [J].

OFFER, G ;

COUSINS, T .

JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE, 1992, 58 (01) :107-116

[32]

Offer G., 1988, DEV MEAT SCI, P173

[33] Water distribution and mobility in meat during the conversion of muscle to meat and ageing and the impacts on fresh meat quality attributes - A review [J].

Pearce, Kelly L. ;

Rosenvold, Katja ;

Andersen, Henrik J. ;

Hopkins, David L. .

MEAT SCIENCE, 2011, 89 (02) :111-124

[34] INFLUENCE OF PH AND TEMPERATURE ON PROPERTIES OF MYOSIN [J].

PENNY, IF .

BIOCHEMICAL JOURNAL, 1967, 104 (02) :609-+

[35] Theoretical aspects of water-holding in meat [J].

Puolanne, E. ;

Halonen, Marjo .

MEAT SCIENCE, 2010, 86 (01) :151-165

[36] THE AMOUNT AND COMPOSITION OF THE PROTEINS IN DRIP FROM STORED PIG MEAT [J].

SAVAGE, AWJ ;

WARRISS, PD ;

JOLLEY, PD .

MEAT SCIENCE, 1990, 27 (04) :289-303

[37] PROTEIN SOLUBILITY AS INFLUENCED BY PHYSIOLOGICAL CONDITIONS IN MUSCLE [J].

SAYRE, RN ;

BRISKEY, EJ .

JOURNAL OF FOOD SCIENCE, 1963, 28 (06) :675-&

[38] Physiological and structural events postmortem of importance for drip loss in pork [J].

Schäfer, A ;

Rosenvold, K ;

Purslow, PP ;

Andersen, HJ ;

Henckel, P .

MEAT SCIENCE, 2002, 61 (04) :355-366

[39] INFLUENCE OF POST-MORTEM CONDITIONS ON SOLUBILITIES OF MUSCLE PROTEINS [J].

SCOPES, RK .

BIOCHEMICAL JOURNAL, 1964, 91 (01) :201-+

[40] Electrostatic forces or structural scaffolding: What stabilizes the lattice spacing of relaxed skinned muscle fibers? [J].

Smith, David A. .

JOURNAL OF THEORETICAL BIOLOGY, 2014, 355 :53-60

← 1 2 3 4 5 →