Biochemical and physicochemical properties of thermally treated natural actomyosin extracted from normal and PSE pork Longissimus muscle

被引：34

作者：

Wang, Haihong ^{[1
]}

Pato, Mary ^{[2
]}

Pietrasik, Zeb ^{[1
]}

Shand, Phyllis ^{[1
]}

机构：

[1] Univ Saskatchewan, Dept Food & Bioprod Sci, Saskatoon, SK S7N 5A8, Canada

[2] Univ Saskatchewan, Dept Biochem, Saskatoon, SK S7N 5E5, Canada

来源：

FOOD CHEMISTRY | 2009年 / 113卷 / 01期

关键词：

PSE pork; Actomyosin; Gelation; Circular dichroism; Differential scanning calorimetry; Disulphide; Surface hydrophobicity; Dynamic rheology; HEAT-INDUCED GELATION; MYOFIBRILLAR PROTEIN; IONIC-STRENGTH; DENATURATION; AGGREGATION; PALE; SOFT; PH; MECHANISMS; GELS;

D O I：

10.1016/j.foodchem.2008.06.084

中图分类号：

O69 [应用化学];

学科分类号：

081704 ;

摘要：

Biochemical and physicochemical properties of thermally treated natural actomyosin (NAM) from normal and pale, soft and exudative (PSE) pork were studied. About 37% and 25% of available sulphydryl groups formed disulphide bonds or other permanent chemical bonds at 70 degrees C in NAM from normal and PSE pork, respectively. Surface hydrophobicities of NAM from normal and PSE pork at 70 degrees C were 3.6 and 2.4 times greater than that at 40 degrees C. About 90% of the alpha-helical structure of NAM was lost by heating to 70 degrees C. The temperature at maximum alpha-helical content decline of NAM was in accordance with the peak 3 thermal transition obtained by differential scanning calorimetry and the lowest storage modulus (G') during thermal rheology. NAM from normal pork underwent aggregation with a higher extent of hydrophobic interaction and disulphide bonds, higher temperatures at maximum velocity for conformational change and unfolding than that from PSE pork. As a consequence, NAM from normal pork had superior theological properties. (C) 2008 Elsevier Ltd. All rights reserved.

引用

页码：21 / 27

页数：7

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