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.
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收藏
页码：21 / 27
页数：7
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