Comparative study on acid-induced gelation of myosin from Atlantic cod (Gardus morhua) and burbot (Lota lota)

被引:52
作者
Riebroy, Siriporn [1 ]
Benjakul, Soottawat [1 ]
Visessanguan, Wonnop [2 ]
Erikson, Ulf [3 ]
Rustad, Turid [4 ]
机构
[1] Prince Songkla Univ, Fac Agroind, Dept Food Technol, Hat Yai 90112, Songkhla, Thailand
[2] Natl Sci & Technol Dev Agcy, Natl Ctr Genet Engn & Biotechnol, Klongluang, Pathumthani, Thailand
[3] SINTEF Fisheries & Aquaculture, N-7465 Trondheim, Norway
[4] Norwegian Univ Sci & Technol, Fac Nat Sci & Technol, Dept Biotechnol, N-7491 Trondheim, Norway
关键词
myosin; acid-induced gelation; aggregation; Atlantic cod; burbot;
D O I
10.1016/j.foodchem.2007.12.008
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
Physicochemical and theological properties of myosin from Atlantic cod and burbot during acid-induced gelation at room temperature (22-23 degrees C) by D-gluconic acid-delta-lactone (GDL) were monitored. Turbidity and particle size of both myosins increased and salt soluble content decreased when pH decreased, suggesting the formation of protein aggregates caused by acidification. The formation of disulphide bonds in myosin gelation was induced by acid. Ca2+-ATPase activity of myosin decreased (p < 0.05), while surface hydrophobicity increased during acidification (p < 0.05). Furthermore, the decreases in maximum transition temperature (T-max) and the denaturation enthalpies (Delta H) were found in both myosins. During acidification, the increases in storage modulus (G') and loss modulus (G") of myosin were observed (p < 0.05), revealing the formation of elastic gel matrix. Thus, gelation of myosin from Atlantic cod and burbot could take place under acidic pH via denaturation and aggregation. However, myosin from Atlantic cod was generally more favourable to gelation than was burbot myosin. (c) 2007 Elsevier Ltd. All rights reserved.
引用
收藏
页码:42 / 53
页数:12
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