Induced formation of dimethylamine and formaldehyde by lizardfish (Saurida micropectoralis) kidney trimethylamine-N-oxide demethylase

被引:39
作者
Benjakul, S [1 ]
Visessanguan, W
Tanaka, M
机构
[1] Prince Songkla Univ, Dept Food Technol, Fac Agroind, Hat Yai 90112, Songkhla, Thailand
[2] Natl Sci & Technol Dev Agcy, Natl Ctr Genet Engn & Biotechnol, Klongluang 12120, Pathumthani, Thailand
[3] Tokyo Univ Fisheries, Dept Food Sci & Technol, Minato Ku, Tokyo 1088477, Japan
基金
日本学术振兴会;
关键词
lizardfish; kidney; TMAOase; formaldehyde; dimethylamine; TMAO; muscle protein; solubility;
D O I
10.1016/S0308-8146(03)00214-0
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
The distribution of trimethylamine-N-oxide demethylase (TMAOase) in various internal organs of lizardfish (Saurida micropectoralis) and its effect on the solubility of myofibrillar proteins were studied. Among the internal organs tested, kidney contained the highest TMAOase activity, followed by spleen, bile sac, intestine and liver, respectively. TMAOase from the kidney showed a higher activity at pH 7.0 than at pH 5.0. The molecular mass was estimated to be 128 kDa, based on activity staining. In the presence of trimethylamine-N-oxide (TMAO) and cofactors (FeC(l)2, ascorbate and cysteine), addition of partially purified kidney TMAOase resulted in an increase of dimethylamine (DMA) and formaldehyde in washed mince from both red seabream (Pagrus major), white muscle fish, and skipjack (Katsuwonus pelamis), red muscle fish, during iced storage, especially in the first 6 days. TMAOase addition led to a loss in protein solubility, which is associated with increased cross-linking of protein. Therefore, contamination of muscle by TMAOase from internal organs, especially kidney, possibly causes the changes in fish texture. (C) 2003 Elsevier Ltd. All rights reserved.
引用
收藏
页码:297 / 305
页数:9
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