|کد مقاله||کد نشریه||سال انتشار||مقاله انگلیسی||ترجمه فارسی||نسخه تمام متن|
|69295||48738||2016||6 صفحه PDF||سفارش دهید||دانلود رایگان|
• We purified a novel microbial transglutaminase from Streptomyces mobaraensis..
• The enzyme exhibited a broad range of pH and temperature stability.
• Application in bacon revealed that the enzyme is tolerant of high-salt conditions.
A novel microbial transglutaminase (MTG-TX) was obtained from Streptomyces mobaraensis by fermentation and purification. The enzyme was purified by ethanol precipitation via a two-step purification method, with a 44.0% yield and a specific activity of 39.2 U mg−1. The purified enzyme exhibited stable performance over a range of pH 5.0–pH 10.0 and displayed maximal activity at pH 6 and 48 °C. We verified through biochemical analyses that the enzyme is a novel MTG variant possessing the same zymogen characteristics as that of another reported MTG from Streptoverticillium ladakanum B1. Furthermore, the loss of enzyme activity by MTG-TX in the presence of high salt was only 79.8% that observed in a control MTG from S. mobaraensis DSM40847. On the basis of salt resistance, the novel MTG-TX presented here also performed well in food-related applications by successfully crosslinking proteins in high-salt environments, thereby enhancing the cohesiveness of bacon.
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Journal: Journal of Molecular Catalysis B: Enzymatic - Volume 133, November 2016, Pages 6–11