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Application of microbial transglutaminase on protein food industry
|Contributors: ||NTOU:Department of Food Science|
|Issue Date: ||2013-10-07T02:26:35Z
|Abstract: ||摘要:轉麩胺酸醯胺基酶 (transglutaminase, TGase) 為一常用蛋白質修飾酵素，經催化蛋白質分子間或分子內形成 e-(g-glutamyl) lysine 共價鍵，對大豆蛋白、酪蛋白、肌凝蛋白等具聚合作用，故改變蛋白質溶解性、保水力、熱安定性等官能特性。微生物 TGase 以麩胺酸殘基g-羧基作為醯基供給者，離胺酸殘基 e-胺基作為醯基接受者，反應後釋出氨，形成 e-(g-glutamyl)lysine 架橋結合。MTGase 催化作用會受到蛋白質構形影響，需在低溫下反應，才能促使蛋白質形膠，故探討此酵素最適添加量、作用溫度與時間，並測定MTGase活性，使該酵素應用於蛋白質形膠。若能利用生物技術平台生產具 cross-linking 能力之酵素如轉麩胺酸醯胺基酶、酪胺酸酶 (tyrosinase)等作為改善傳統加工產品品質，對於促進傳統產業蛻變將有極大助益，也是產業界、學術界及政府相關單位極力推動的重要目標。|
Abstract:Transglutaminase (TGase) is protein modifying enzyme, which can catalyze the cross-linkage of e-(g-glutamyl) lysine among protein molecules and peptides including soy bean proteins, casein, and muscle proteins. This modification will change their functionalities such as solubility, water holding capacity and thermal stability. Catalysis by microbial TGase was considered to be affected by the conformation of proteins and needed an appropriate reaction time to form e-(g-glutamyl) lysine bonding. Accordingly, this study will investigate the optimal condition for the production of MTGase using GRAS bacteria, optimal catalysis conditions including catalysis temperature and time, amount of enzyme addition, etc. and determination of MTGase activity. Comparison of the quality of protein foods with modification by MTGase with typical protein foods. The platform for the production of MTGase and the technology for the improvement of protein foods will employ to promote and upgrade the traditional food industry.
|Appears in Collections:||[食品科學系] 研究計畫|
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