Influence of Microbial Transglutaminase on the Quality of Wheat Flour

Abstract

Abstract: The influence of microbial transglutaminase (MTG) on the rheological properties of dough and gluten was investigated by farinograph and extensograph measurement and HPLC analysis. When 5 U/g MTG was added to wheat flour, the dough stability time increased by 18%, the degree of softening decreased about 15%, and the farinograph index also ascended. Addition of 5 U/g MTG had more significant effects on extensograph properties, and the longer the standing time, the better extensograph properties were improved. In addition, the contents of ω5-gliadin and ωb-gliadin in flour suspension declined by 99% and 88%, respectively, as opposed to 42% and 25% observed when 10 U/g MTG was added. MTG could improve the quality of gluten by catalyzing the intermolecular and intramolecular interactions of various components and producing more macromolecular proteins. In conclusion, MTG is effective in improving the quality of flour and therefore has wide prospects for applications in baked foods.

Key words: microbial transglutaminase (MTG), dough rheological properties, gluten

CLC Number:

TS211.4

References

[1] 刘冬儿. 小麦蛋白制品的开发和利用[J]. 食品科技, 1999 (1): 22-25.
[2] 贾光锋, 范丽霞, 王金水. 小麦面筋蛋白结构、功能性及应用[J]. 粮食加工, 2004 (2): 11-13.
[3] 张海华, 周惠明. 小麦面筋蛋白结构及其改性研究[J]. 粮食与油脂, 2010 (9): 1-3.
[4] 王怡然, 王金水, 赵谋明等. 小麦面筋蛋白组成、结构和特性[J]. 食品工业科技, 2007, 28 (10): 228-231.
[5] 董超华, 徐如宏, 张庆勤. 小麦醇溶蛋白和谷蛋白研究进展[J]. 山地农业生物学报, 2003, 22 (02): 164-168.
[6] 郝春燕, 李建国, 李雅轩等. 小麦醇溶蛋白基因克隆研究进展[J]. 首都师范大学学报(自然科学版）, 2006, 27 (2): 67-70.
[7] Kinetics, A., Kristiina, K., Antti, K.,et al. Kinetics of Transglutaminase-Induced Cross-Linking of Wheat Proteins in Dough[J]. Agricultural and Food Chemistry, 2005, 53: 1039-1045.
[8] Ando, H., M.Adachi., K.Umeda.,et al. Purification and characteristics of a novel transglutaminase derived from microorganisms[J]. Agricultural and Biological Chemistry, 1989, 53 (10): 2613-2617.
[9] 周迪楠, 田亚平, 华子安等. 微生物转谷氨酰胺酶的纯化方法和酶学性质研究[J]. 工业微生物, 2004, 34 (003): 20-23.
[10] Folk, J.E. and S.I.Chung. Molecular and catalytic properties of transglutaminases[J]. 1973 (38): 91-109.
[11] Iwami, k., and Yasumoto, K. Amine-binding capacities of food proteins in transglutaminase reaction and digestibility of wheat gliadin with ε-attached lysine[J]. Food Agriculture, 1986, 37: 495-503.
[12] Seguro, K., Kumazawa, Y., Kuraishi, C.,et al. The ε-(γ-glutamyl) lysine mojety in crosslinked casein is an available source for lysine for rats[J]. Nutrition, 1996, 126: 2557-2562.
[13] Larr?, C., Desserme, C., Barbot, J.,et al. Biochemical analysie and rheological properties of gluten modified by transglutaminase [J]. Cereal Chemistry, 2000, 77: 121-127.
[14] Gerrard, J. A., Fayle, S. E., Brown, P. A.,et al. Effects of microbial transglutaminase on the wheat proteins of bread and croissant dough[J]. Food Science, 2001, 66: 782-786.
[15] Bauer, N., Koehler, P., Wieser, H., et al. Studies on Effects of Microbial Transglutaminase on Gluten Proteins of Wheat.I.Biochemical Analysis[J]. Cereal Chemistry, 2003, 80 (6): 781-781.
[16] 田建珍. 专用小麦粉生产技术[M]. 郑州：郑州大学出版社, 2004.
[17] Basman, A., K?ksel, H. and Perry, K. Effects of increasing levels of transglutaminase on the rheological properties and bread quality characteristics of two wheat flours[J]. European Food Research and Technology, 2002, 215 (5): 419-424.
[18] 陈晓明. 谷氨酰胺转氨酶对大豆粉-面粉面团特性的影响[J]. 食品与机械, 2008, 24 (1): 139-142.
[19] Wieser, Y., Rinzema, A., Tramper, J., et al. Klassifizierung der Proteinkomponenten des Weizenklebers[J]. Getreide Mehl Brot, 1991, 45: 35-38.
[20] Müller, S., and Wiser, H. The location of disulphide bonds in monomeric γ-type gliadins[J]. Cereal Science, 1997, 26: 169-176.