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Current Nutrition & Food Science

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ISSN (Print): 1573-4013
ISSN (Online): 2212-3881

Review Article

Application of Microbial Transglutaminase in Wheat Bread Industry: A Review

Author(s): Neda M. Meybodi, Leila Mirmoghtadaie*, Zhaleh Sheidaei, Masoumeh Arab, Sarah S. Nasab, Musarreza Taslikh and Amir M. Mortazavian*

Volume 17, Issue 5, 2021

Published on: 01 October, 2020

Page: [450 - 457] Pages: 8

DOI: 10.2174/1573401316999201001145814

Price: $65

Abstract

Bread as the main food all over the world is generally based on wheat flour due to its unique properties to form a three-dimensional gluten network. In fact, the quality of bread is influenced by wheat gluten quality and quantity. The quality of gluten protein is mainly defined based on its amino acids composition and bonding (covalent and non-covalent). Gluten protein quality is considered weak based on its essential amino acid content: lysine and threonine. Covalent crosslinks as the main factor in determining the integrity of the gluten network are also interrupted by the activity of proteolytic enzymes and reducing agents. Different treatments (physical, chemical and enzymatic) are used to alleviate these detrimental effects and improve the bread making quality of wheat flour. Given that, food industry is looking for using enzymes (respecting their specificity, ease of use and low risk of toxic products formation) microbial transglutaminase is an efficient option, considering its ability to introduce new crosslinks. This new crosslink formation can either improve gluten protein quality in damaged wheat flour or imitate the function of gluten protein in gluten free bread. The aim of this article is to review the application of microbial transglutaminase enzyme as an improving agent in wheat bread industry.

Keywords: Wheat bread, transglutaminase, gluten, enzyme, function, application.

Graphical Abstract
[1]
Joye IJ, Lagrain B, Delcour JA. Use of chemical redox agents and exogenous enzymes to modify the protein network during breadmaking–a review. J Cereal Sci 2009; 50(1): 11-21.
[http://dx.doi.org/10.1016/j.jcs.2009.04.001]
[2]
Goesaert H, Brijs K, Veraverbeke W, Courtin C, Gebruers K, Delcour J. Wheat flour constituents: how they impact bread quality, and how to impact their functionality. Trends Food Sci Technol 2005; 16(1): 12-30.
[http://dx.doi.org/10.1016/j.tifs.2004.02.011]
[3]
Wang P, Jin Z, Xu X. Physicochemical alterations of wheat gluten proteins upon dough formation and frozen storage–a review from gluten, glutenin and gliadin perspectives. Trends Food Sci Technol 2015; 46(2): 189-98.
[http://dx.doi.org/10.1016/j.tifs.2015.10.005]
[4]
Regula J, Kedzior Z. Gluten-free bread: health and technological aspects bread and its fortification food biology series. CRC Press 2015; pp. 373-403.
[5]
Wieser H. Chemistry of gluten proteins. Food Microbiol 2007; 24(2): 115-9.
[http://dx.doi.org/10.1016/j.fm.2006.07.004] [PMID: 17008153]
[6]
Song Y, Zheng Q. Dynamic rheological properties of wheat flour dough and proteins. Trends Food Sci Technol 2007; 18(3): 132-8.
[http://dx.doi.org/10.1016/j.tifs.2006.11.003]
[7]
Turfani V, Narducci V, Durazzo A, Galli V, Carcea M. Technological, nutritional and functional properties of wheat bread enriched with lentil or carob flours. Food Sci Tech 2017; 78(Suppl. C): 361-6.
[http://dx.doi.org/10.1016/j.lwt.2016.12.030]
[8]
Gujral HS, Rosell CM. Improvement of the breadmaking quality of rice flour by glucose oxidase. Food Res Int 2004; 37(1): 75-81.
[http://dx.doi.org/10.1016/j.foodres.2003.08.001]
[9]
Lambrecht M. Interactions and reactions between different types of proteins and their importance in wheat-based model and noodle systems 2016.
[10]
Ortolan F, Steel CJ. Protein characteristics that affect the quality of vital wheat gluten to be used in baking: a review. Compr Rev Food Sci Food Saf 2017; 16(3): 369-81.
[http://dx.doi.org/10.1111/1541-4337.12259]
[11]
Mollakhalili Meybodi N, Mohammadifar MA, Feizollahi E. Gluten-free bread quality: a review of the improving factors. J Food Qual Hazards Control 2015; 2(3): 81-5.
[12]
Caballero P, Bonet A, Rosell C, Gómez M. Effect of microbial transglutaminase on the rheological and thermal properties of insect damaged wheat flour. J Cereal Sci 2005; 42(1): 93-100.
[http://dx.doi.org/10.1016/j.jcs.2004.12.006]
[13]
Meerts M, Van Ammel H, Meeus Y, et al. Enhancing the rheological performance of wheat flour dough with glucose oxidase, transglutaminase or supplementary gluten. Food Bioproc Tech 2017; 10: 2188-98.
[14]
Yokoyama K, Nio N, Kikuchi Y. Properties and applications of microbial transglutaminase. Appl Microbiol Biotechnol 2004; 64(4): 447-54.
[http://dx.doi.org/10.1007/s00253-003-1539-5] [PMID: 14740191]
[15]
Kieliszek M, Misiewicz A. Microbial transglutaminase and its application in the food industry. A review. Folia Microbiol (Praha) 2014; 59(3): 241-50.
[http://dx.doi.org/10.1007/s12223-013-0287-x] [PMID: 24198201]
[16]
Jaros D, Partschefeld C, Henle T, Rohm H. Transglutaminase in dairy products: chemistry, physics, applications. J Texture Stud 2006; 37(2): 113-55.
[http://dx.doi.org/10.1111/j.1745-4603.2006.00042.x]
[17]
Kanaji T, Ozaki H, Takao T, et al. Primary structure of microbial transglutaminase from Streptoverticillium sp. strain s-8112. J Biol Chem 1993; 268(16): 11565-72.
[PMID: 8099353]
[18]
Aaron L, Torsten M. Microbial transglutaminase: a new potential player in celiac disease. Clin Immunol 2019; 199: 37-43.
[http://dx.doi.org/10.1016/j.clim.2018.12.008] [PMID: 30543926]
[19]
Romeih E, Walker G. Recent advances on microbial transglutaminase and dairy application. Trends Food Sci Technol 2017; 62(Suppl. C): 133-40.
[http://dx.doi.org/10.1016/j.tifs.2017.02.015]
[20]
Heil A, Ohsam J, van Genugten B, et al. Microbial transglutaminase used in bread preparation at standard bakery concentrations does not increase immunodetectable amounts of deamidated gliadin. J Agric Food Chem 2017; 65(32): 6982-90.
[http://dx.doi.org/10.1021/acs.jafc.7b02414] [PMID: 28721717]
[21]
de Góes-Favoni SP, Bueno FR. Microbial transglutaminase: general characteristics and performance in food processing technology. Food Biotechnol 2014; 28(1): 1-24.
[http://dx.doi.org/10.1080/08905436.2013.870076]
[22]
Santhi D, Kalaikannan A, Malairaj P, Arun Prabhu S. Application of microbial transglutaminase in meat foods: a review. Crit Rev Food Sci Nutr 2017; 57(10): 2071-6.
[http://dx.doi.org/10.1080/10408398.2014.945990] [PMID: 25897817]
[23]
Moore MM, Heinbockel M, Dockery P, Ulmer H, Arendt EK. Network formation in gluten-free bread with application of transglutaminase. Cereal Chem 2006; 83(1): 28-36.
[http://dx.doi.org/10.1094/CC-83-0028]
[24]
Masci S, Lafiandra D, D’Ovidio R. The gluten proteins. Royal Society of Chemistry 2004.
[25]
Bailey CH. The chemistry of wheat flour. Chemical Catalog Company 1925.
[26]
Onyango C, Mutungi C, Unbehend G, Lindhauer MG. Rheological and baking characteristics of batter and bread prepared from pregelatinised cassava starch and sorghum and modified using microbial transglutaminase. J Food Eng 2010; 97(4): 465-70.
[http://dx.doi.org/10.1016/j.jfoodeng.2009.11.002]
[27]
Corke H, De Leyn I, Nip W-K, Cross NA. Bakery products: science and technology. Hoboken, NJ: John Wiley & Sons 2008.
[28]
Kunkulberga D, Seglins V. Maizes ražošanas tehnoloģija (Technology of breadmaking). Latvia: RTU izdevniecība 2010.
[29]
Luongo D, Maurano F, Bergamo P, Rossi M. Microbial transglutaminase: a biotechnological tool to manage gluten intolerance. Anal Biochem 2020; 592: 113584.
[http://dx.doi.org/10.1016/j.ab.2020.113584] [PMID: 31953047]
[30]
Kumar J, Kumar M, Pandey R, Chauhan NS. Physiopathology and management of gluten-induced celiac disease. J Food Sci 2017; 82(2): 270-7.
[http://dx.doi.org/10.1111/1750-3841.13612] [PMID: 28140462]
[31]
Helmerhorst EJ, Zamakhchari M, Schuppan D, Oppenheim FG. Discovery of a novel and rich source of gluten-degrading microbial enzymes in the oral cavity. PLoS One 2010; 5(10): e13264.
[http://dx.doi.org/10.1371/journal.pone.0013264] [PMID: 20948997]
[32]
Engstrom N, Saenz-Méndez P, Scheers J, Scheers N. Towards Celiac-safe foods: decreasing the affinity of transglutaminase 2 for gliadin by addition of ascorbyl palmitate and ZnCl2 as detoxifiers. Sci Rep 2017; 7(1): 77.
[http://dx.doi.org/10.1038/s41598-017-00174-z] [PMID: 28250436]
[33]
Hall NJ, Rubin G, Charnock A. Systematic review: adherence to a gluten-free diet in adult patients with coeliac disease. Aliment Pharmacol Ther 2009; 30(4): 315-30.
[http://dx.doi.org/10.1111/j.1365-2036.2009.04053.x] [PMID: 19485977]
[34]
Mohammadi M, Azizi M-H, Neyestani TR, Hosseini H, Mortazavian AM. Development of gluten-free bread using guar gum and transglutaminase. J Ind Eng Chem 2015; 21: 1398-402.
[http://dx.doi.org/10.1016/j.jiec.2014.06.013]
[35]
Skovbjerg H, Koch C, Anthonsen D, Sjöström H. Deamidation and cross-linking of gliadin peptides by transglutaminases and the relation to celiac disease. Biochim Biophys Acta 2004; 1690(3): 220-30.
[http://dx.doi.org/10.1016/j.bbadis.2004.06.009] [PMID: 15511629]
[36]
Dekking EHA, Van Veelen PA, de Ru A, Kooy-Winkelaar EMC, Gröneveld T, Nieuwenhuizen WF, et al. Microbial transglutaminases generate T cell stimulatory epitopes involved in celiac disease. J Cereal Sci 2008; 47(2): 339-46.
[http://dx.doi.org/10.1016/j.jcs.2007.05.004]
[37]
Gianfrani C, Siciliano RA, Facchiano AM, et al. Transamidation of wheat flour inhibits the response to gliadin of intestinal T cells in celiac disease. Gastroenterology 2007; 133(3): 780-9.
[http://dx.doi.org/10.1053/j.gastro.2007.06.023] [PMID: 17678925]
[38]
Lombardi E, Bergamo P, Maurano F, et al. Selective inhibition of the gliadin-specific, cell-mediated immune response by transamidation with microbial transglutaminase. J Leukoc Biol 2013; 93(4): 479-88.
[http://dx.doi.org/10.1189/jlb.0412182] [PMID: 23108099]
[39]
Lerner A, Matthias T. Food industrial microbial transglutaminase in celiac disease: treat or trick. Int J Celiac Dis 2015; 3(1): 1-6.
[40]
Phimolsiripol Y, Siripatrawan U, Tulyathan V, Cleland DJ. Effects of freezing and temperature fluctuations during frozen storage on frozen dough and bread quality. J Food Eng 2008; 84(1): 48-56.
[http://dx.doi.org/10.1016/j.jfoodeng.2007.04.016]
[41]
Giannou V, Kessoglou V, Tzia C. Quality and safety characteristics of bread made from frozen dough. Trends Food Sci Technol 2003; 14(3): 99-108.
[http://dx.doi.org/10.1016/S0924-2244(02)00278-9]
[42]
Selomulyo VO, Zhou W. Frozen bread dough: effects of freezing storage and dough improvers. J Cereal Sci 2007; 45(1): 1-17.
[http://dx.doi.org/10.1016/j.jcs.2006.10.003]
[43]
Sun D-W. Handbook of frozen food processing and packaging. USA: CRC Press 2016.
[http://dx.doi.org/10.1201/b11204]
[44]
Yi J. Improving frozen bread dough quality through processing and ingredients. PhD Thesis. University of Georgia: Athens 2008.
[45]
Rosell CM, Gómez M. Frozen dough and partially baked bread: an update. Food Rev Int 2007; 23(3): 303-19.
[http://dx.doi.org/10.1080/87559120701418368]
[46]
Dizlek H, Özer MS. Improvement bread characteristics of high level sunn pest (Eurygaster integriceps) damaged wheat by using transglutaminase and some additives. J Cereal Sci 2017; 77: 90-6.
[http://dx.doi.org/10.1016/j.jcs.2017.08.003]
[47]
Pico J, Bernal J, Gómez M. Wheat bread aroma compounds in crumb and crust: a review. Food Res Int 2015; 75: 200-15.
[http://dx.doi.org/10.1016/j.foodres.2015.05.051] [PMID: 28454949]
[48]
La Rosa D, Barba A, Frias-Hernández J, Olalde-Portugal V, González Castañeda J. Processing, nutritional evaluation, and utilization of whole mesquite flour (Prosopis laevigata). J Food Sci 2006; 71(4)
[http://dx.doi.org/10.1111/j.1750-3841.2006.00001.x]
[49]
Hefnawy T, El-Shourbagy G, Ramadan M. Impact of adding chickpea (Cicer arietinum L.) flour to wheat flour on the rheological properties of toast bread. Int Food Res J 2012; 19(2): 521-5.
[50]
Bigne F, Romero A, Ferrero C, Puppo M, Guerrero A. Rheological and microstructural study of wheat doughs partially replaced with mesquite flour (Prosopis alba) and added with transglutaminase. Food Bioprocess Technol 2017; 10(5): 819-30.
[http://dx.doi.org/10.1007/s11947-017-1869-4]
[51]
Basman A, Köksel H, Ng P. Utilization of transglutaminase to increase the level of barley and soy flour incorporation in wheat flour breads. J Food Sci 2003; 68(8): 2453-60.
[http://dx.doi.org/10.1111/j.1365-2621.2003.tb07045.x]
[52]
Hu X, Xu X, Fan J-F, Cheng Y-Q, Li L. Functional properties of microbial transglutaminase modified soybean glycinin and?- conglycinin. Int J Food Eng 2011; 7(2): 4.
[http://dx.doi.org/10.2202/1556-3758.2158]
[53]
Gharibzahedi SMT, Yousefi S, Chronakis IS. Microbial transglutaminase in noodle and pasta processing. Crit Rev Food Sci Nutr 2017.
[54]
Motoki M, Kumazawa Y. Recent research trends in transglutaminase technology for food processing. Food Sci Technol Res 2000; 6(3): 151-60.
[http://dx.doi.org/10.3136/fstr.6.151]
[55]
Seguro K, Kumazawa Y, Ohtsuka T, et al. Epsilon.-(.gamma.-glutamyl) lysine: hydrolysis by. gamma.-glutamyltransferase of different origins, when free or protein bound. J Agric Food Chem 1995; 43(8): 1977-81.
[http://dx.doi.org/10.1021/jf00056a004]
[56]
Nonaka M, Matsuura Y, Motoki M. Incorporation of lysine-and lysine dipeptides into α s1-casein by Ca2+-independent microbial transglutaminase. Biosci Biotechnol Biochem 1996; 60(1): 131-3.
[http://dx.doi.org/10.1271/bbb.60.131]
[57]
Seguro K, Kumazawa Y, Kuraishi C, Sakamoto H, Motoki M. The epsilon-(gamma-glutamyl)lysine moiety in crosslinked casein is an available source of lysine for rats. J Nutr 1996; 126(10): 2557-62.
[http://dx.doi.org/10.1093/jn/126.10.2557] [PMID: 8857517]
[58]
Hu X, Legler PM, Khavrutskii I, et al. Probing the donor and acceptor substrate specificity of the γ-glutamyl transpeptidase. Biochemistry 2012; 51(6): 1199-212.
[http://dx.doi.org/10.1021/bi200987b] [PMID: 22257032]
[59]
Motoki M, Seguro K. Transglutaminase and its use for food processing. Trends Food Sci Technol 1998; 9(5): 204-10.
[http://dx.doi.org/10.1016/S0924-2244(98)00038-7]
[60]
Kuraishi C, Yamazaki K, Susa Y. Transglutaminase: its utilization in the food industry. Food Rev Int 2001; 17(2): 221-46.
[http://dx.doi.org/10.1081/FRI-100001258]
[61]
Cauvain SP, Young LS. Technology of breadmaking 2007; 82-3.
[62]
Renzetti S, Dal Bello F, Arendt EK. Microstructure, fundamental rheology and baking characteristics of batters and breads from different gluten-free flours treated with a microbial transglutaminase. J Cereal Sci 2008; 48(1): 33-45.
[http://dx.doi.org/10.1016/j.jcs.2007.07.011]
[63]
Shin M, Gang D-O, Song J-Y. Effects of protein and transglutaminase on the preparation of gluten-free rice bread. Food Sci Biotechnol 2010; 19(4): 951-6.
[http://dx.doi.org/10.1007/s10068-010-0133-8]
[64]
Pongjaruvat W, Methacanon P, Seetapan N, Fuongfuchat A, Gamonpilas C. Influence of pregelatinised tapioca starch and transglutaminase on dough rheology and quality of gluten-free jasmine rice breads. Food Hydrocoll 2014; 36(Suppl. C): 143-50.
[http://dx.doi.org/10.1016/j.foodhyd.2013.09.004]
[65]
Smerdel B, Pollak L, Novotni D, Čukelj N, Benković M, Lušić D, et al. Improvement of gluten-free bread quality using transglutaminase, various extruded flours and protein isolates. J Food Nutr Res 2012; 51(4): 242-53.
[66]
Huang W, Yuan Y, Kim Y, Chung O. Effects of transglutaminase on rheology, microstructure, and baking properties of frozen dough. Cereal Chem 2008; 85(3): 301-6.
[http://dx.doi.org/10.1094/CCHEM-85-3-0301]
[67]
Kim YS, Huang W, Du G, Pan Z, Chung O. Effects of trehalose, transglutaminase, and gum on rheological, fermentation, and baking properties of frozen dough. Food Res Int 2008; 41(9): 903-8.
[http://dx.doi.org/10.1016/j.foodres.2008.07.013]
[68]
Li Z, Tang X, Huang W, Liu JG, Tilley M, Yao Y. Rheology, microstructure, and baking characteristics of frozen dough containing Rhizopus chinensis lipase and transglutaminase. Cereal Chem 2011; 88(6): 596-601.
[http://dx.doi.org/10.1094/CCHEM-07-11-0082]
[69]
Steffolani ME, Ribotta PD, Perez GT, Puppo MC, León AE. Use of enzymes to minimize dough freezing damage. Food Bioprocess Technol 2012; 5(6): 2242-55.
[http://dx.doi.org/10.1007/s11947-011-0538-2]
[70]
Bonet A, Caballero P, Gomez M, Rosell C. Microbial transglutaminase as a tool to restore the functionality of gluten from insect-damaged wheat. Cereal Chem 2005; 82(4): 425-30.
[http://dx.doi.org/10.1094/CC-82-0425]
[71]
Köksel H, Sivri D, Ng P, Steffe J. Effects of transglutaminase enzyme on fundamental rheological properties of sound and bug-damaged wheat flour doughs. Cereal Chem 2001; 78(1): 26-30.
[http://dx.doi.org/10.1094/CCHEM.2001.78.1.26]
[72]
Ribotta PD, Pérez GT, Añón MC, León AE. Optimization of additive combination for improved soy–wheat bread quality. Food Bioprocess Technol 2010; 3(3): 395-405.
[http://dx.doi.org/10.1007/s11947-008-0080-z]
[73]
Schoenlechner R, Szatmari M, Bagdi A, Tömösközi S. Optimisation of bread quality produced from wheat and proso millet (Panicum miliaceum L.) by adding emulsifiers, transglutaminase and xylanase. Food Sci Tech 2013; 51(1): 361-6.
[http://dx.doi.org/10.1016/j.lwt.2012.10.020]
[74]
Roccia P, Ribotta PD, Ferrero C, Pérez GT, León AE. Enzymes action on wheat–soy dough properties and bread quality. Food Bioprocess Technol 2012; 5(4): 1255-64.
[http://dx.doi.org/10.1007/s11947-010-0396-3]
[75]
Pourmohammadi K, Mohammad Bagher Hashemi S, Mousavi Khaneghah A, Alami M, Shahedi M, Sadeghi Mahoonak A, et al. Effect of microbial transglutaminase on protein electrophoretic pattern and solubility of wheat flour and hull-less barley flour blends. Curr Nutr Food Sci 2016; 12(4): 304-9.
[http://dx.doi.org/10.2174/1573401312666160909162441]

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