Applications of Transglutaminase in Food Industry: 2. Possible Usage of the Enzyme in the Food Processes (Turkish with English Abstract)

Year 2008, Volume: 33 Issue: 3, 143 - 149, 01.06.2008

Zerrin Yüksel Yaşar Kemal Erdem

Abstract

The modification of food proteins by transglutaminase (tgase) which catalyzes the crosslinkings between Gln and Lys has recently become a great interest to food scientists. The gel formation in dilute protein dispersions or solutions, improvement of the mechanical strength, physical texture formation in dilute oil-protein dispersions, the corporation of aminoacids which were lack in the structure to the proteins, prevent the textural deformations, reducing the usage of the food additives will be possible with usage of tgase.

Keywords

Transglutaminase, food, protein, crosslinking, texture, functionality, additives

Gıda Endüstrisinde Transglutaminaz Uygulamaları: 2. Enzimin Gıda Süreçlerinde Kullanım Olanakları

Abstract

Transglutaminaz enzimi (Tgaz), protein zincirindeki Gln ile Lys arasında gerçekleştirdiği çapraz bağlanmalar ile neden olduğu protein modifikasyonu gıda bilimcilerinin son dönemde gündemine oturmuş durumdadır. Tgaz kullanımıyla gıda işleme teknolojisinde, düşük viskoziteli protein çözelti ve/veya dispersiyonlarında jel yapı oluşturma, mekanik dayanımı artırma, düşük yağ – protein içeriğinde mekanik yapı oluşturma, var olan yapıya eksikliği duyulan amino asit katılımını sağlama, tekstürel deformasyonu ve gıda katkı maddeleri kulanımını azaltma veya tamamen ortadan kaldırma olasıdır.

Keywords

Transglutaminaz, gıda, protein, çaprazbağlanma, tekstür, fonksiyonellik, katkı maddeleri

References

• Sakamoto H, Kumazawa Y, Kawajiri H, Motoki M. 1995. e-(g-glutamyl)lysine crosslink Distribution in Foods as Determined by Improved Method. J. Food Sci., 60: 416-419.
• Kuraishi C, Sakamoto J, Yamazaki K, Susa Y, Kuhara C, Soeda T. 1997. Production of restructured meat using microbial transglutaminase without salt or cooking. Journal of Food Science, 62:(3) 488-490, 515.
• Motoki M, Seguro K. 1998. Transglutaminase and Its Use For Food Processing. Trends in Food Sci. and Technol., 9: 204-210.
• Nielsen GS, Petersen BR, Moller AJ. 1995. Impact of salt, phosphate and temperature on the effect of a Transglutaminase (F XIIIa) on the texture of restructure meat. Meat Science, 41:(3) 293-299.
• Pietrasik Z, Li-Chan ECY. 2002. Binding and textural properties of beef gels as affected by protein, k-carrageenan and microbial transglutaminase addition. Food Research International, 35: 91-98.
• Tseng TF, Liu DC, Chen MT. 2000. Evaluation of transglutaminase on the quality of low-salt chicken meat-balls. Meat Science, 55:427-431.
• Zhu Y, Rinzema A, Tramper J, Bol J. 1995. Microbial Transglutaminase-A Review of Its Production and Application in Food Processing. Appl. Microbiol Biotechnol., 44: 277-282.
• Sakamoto H, Kumazawa Y, Motoki M. 1994. Strength of Protein gels Prepared with Microbial Transglutaminase as Related to Reaction Conditions. J. Food Sci., 59: 866 – 871.
• Muguruma M, Tsuruoka K, Katayama K, Erwanto Y, Kawahara S, Yamauchi K, Sathe SK, Soeda T. 2003. Soybean and milk proteins modified by transglutaminase improves chicken sausage texture even at reduced levels of phosphate. Meat Science, 63: 191-197.
• Kuraishi C, Sakamoto J, Soeda T. 1996. USA. The usefulness of transglutaminase for food processing. Biotechnology for Improved Foods and Flavor.Edited by: Takeoka, G., ACS Symposium Series Chapter, 3, 29-38.
• Kılıç B. 2002. Effect of microbial transglutaminase and sodium caseinate on quality of chicken döner kebab. Meat Science, 61:120-126.
• Matsumura Y, Moti T. 1996. ‘Gelation’ in Methods of Testing Protein Functionality (Hall, G.M., ed.), pp. 76-109.
• Cristensen BM, Sorensen ES, Hojrup P, Petersen TE, Ramussen LK. 1996. Localization of Transglutaminase Crosslinking sites in bovine Caseins. J. Agric. Food Chem., 44: 1943-1947.
• Faegermand M, Quvist KB. 1997. Transglutaminase: effect on rheological properties, microstructure and permeability of set style acid milk gel. Food Hydrocolloids, 11: 287-292.
• Dickinson E, Yamato Y. 1996. Rheology of Milk Protein Gels and Protein – stabilized Emulsion Gels Crosslinked with Transglutaminase. J. Agric. Food Chem., 44: 1371 – 1377.
• Ikura K, Kometani T, Sasaki R, Chiba H. 1980 . Crosslinking of Soybean 7S and 11S Protein by Transglutaminase. Agric. Biol. Chem., 44: 2979 – 2984.
• Motoki M, Nio N. 1983. Crosslinking Between Different Food Proteins by Transglutaminase. J. Food Sci., 48: 561 – 566.
• Kurth L, Rogers PJ. 1984. Transglutaminase Catalyzed Crosslinking of Myosin to Soya Protein, Casein and Gluten. J. Food Sci., 49: 573 – 589.
• Hurrel RF, Carpenter KJ, Sinclair WJ, Otterburn MS, Asquith RS. 1976. Mechanisms of Heat Damage in Proteins. British J. Nutr., 35: 383-395.
• Seguro K, Kumazawa Y, Kuraishi C, Sakamoto H, Motoki M. 1996. The e-(g-glutamyl)lysine Moiety in Crosslinked Casein is an Available Source of Lysine For Rats. J. Nutr., 126: 2557-2562.
• Ikura K, Sasaki R, Motoki M. 1992. Use of Transglutaminase in Quality Improvement and processing of Food Proteins. Comments Agric. Food Chem., 2: 389-409.
• Koseki T, Kitabatake N, Doi E. 1989. Irreversible Thermal Denaturatıon and Formation of Linear Aggregates of Ovalbumin. Food Hydrocolloids, 3: 123-134.
• Clark AH, Lee Tuffnell DD. 1986. Gelation of Globular Proteins in Functional Properties of Food Macromolecules, JR Mitchell and DA Ledward (eds.), pp. 203-272.
• Dickinson E, Stainsby G. 1982. Colloids in Food, pp. 411-461, Applied Science, London, UK.
• Hamada JS. 1992. Modification of food Proteins by Enzymatic Methods, in Biochemistry of Food Proteins (Hudson, B.J.W., ed.), pp.249-270, Elsevier.
• Robinson DS. 1987. in Food: Biochemistry and Nutritional Value, pp.196-205, Longman.
• Folk JE, Finlayson JS. 1977. The e-(g-glutamyl)lysine Crosslink and the Catalytic role of Transglutaminase. Adv. Protein Chem., 31: 1-133.
• Berbers GAM, Bentlage HGM, Brans AMM, Bloemendal H, Jong WW. 1983. b-crystallin:Endogenous substrate of Lens Transglutaminase. Eur. J. Biochem., 135: 315-320.