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Gıda Endüstrisinde Transglutaminaz Uygulamaları: 1. Enzimin Genel Özellikleri

Yıl 2007, Cilt: 32 Sayı: 6, 287 - 292, 01.12.2007

Öz

Transglutaminaz enzimi (Tgaz); amin birleşmesi, çapraz bağ oluşumu ve deamidasyon tepkimeleri ile proteinleri modifiye edebilen bir enzimdir ( EC 2.3.2.13, protein-glutamin -glutamil-transferaz ). 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.

Kaynakça

  • Blanshard JMV, Mitchell JR. 1998. Food Structure- Its Creation and Evaluation, Buttenworths.
  • Aguilera JM. 1992. Generation of Engineered Structures in Gels, in Physical Chemistry of Foods (Schartzberg, H.G. and Hartel, R.W. eds), pp.387-421, Marcel Dekker
  • Schorsch C, Carrie H, Norton IT. 2000. Crosslinking Casein micelles by a Microbial Transglutaminase: Influence of Crosslinks in Acid-induced Gelation. International Dairy Journal, 10:529-539.
  • Phillips LG, Whitehead DM, Kinsella J. 1994. Structure-Function Properties of Food Proteins, Academic Press.
  • Matsumura Y, Moti T. 1996. Gelation, in Methods of Testing Protein Functionality (Hall, G.M., ed.), pp. 76-109, Blackie.
  • Clark AH, Ross-Murphy SB. 1987. Structural and Mechanical Properties of Biopolymer Gels. Adv. Polym. Sci., 83: 57- 192.
  • Doi E. 1993. Gels and Gelling of Globular Proteins. Trends Food Sci., Technol. 4: 1-5.
  • Messens W, Wan Camp J, Huyghebaert A. 1979. The Use of High Pressure to Modify the Functionality of Food Proteins. Trends Foods Sci. Technol., 8: 107-112.
  • Dickinson E, Mcclements DJ. 1995. Advances in Food Colloids, pp 27-80, Blackie.
  • 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 (Mitchell, J.R. and Ledward, D.A. eds), pp. 203-272, Elsevier.
  • 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. 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.
  • Motoki M, Seguro K. 1998. Transglutaminase and Its Use For Food Processing. Trends in Food Sci. and Technol., 9: 204-210.
  • Berbers GAM, Bentlage HGM, Brans AMM, Bloemendal H, Jong WW. 1983. b-crystallin: Endogenous substrate of Lens Transglutaminase. Eur. J. Biochem., 135: 315-320.
  • Wold F. 1985. Reactions of the Amid-side Chains of Glutamine and Asparagine In Vivo. Trends Biochem. Sci., 10: 4-6.
  • Nio N, Motoki M, Takinami K. 1986. Gelation Mechanism of Protein Solutions by Transglutminase. J. Agric, Biol. Chem., 48: 851-855.
  • Aboumahmoud R, Savello P. 1990. Crosslinking of whey Proteins by Transglutaminase. J. Dairy Sci., 73: 256-263.
  • Matsumura Y, Chanyonvorakul Y, Kumozawa Y, Othsuka T, Mori T. 1996. Enhance Susceptibility to Transglutaminase Reaction of a-lactalbumin in the Molten Globule State. Biochem. Biophys. Acta, 1292: 69-76.
  • Faergemand B, Murray BS, Dickinson E. 1997. Crosslinking of Milk Proteins With Transglutaminase At the Oil-Water Interface. J. Agric, Biol. Chem., 45: 2514-2519.
  • Hornyak TJ, Bishop PD, Shafer JA. 1989. a-Thrombincatalyzed activation of Human Platalet Factor XIIIa : Relationship Between Ptoteolysis and Favtor XIIIa Activity. Biochem., 28: 7329-7332.
  • Dickinson E. 1993. Towards Natural Emulsifiers. Trends Food Sci. Technol., 4: 330-334.
  • Wilson SA. 1992. Modified Milk Proteins via Enzymatic Crosslinking, Hamilton, Sep. 11, in Proc. of Meal Industry Research Institutes of New Zealand, Mirinz, 247-277.
  • Seguro K, Kumazawa Y, Ohtsuka T, Toiguchi S, Motoki M. 1995. Microbial Transglutaminase and e-(g-Glutamyl)Lysine Crosslink Effects on Elastic Properties of Kamaboko Gel. J. Food Sci., 60: 305-311.
  • Kurth L, Rogers PJ. 1984. Transglutaminase Catalyzed Crosslinking of Myosin to Soya Protein, Casein and Gluten. J. Food Sci., 49: 573 – 589.
  • Enzyme Nomenculature. 1992. Nomenculature Committee of the International Union of Biochemistry and Molecular Biology, p.201, Academic Press, inc.
  • Nonaka M, Matsuura Y, Nakano K, Motoki M. 1997. Improvement of the pH-Solubulity Profile of Sodium Caseinat by Using Ca2+ -Independent Microbial Transglutaminase with Gelatin. Food Hydrocolloids, 11: 347-349.
  • Nielsen PM. 1995. Reactions and Potential Industrial Applications of Transglutaminase. Review of Literature and Patents. Food Biotechnology, 9: 119-156.
  • 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.
  • 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.

Applications of Transglutaminase in Food Industry: 1: General Properties of the Enzyme (Turkish with English Abstract)

Yıl 2007, Cilt: 32 Sayı: 6, 287 - 292, 01.12.2007

Öz

Transglutaminase (Tgase) is an enzyme which catalyzes the reactions i.e. amin corporation, crosslinking and deamidation ( EC 2.3.2.13, protein-glutamine -glutamil-transferaz ). 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. 

Kaynakça

  • Blanshard JMV, Mitchell JR. 1998. Food Structure- Its Creation and Evaluation, Buttenworths.
  • Aguilera JM. 1992. Generation of Engineered Structures in Gels, in Physical Chemistry of Foods (Schartzberg, H.G. and Hartel, R.W. eds), pp.387-421, Marcel Dekker
  • Schorsch C, Carrie H, Norton IT. 2000. Crosslinking Casein micelles by a Microbial Transglutaminase: Influence of Crosslinks in Acid-induced Gelation. International Dairy Journal, 10:529-539.
  • Phillips LG, Whitehead DM, Kinsella J. 1994. Structure-Function Properties of Food Proteins, Academic Press.
  • Matsumura Y, Moti T. 1996. Gelation, in Methods of Testing Protein Functionality (Hall, G.M., ed.), pp. 76-109, Blackie.
  • Clark AH, Ross-Murphy SB. 1987. Structural and Mechanical Properties of Biopolymer Gels. Adv. Polym. Sci., 83: 57- 192.
  • Doi E. 1993. Gels and Gelling of Globular Proteins. Trends Food Sci., Technol. 4: 1-5.
  • Messens W, Wan Camp J, Huyghebaert A. 1979. The Use of High Pressure to Modify the Functionality of Food Proteins. Trends Foods Sci. Technol., 8: 107-112.
  • Dickinson E, Mcclements DJ. 1995. Advances in Food Colloids, pp 27-80, Blackie.
  • 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 (Mitchell, J.R. and Ledward, D.A. eds), pp. 203-272, Elsevier.
  • 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. 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.
  • Motoki M, Seguro K. 1998. Transglutaminase and Its Use For Food Processing. Trends in Food Sci. and Technol., 9: 204-210.
  • Berbers GAM, Bentlage HGM, Brans AMM, Bloemendal H, Jong WW. 1983. b-crystallin: Endogenous substrate of Lens Transglutaminase. Eur. J. Biochem., 135: 315-320.
  • Wold F. 1985. Reactions of the Amid-side Chains of Glutamine and Asparagine In Vivo. Trends Biochem. Sci., 10: 4-6.
  • Nio N, Motoki M, Takinami K. 1986. Gelation Mechanism of Protein Solutions by Transglutminase. J. Agric, Biol. Chem., 48: 851-855.
  • Aboumahmoud R, Savello P. 1990. Crosslinking of whey Proteins by Transglutaminase. J. Dairy Sci., 73: 256-263.
  • Matsumura Y, Chanyonvorakul Y, Kumozawa Y, Othsuka T, Mori T. 1996. Enhance Susceptibility to Transglutaminase Reaction of a-lactalbumin in the Molten Globule State. Biochem. Biophys. Acta, 1292: 69-76.
  • Faergemand B, Murray BS, Dickinson E. 1997. Crosslinking of Milk Proteins With Transglutaminase At the Oil-Water Interface. J. Agric, Biol. Chem., 45: 2514-2519.
  • Hornyak TJ, Bishop PD, Shafer JA. 1989. a-Thrombincatalyzed activation of Human Platalet Factor XIIIa : Relationship Between Ptoteolysis and Favtor XIIIa Activity. Biochem., 28: 7329-7332.
  • Dickinson E. 1993. Towards Natural Emulsifiers. Trends Food Sci. Technol., 4: 330-334.
  • Wilson SA. 1992. Modified Milk Proteins via Enzymatic Crosslinking, Hamilton, Sep. 11, in Proc. of Meal Industry Research Institutes of New Zealand, Mirinz, 247-277.
  • Seguro K, Kumazawa Y, Ohtsuka T, Toiguchi S, Motoki M. 1995. Microbial Transglutaminase and e-(g-Glutamyl)Lysine Crosslink Effects on Elastic Properties of Kamaboko Gel. J. Food Sci., 60: 305-311.
  • Kurth L, Rogers PJ. 1984. Transglutaminase Catalyzed Crosslinking of Myosin to Soya Protein, Casein and Gluten. J. Food Sci., 49: 573 – 589.
  • Enzyme Nomenculature. 1992. Nomenculature Committee of the International Union of Biochemistry and Molecular Biology, p.201, Academic Press, inc.
  • Nonaka M, Matsuura Y, Nakano K, Motoki M. 1997. Improvement of the pH-Solubulity Profile of Sodium Caseinat by Using Ca2+ -Independent Microbial Transglutaminase with Gelatin. Food Hydrocolloids, 11: 347-349.
  • Nielsen PM. 1995. Reactions and Potential Industrial Applications of Transglutaminase. Review of Literature and Patents. Food Biotechnology, 9: 119-156.
  • 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.
  • 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.
Toplam 31 adet kaynakça vardır.

Ayrıntılar

Birincil Dil Türkçe
Bölüm Makaleler
Yazarlar

Zerrin Yüksel Bu kişi benim

Yaşar Kemal Erdem Bu kişi benim

Yayımlanma Tarihi 1 Aralık 2007
Yayımlandığı Sayı Yıl 2007 Cilt: 32 Sayı: 6

Kaynak Göster

APA Yüksel, Z. ., & Erdem, Y. K. . (2007). Gıda Endüstrisinde Transglutaminaz Uygulamaları: 1. Enzimin Genel Özellikleri. Gıda, 32(6), 287-292.
AMA Yüksel Z, Erdem YK. Gıda Endüstrisinde Transglutaminaz Uygulamaları: 1. Enzimin Genel Özellikleri. GIDA. Aralık 2007;32(6):287-292.
Chicago Yüksel, Zerrin, ve Yaşar Kemal Erdem. “Gıda Endüstrisinde Transglutaminaz Uygulamaları: 1. Enzimin Genel Özellikleri”. Gıda 32, sy. 6 (Aralık 2007): 287-92.
EndNote Yüksel Z, Erdem YK (01 Aralık 2007) Gıda Endüstrisinde Transglutaminaz Uygulamaları: 1. Enzimin Genel Özellikleri. Gıda 32 6 287–292.
IEEE Z. . Yüksel ve Y. K. . Erdem, “Gıda Endüstrisinde Transglutaminaz Uygulamaları: 1. Enzimin Genel Özellikleri”, GIDA, c. 32, sy. 6, ss. 287–292, 2007.
ISNAD Yüksel, Zerrin - Erdem, Yaşar Kemal. “Gıda Endüstrisinde Transglutaminaz Uygulamaları: 1. Enzimin Genel Özellikleri”. Gıda 32/6 (Aralık 2007), 287-292.
JAMA Yüksel Z, Erdem YK. Gıda Endüstrisinde Transglutaminaz Uygulamaları: 1. Enzimin Genel Özellikleri. GIDA. 2007;32:287–292.
MLA Yüksel, Zerrin ve Yaşar Kemal Erdem. “Gıda Endüstrisinde Transglutaminaz Uygulamaları: 1. Enzimin Genel Özellikleri”. Gıda, c. 32, sy. 6, 2007, ss. 287-92.
Vancouver Yüksel Z, Erdem YK. Gıda Endüstrisinde Transglutaminaz Uygulamaları: 1. Enzimin Genel Özellikleri. GIDA. 2007;32(6):287-92.

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