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Study on a Binder by Using Porcine Blood Plasma Transglutaminase, Thrombin and Fibrinogen
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 Title & Authors
Study on a Binder by Using Porcine Blood Plasma Transglutaminase, Thrombin and Fibrinogen
Tsai, Chong-Ming; Tseng, Tsai-Fuh; Yang, Jeng-Huh; Chen, Ming-Tsao;
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 Abstract
The purpose of this study was to prepare a binder containing porcine blood transglutaminase (TGase), thrombin and fibrinogen. Extracted TGase, thrombin and fibrinogen were used alone or mixed with different proportions of their volume (v/v/v) by nine combinations as follows were 0.5:1:15, 0.5:1:20, 0.5:1:25, 1:1:15, 1:1:20, 1:1:25, 1.5:1:15, 1.5:1:20 and 1.5:1:25, respectively. Five ml of each combination were mixed with 0.6 ml of 0.25 M calcium chloride before experiment. After storage at 4C for 0, 1, 2, 3, 4 and 5 weeks, enzyme activity, total plate count, pH value, and SDS-PAGE of TGase, thrombin and fibrinogen were tested and pH value, clotting time and gel strength of the nine combination binders were determined. The results showed that total plate count of thrombin and pH value of TGase were significantly higher (p<0.05) than in other treatments. SDS-PAGE results showed that purified TGase, thrombin and fibrinogen from porcine blood plasma compared with commercial products (Sigma) had the same band patterns and nine different combination binders had no significant effect. Enzymatic activity of TGase and thrombin decreased as storage time increased. Total plate count of TGase, thrombin and fibrinogen and clotting time of the binder increased as storage time increased. The higher amount of fibrinogen in combinations, the stronger the gel strength.
 Keywords
Porcine Blood Plasma;Transglutaminase;Thrombin;Fibrinogen and Binder;
 Language
English
 Cited by
 References
1.
Anbe, H. 1961. Japanese Handbook of hematology. (6-II) pp. 788- 791. Japan

2.
Ando, H., M. Ahachi, K. Umeda, A. Matsuura, M. Nonaka, R. Uchio, H. Tanaka and M. Motoki. 1989. Purification and characteristics of a novel transglutaminase derived from microorganisms. Agric. Biol. Chem. 53:2613-2617

3.
Binnie, C. G. and S. T. Lord. 1993. The fibrinogen sequences that interact with thrombin. Blood 81:3186-3192

4.
Chen, J. S. K. and K. Mehta. 1999. Tissue transglutaminase: an enzyme with a split personality. Int. J. Biochem. Cell Biol. 31:817-836 crossref(new window)

5.
Chung, S. I., M. S. Lewis and J. E. Folk. 1974. Relationships of the catalytic properties of human plasma and platelet transglutaminase (activates blood coagulation factor XIII) to their subunit structures. J. Biol. Chem. 249:940-950

6.
Divakavan, S. 1982. Animal blood processing and utilization. Central Leather Research Institute Madras India

7.
Fargemand, M., J. Otte and K. B. Qvist. 1998. Emulsifying properties of milk prtoeins cross-linked with microbial transglutaminase. Int. Dairy J. 8:715-723 crossref(new window)

8.
Folk, J. E. 1970. Transglutaminase. In "Method in Enzymology", (Ed. H. Tabor and C. W. Tabor), 17:889-894. Acadenic Press, New York crossref(new window)

9.
Folk, J. E. 1980. Transglutaminase. Ann. Rev. Biochem. 49:517- 531 crossref(new window)

10.
Gornall, A. G., C. J. Bardwill and M. M. David. 1949. Determination of serum proteins by means of the biuret reaction. J. Biol. Chem. 177:751-766

11.
Greenberg, C. S. and M. A. Shuman. 1982. The zymogen forms of blood coagulation factor XIII bind specifically to fibrinogen. J. Biol. Chem. 257:6069-6101

12.
Harding, H. W. J. and G. E. Rogers. 1972. Formation of the $\varepsilon$- (${\gamma}$- glutamyl) lysine cross- link in hair proteins. Investigation of transamidases in hair follicles. Biochemistry 11:2858-2862 crossref(new window)

13.
Herrick, S., O. Blanc-Brude, A. Gray and G. Laurent. 1999. Fibrinogen. Int. J. Biochem. Cell Biol. 31:741-746 crossref(new window)

14.
Huang, C. C. and T. Y. Wang. 1997. Effect of fresh and frozen chicken meat on the quality of restructured chicken steaks. J. Chin. Soc. Anim. Sci. 26:347-358

15.
Huang, H. J. 1987. Studies on the tested preparation of hemostat from porcine blood and its hemostating effect. Master Thesis. National Chung-Hsing University, Taichung, Taiwan

16.
Huang, H. J., D. C. Liu, H. L. Guo and M. T. Chen. 1992. Preparation of hemostat from porcine blood-study on properties of fibrinogen and thrombin. J. Chin. Soc. Anim. Sci. 21(2):203-211

17.
Imm, T. Y., P. Lian and C. M. Lee. 2000. Gelation and water binding properties of transglutaminase-treated skim milk powder. J. Food Sci. 65:200-205 crossref(new window)

18.
Kang, H. and Y. D. Cho. 1996. Purification and properties of transglutaminase from soybean (Glycine max) leaves. Biochem. Biophys. Res. Commun. 223:288-292 crossref(new window)

19.
Kuraishi, C., J. Sakamoto, K. Yamazaki, Y. Susa, C. Kuhara and T. Soeda. 1997. Production of restructured meat using microbial transglutaminase without salt or cooking. J. Food Sci. 62:488- 490,515 crossref(new window)

20.
Laemmli, U. K. 1970. Cleavage of structural protein during the assembly of the head of bacteriophage T4. Nature. 227:681

21.
Lee, C. C. 1991. Enzymatic modification on fish proteins to improve the gelation by transglutaminase. Master Thesis. National Ocean University, Keelung, Taiwan

22.
Lin, S. M. 1995. Isolation, purification and characterization of microbial transglutaminase and its application in surimi products. Master Thesis. National Ocean University. Keelung, Taiwan

23.
Liu, H. H. 1999. Study on separation of transglutaminase from blood and its application in preparation of meat products. Master Thesis. Tunghai University, Taichung, Taiwan

24.
Machovich, R. 1986. Choices among the possible reaction routes catalyzed by thrombin. Ann. N. Y. Acda. Sci. 485:170-183 crossref(new window)

25.
Motoki, M. and K. Seguro. 1994. Trends in Japanese soy protein research. Inform. 5:308-313

26.
Ninomi, R., S. Saido and U. Inada. 1984. Basal study on effective utilization of animal blood. In: Result report of supporting study on meat. pp. 296-301. Ido memorial financial group. Japan

27.
Nonaka, M., S. Toiguchi, H. Sakamoto, H. Kawajiri, T. Soeda and M. Motoki. 1994. Changes caused by microbial transglutaminase on physical properties of thermally induced soy protein gels. Food Hydrocolloids 8:1-8 crossref(new window)

28.
SAS. 1996. SAS User's Guide: Statistics. Cary, NC. SAS Institute

29.
Schwartz, M. L., S. V. Pizzo, R. L. Hill and P. A. Mckee. 1973. Human factor XIII from plasma and platelets. J. Biol. Chem. 248:1395-1407

30.
Tsai, M. H. 1987. Blood transfusion scopy. In: Clinical hematology. pp. 111-177. Yi Hsien Publishing Co

31.
Tseng, T. F. 1999. Purification and characteristics of transglutaminase and its application. Dissertation. National Chung-Hsing University. Taichung. Taiwan

32.
Tseng, T. F., D. C. Liu and M. T. Chen. 1999. Characteristics of transglutaminase derived from pig plasma. J. Agric. Assoc. China. 1(4):452-458

33.
Wijngaards, G. and E. J. C. Paardekooper. 1987. Preparation of a composite meat product by means of an enzymatically formed protein gel. In (Ed. P. S. Van Roon and J. H. Houben) Trends in Modern Meat Technology 2, Proceeding of the International Symposium, Den Dolder, Netherlands, 23-25 November, pp. 125-129, Wageningen: Pudoc

34.
Yeh, Y. W. 2000. Purification, biochemical character and application of transglutaminase from Streptoverticllium kentuckense CCRC 12429. Master Thesis. National Chung- Hsing University. Taichung. Taiwan