Effect of Transglutaminase Cross Linking on the Functional Properties as a Function of NaCl Concentration of Legumes Protein Isolate
The effect of cross linking of the protein isolates of
three legumes with the microbial enzyme transglutaminase (EC
2.3.2.13) on the functional properties at different NaCl concentration
was studied. The reduction in the total free amino groups (OD340) of
the polymerized protein showed that TGase treatment cross-linking
the protein subunit of each legume. The solubility of the protein
polymer of each legume was greatly improved at high concentration
of NaCl. At 1.2 M NaCl the solubility of the native legumes protein
was significantly decreased but after polymerization slightly
improved. Cross linked proteins were less turbid on heating to higher
temperature as compared to native proteins and the temperature at
which the protein turns turbid also increased in the polymerized
proteins. The emulsifying and foaming properties of the protein
polymer were greatly improved at all concentrations of NaCl for all
legumes.
[1] Adebowale, K. O., and Lawal, O. S. (2003). Foaming, gelation and
electrophoretic characteristics of mucuna bean (Mucuna pruriens)
protein concentrates. Food Chemistry, 83, 237-246.
[2] Onweluzo, J. C., Obanu, Z. A., and Onuoha, K. C. (1994). Functional
properties of some lesser known tropical legumes. Journal of Food
Science and Technology, 31, 302-306
[3] Motoki, M., and Seguro, K. (1998). Transglutaminase and its use for
food processing. Trends in Food Science and Technology, 9, 204-210
[4] Kuraishi, C., Yamazaki, K., & Susa, Y. (2001). Transglutaminase: its
utilization in the food industry. Food Reviews International, 17, 221-
246.
[5] Lorenzen, P. C. (2000). Techno-functional properties of
transglutaminase- treated milk proteins. Milchwissenschaft, 55, 667-670
[6] Gerrard, G. A. (2002). Protein-protein crosslinking in food: Methods,
consequences, applications. Trends in Food Science and Technology, 13,
391-399.
[7] Singh, H. (1991). Modification of food proteins by covalent cross
linking. Trends in Food Science and Technology, 2, 196-200.
[8] Iwabuchi, S., & Yamauchi, F. (1987). Determination of glycinin and
conglycinin in soy proteins by immunological methods. Journal of
Agriculture and Food Chemistry, 35, 200-205.
[9] Kato, A., Shimokawa, K., & Kobayashi, K. (1991). Improvement of the
functional properties of insoluble gluten by pronase digestion followed
by dextran conjuagation. Journal of Agriculture and Food Chemistry,
39, 1053-1056.
[10] Church, F. C., Swaisgood, H. E., Porter, D. H., & Catignani, G. L.
(1983). Spectrophotometric assay using o-phthaldialdehyde for
determination of proteolysis in milk and isolated milk proteins. Journal
of Dairy Science, 66, 1219-1227.
[11] Kato, Y., Aoki, T., Kato, N., Nakamura, R., & Matsuda, T. (1995).
Modification of ovalbumin with glucose 6-phosphate by amino-carbonyl
reaction. Improvement of protein heat stability and emulsifying activity.
Journal of Agriculture and Food Chemistry, 43, 301-305.
[12] Pearce, K. N., & Kinsella, J. E. (1978). Emulsifying properties of
proteins: Evaluation of a turbidimetric technique. Journal of Agriculture
and Food Chemistry, 26, 716-723.
[13] Lawhon, J.T., Cater, C.M. and Mattil, K.F. (1972). A comparative study
of the whipping potential of an extract from several oilseed flours.
Cereal Science, 17, 240-244.
[14] Ahmed, E.A. and Schmidt, R.H. (1979). Functional properties of peanut
and soybean proteins as influenced by processing method. Peanut
Science, 6, 1-6.
[15] Sakamoto, H., Kumazawa, Y., Toiguchi, S., Serguro, K., Soedo, T., &
Motoki, M. (1995). Gel strength enhancement by addition microbial
transglutaminase during onshore surimi manufacture. Journal of Food
Science, 60, 300-304.
[16] Sergo, K., Kumazawa, Y., Ohtsuka, T., Toiguchi, S., & Motoki, M.
(1995). Microbial transglutaminase and e-(c-Glutamyl) lysine crosslinks:
Effects on elastic properties of Kamaboko gels. Journal of Food Science,
60, 305-311.
[17] Babiker E. E. (2000). Effect of transglutaminase treatment on the
functional properties of native and chymotrypsin-digested soy protein.
Food Chemistry, 70, 139-145.
[18] Hassan A. B., Osman G. A., Babiker E. E. (2007). Effect of
chymotrypsin digestion followed by polysaccharide conjugation or
transglutaminase treatment on functional properties of millet proteins.
Food Chemistry, 102, 257-262.
[19] Aluko, R. E. and Yada, R. Y. (1993). Relationship of hydrophobicity
and solubility with some functional properties of cowpea (Vigna
unguiculuta) protein isolate. J. Sci. Food Agric., 62, 33 1-5.
[20] Nai, C. S., Ching, Y. M., Wai, Y. M., and Yoshinori, M. (2002).
Functional properties of oat globulin modified by a calcium-independent
microbial transglutaminase. Journal of Agricultural Food Chemistry,
50, 2666-2672.
[21] Flanagan J., Gunning Y., FitzGerald, R.J. (2003). Effect of cross-linking
with transglutaminase on the heat stability and some functional
characteristics of sodium caseinate. Food Research International, 36,
267-274.
[22] Olayide S. L. (2004). Functionality of African locust bean (Parkia
biglobossa) protein isolate: effects of pH, ionic strength and various
protein concentrations. Food Chemistry 86 (2004) 345-355.
[23] Aluko, R. E., and Yada, R. Y. (1995). Some functional properties of a
cowpea (Vigna unguiculata) globulin isolate treated with
transglutaminase. Bioscience Biotechnology Biochemistry, 59, 2298-
2299.
[24] Akintayo, E. T., Oshodi, A. A., and Esuoso, K. O. (1999). Effects of
NaCl, ionic strength and pH on the foaming and gelation of pigeon pea
(Cajanus cajan) protein concentrates. Food Chemistry, 66, 51-56.
[1] Adebowale, K. O., and Lawal, O. S. (2003). Foaming, gelation and
electrophoretic characteristics of mucuna bean (Mucuna pruriens)
protein concentrates. Food Chemistry, 83, 237-246.
[2] Onweluzo, J. C., Obanu, Z. A., and Onuoha, K. C. (1994). Functional
properties of some lesser known tropical legumes. Journal of Food
Science and Technology, 31, 302-306
[3] Motoki, M., and Seguro, K. (1998). Transglutaminase and its use for
food processing. Trends in Food Science and Technology, 9, 204-210
[4] Kuraishi, C., Yamazaki, K., & Susa, Y. (2001). Transglutaminase: its
utilization in the food industry. Food Reviews International, 17, 221-
246.
[5] Lorenzen, P. C. (2000). Techno-functional properties of
transglutaminase- treated milk proteins. Milchwissenschaft, 55, 667-670
[6] Gerrard, G. A. (2002). Protein-protein crosslinking in food: Methods,
consequences, applications. Trends in Food Science and Technology, 13,
391-399.
[7] Singh, H. (1991). Modification of food proteins by covalent cross
linking. Trends in Food Science and Technology, 2, 196-200.
[8] Iwabuchi, S., & Yamauchi, F. (1987). Determination of glycinin and
conglycinin in soy proteins by immunological methods. Journal of
Agriculture and Food Chemistry, 35, 200-205.
[9] Kato, A., Shimokawa, K., & Kobayashi, K. (1991). Improvement of the
functional properties of insoluble gluten by pronase digestion followed
by dextran conjuagation. Journal of Agriculture and Food Chemistry,
39, 1053-1056.
[10] Church, F. C., Swaisgood, H. E., Porter, D. H., & Catignani, G. L.
(1983). Spectrophotometric assay using o-phthaldialdehyde for
determination of proteolysis in milk and isolated milk proteins. Journal
of Dairy Science, 66, 1219-1227.
[11] Kato, Y., Aoki, T., Kato, N., Nakamura, R., & Matsuda, T. (1995).
Modification of ovalbumin with glucose 6-phosphate by amino-carbonyl
reaction. Improvement of protein heat stability and emulsifying activity.
Journal of Agriculture and Food Chemistry, 43, 301-305.
[12] Pearce, K. N., & Kinsella, J. E. (1978). Emulsifying properties of
proteins: Evaluation of a turbidimetric technique. Journal of Agriculture
and Food Chemistry, 26, 716-723.
[13] Lawhon, J.T., Cater, C.M. and Mattil, K.F. (1972). A comparative study
of the whipping potential of an extract from several oilseed flours.
Cereal Science, 17, 240-244.
[14] Ahmed, E.A. and Schmidt, R.H. (1979). Functional properties of peanut
and soybean proteins as influenced by processing method. Peanut
Science, 6, 1-6.
[15] Sakamoto, H., Kumazawa, Y., Toiguchi, S., Serguro, K., Soedo, T., &
Motoki, M. (1995). Gel strength enhancement by addition microbial
transglutaminase during onshore surimi manufacture. Journal of Food
Science, 60, 300-304.
[16] Sergo, K., Kumazawa, Y., Ohtsuka, T., Toiguchi, S., & Motoki, M.
(1995). Microbial transglutaminase and e-(c-Glutamyl) lysine crosslinks:
Effects on elastic properties of Kamaboko gels. Journal of Food Science,
60, 305-311.
[17] Babiker E. E. (2000). Effect of transglutaminase treatment on the
functional properties of native and chymotrypsin-digested soy protein.
Food Chemistry, 70, 139-145.
[18] Hassan A. B., Osman G. A., Babiker E. E. (2007). Effect of
chymotrypsin digestion followed by polysaccharide conjugation or
transglutaminase treatment on functional properties of millet proteins.
Food Chemistry, 102, 257-262.
[19] Aluko, R. E. and Yada, R. Y. (1993). Relationship of hydrophobicity
and solubility with some functional properties of cowpea (Vigna
unguiculuta) protein isolate. J. Sci. Food Agric., 62, 33 1-5.
[20] Nai, C. S., Ching, Y. M., Wai, Y. M., and Yoshinori, M. (2002).
Functional properties of oat globulin modified by a calcium-independent
microbial transglutaminase. Journal of Agricultural Food Chemistry,
50, 2666-2672.
[21] Flanagan J., Gunning Y., FitzGerald, R.J. (2003). Effect of cross-linking
with transglutaminase on the heat stability and some functional
characteristics of sodium caseinate. Food Research International, 36,
267-274.
[22] Olayide S. L. (2004). Functionality of African locust bean (Parkia
biglobossa) protein isolate: effects of pH, ionic strength and various
protein concentrations. Food Chemistry 86 (2004) 345-355.
[23] Aluko, R. E., and Yada, R. Y. (1995). Some functional properties of a
cowpea (Vigna unguiculata) globulin isolate treated with
transglutaminase. Bioscience Biotechnology Biochemistry, 59, 2298-
2299.
[24] Akintayo, E. T., Oshodi, A. A., and Esuoso, K. O. (1999). Effects of
NaCl, ionic strength and pH on the foaming and gelation of pigeon pea
(Cajanus cajan) protein concentrates. Food Chemistry, 66, 51-56.
@article{"International Journal of Biological, Life and Agricultural Sciences:63572", author = "Nahid A. Ali and Salma H. Ahmed and ElShazali A. Mohamed and Isam A. Mohamed Ahmed and Elfadil E.Babiker", title = "Effect of Transglutaminase Cross Linking on the Functional Properties as a Function of NaCl Concentration of Legumes Protein Isolate", abstract = "The effect of cross linking of the protein isolates of
three legumes with the microbial enzyme transglutaminase (EC
2.3.2.13) on the functional properties at different NaCl concentration
was studied. The reduction in the total free amino groups (OD340) of
the polymerized protein showed that TGase treatment cross-linking
the protein subunit of each legume. The solubility of the protein
polymer of each legume was greatly improved at high concentration
of NaCl. At 1.2 M NaCl the solubility of the native legumes protein
was significantly decreased but after polymerization slightly
improved. Cross linked proteins were less turbid on heating to higher
temperature as compared to native proteins and the temperature at
which the protein turns turbid also increased in the polymerized
proteins. The emulsifying and foaming properties of the protein
polymer were greatly improved at all concentrations of NaCl for all
legumes.", keywords = "Functional properties, Legumes, Protein isolate,NaCl, Transglutaminase.", volume = "4", number = "1", pages = "131-6", }
