References
- Kato A, Nakamura S, Takasaki H, Maki, S. New functional properties of glycosylated lysozymes constructed by chemical and genetic modifications. pp. 243-256. In: Macromolecular Interactions in Food Technology. Parris N, Kato A, Creamer L, Pearce J (eds). ACS Symposium Series 650, American Chemical Society, USA (1996)
- Ibrahim HR, Kato A. Design of amphipathic lysozyme using chemical and genetic modifications to achieve optimal food functionality and diverse antimicrobial action. pp. 16-28. In: Food Proteins-Structure and Functionality. Schwenke KD, Mothes R (eds). VCH, New York, NY, USA (1993)
- Alexandre MC, Larre C, Viroben G, Popineau Y, Guegen J. Modification of a wheat gliadin by bovine plasma factor XIII. pp. 172-179. In: Food Proteins. Structure and Functionality. Shwenke KD, Mothes R (eds). VCH, Weinheim, Germany (1993)
- Damodaran S. Protein-stabilized foam and emulsions. pp 57 -110. In: Food Proteins and Their Applications. Damodaran S, Paraf A. (eds). Dekker, New York, NY, USA (1997)
- Ikura K, Kometani T, Sasaki R, Chiba H. Crosslinking of soybean 7S and 11S proteins by transglutaminase. Agric. Biol. Chem. 44: 2979-2984 (1980) https://doi.org/10.1271/bbb1961.44.2979
- Ikura K, Yoshikawa M, Sasaki R, Chiba H. Incorporation of amino acids into food proteins by trans glutaminase. Agric. Biol. Chem. 45: 2587-2592 (1981) https://doi.org/10.1271/bbb1961.45.2587
- Motoki M, Nio N. Crosslinking between different food proteins by transglutaminase. J. Food Sci. 48: 2587-2592 (1981)
- Nio N, Motoki M, Takinami K. Gelation mechanism of protein solution by trans glutaminase. Agric. Biol, Chem. 50: 851-855 (1986) https://doi.org/10.1271/bbb1961.50.851
- Traore F, Meunier JC. Cross-linking activity of placental F XIIIa on whey proteins and caseins. J. Agric. Food Chem. 40: 399-402 (1992) https://doi.org/10.1021/jf00015a007
- Folk JE, Chung SI. Molecular and catalytic properties of transglutaminase. Adv. Enzymol. 38: 109-191 (1973)
-
Lee DS, Matsumoto S, Matsumura Y, Mori T. Identification of the
${\epsilon}$ -(${\gamma}$ -glutamyl)lysine cross-linking sites in a-lactalbumin polymerized by mammalian and microbial transglutaminases. J. Agric. Food Chem. 50: 7412-7419 (2002) https://doi.org/10.1021/jf020529a - Ando H, Adachi M, Umeda K, Matsuura A, Nonaka M, Uchio R, Tanaka H, Motoki M. Purification and characteristics of a novel trans glutaminase derived from Microorganisms. Agric. Biol. Chem. 53: 2613-2617 (1989) https://doi.org/10.1271/bbb1961.53.2613
-
Faergemand M, Qtte J, Qvist KB. Enzymatic cross-linking of whey proteins by a
$Ca^{2+}$ -independent microbial transglutaminase from Streptomyces lydicus. Food Hydrocoll 11: 19-25 (1997) https://doi.org/10.1016/S0268-005X(97)80006-9 -
Matsumura Y, Lee DS, Mori T. Molecular weight distributions of
${\alpha}$ -lactalbumin polymers formed by mammalian and microbial transglutaminases. Food Hydrocoll 14: 49-59 (2000) https://doi.org/10.1016/S0268-005X(99)00045-4 -
Nonaka M, Tanaka H, Okiyama A, Motoki M, Ando H, Umeda K, Matsuura A. Polymerization of several proteins by
$Ca^{2+}$ -independent trans glutaminase derived from microorganisms. Agric. Biol. Chem. 53: 2619-2623 (1989) https://doi.org/10.1271/bbb1961.53.2619 - Sakamoto H, Kumazawa Y, Motoki M. Strength of protein gels prepared with microbial transglutarninase related to reaction conditions. J. Food Sci. 59, 866-871 (1994) https://doi.org/10.1111/j.1365-2621.1994.tb08146.x
- Kuraishi C, Sakamoto J, Soeda T. The usefulness of transglutarninase for food processing. pp 29-38. In: Biotechnology for Improved and Flavors. Kuraishi C, Soeda T (eds). American Chemical Society, Washington, DC, USA (1996)
-
Kumazawa Y, Sakamoto H, Kawauiri H, Motoki M. Determiantion of
${\epsilon}$ -(${\gamma}$ -glutamyl)lysine in several fish eggs and muscle proteins. Fish. Sci. 62: 331-332 (1995) - Motoki M, Seguro K. Transglutaminase and its use for food processing. Food Sci. Technol. 9: 204-210 (1998) https://doi.org/10.1016/S0924-2244(98)00038-7
- Sakamoto H, Yamazaki K, Kaga C, Yamamoto Y, Ito R, Kurosawa Y Strength enhancement by addition of microbial transglutaminase during chinese noodle processing. Nippon Shokuhin Kagaku Kogaku Kaishi 43: 598-602 (1996) https://doi.org/10.3136/nskkk.43.598
- Han XQ, Damodaran S. Thermodynamic compatibility of substrate proteins affects their cross-linking by transglutaminase. J. Agric. Food Chem. 44: 1211-1217 (1996) https://doi.org/10.1021/jf950569x
- Lee DS, Matsumoto S, Hayashi Y, Matsumura Y, Mori T. Differences in physical and structural properties of heat-induced gels from glycinins among soybean cultivars, Food Sci. Technol. Res. 8: 360-366 (2002) https://doi.org/10.3136/fstr.8.360
- Thanh VH, Okubo K, Shibasaki K. Isolation and characterization of the multiple 7S globulins of soybean proteins. Plant Physiol. 56: 19-22 (1975) https://doi.org/10.1104/pp.56.1.19
- Folk JE. Methods in Enzymology. Vol. 17A, pp. 889-894. Tabor H, Tabor CW (eds). Academic Press, New York, NY, USA (1970)
- Lowry OH, Rosebrough NJ, Farr AL, Randall RJ. Protein measurement with the folin phenol reagent. J. Biol. Chem. 193: 265-275 (1951)
- Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685 (1970) https://doi.org/10.1038/227680a0
- Reddy SR, Fogler HS. Emulsion stability: Determination from turbidity. J. Colloid Interface Sci. 79: 101-104 (1981) https://doi.org/10.1016/0021-9797(81)90052-7
- Lee DS. Studies on mechanism of polymerization of food proteins by transglutaminases from mammalian and microbial origins. PhD thesis, Kyoto University, Kyoto, Japan (1997)
-
Liu M, Damodaran S. Effect of transglutarninase-catalyzed polymerization of
${\beta}$ -casein on its emulsifying properties. J. Agric. Food Chem. 47: 1514-1519 (1999) https://doi.org/10.1021/jf981030c - Liu M, Lee DS, Damodaran S. Emulsifying properties of acidic subunits of soy 11S globulin. J. Agric. Food Chem. 47: 4970-4975 (1999) https://doi.org/10.1021/jf9902200