Functional properties of limited hydrolysed cross-linked casein-gelatin composites

International Journal of Food Science and Technology

Volumn 48, Issue 2, 2013, Pages 260-266

  Sheng, Wen Wen ^a   Zhao, Xin Huai ^a  

^a NORTHEAST AGRICULTURAL UNIVERSITY   (China)

Author keywords

Casein gelatin composite; Functional properties; Limited hydrolysis; Trypsin

Indexed keywords

APPARENT VISCOSITY; AQUEOUS DISPERSIONS; CASEINATE; DEGREE OF HYDROLYSIS; EMULSIFYING ACTIVITY INDICES; EMULSIFYING PROPERTY; EMULSION STABILITY; FUNCTIONAL PROPERTIES; IN-VITRO; LIMITED PROTEOLYSIS; LOSS MODULI; MICROBIAL TRANSGLUTAMINASE; OIL ABSORPTION CAPACITY; SDS-PAGE; SURFACE HYDROPHOBICITY; TRYPSIN;

BIOLOGICAL MATERIALS; CASEIN; EMULSIFICATION; HYDROPHOBICITY; PROTEOLYSIS; SOLUBILITY;

HYDROLYSIS;

BOVINAE;

EID: 84872397934     PISSN: 09505423     EISSN: 13652621     Source Type: Journal    
DOI: 10.1111/j.1365-2621.2012.03182.x     Document Type: Article

References (42)

1. Agyare, K.K., Addob, K. & Xiong, Y.L. (2009). Emulsifying and foaming properties of transglutaminase-treated wheat gluten hydrolysate as influenced by pH, temperature and salt. Food Hydrocolloids, 23, 72-81.
2. Arvanitoyannis, I., Nakayama, A. & Aiba, S. (1998a). Edible films made from hydroxypropyl starch and gelatin and plasticized by polyols and water. Carbohydrate Polymers, 36, 105-119.
3. Arvanitoyannis, I., Nakayama, A. & Aiba, S. (1998b). Chitosan and gelatin based edible films: state diagrams, mechanical and permeation properties. Carbohydrate Polymers, 37, 371-382.
4. Babiker, E.F.E., Fujisawa, N., Matsudomi, N. & Kato, A. (1996). Improvement in the functional properties of gluten by protease digestion or acid hydrolysis followed by microbial transglutaminase treatment. Journal of Agricultural and Food Chemistry, 44, 3746-3750.
5. Cazacu-Davidescu, L.M., Kostyra, H., Marciniak-Darmochwal, K. & Kostyra, E. (2005). Influence of non-enzymatic glycosylation (glycation) of pea (pisum sativum) albumins on their enzymatic hydrolysis. Journal of the Science of Food and Agriculture, 85, 948-954.
6. Chen, R.N., Ho, H.O. & Sheu, M.T. (2005). Characterization of collagen matrices crosslinked using microbial transglutaminase. Biomaterials, 26, 4229-4235.
7. Chobert, J.M., Sitohy, M.Z. & Whitaker, J.R. (1988). Solubility and emulsifying properties of caseins modified enzymatically by staphylococcus aureus V8 protease. Journal of Agricultural and Food Chemistry, 36, 220-224.
8. 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.
9. Duangmal, K. & Taluengphol, A. (2009). Effect of protein additives, sodium ascorbate, and microbial transglutaminase on the texture and colour of red tilapia surimi gel. International Journal of Food Science and Technology, 45, 48-55.
10. Gan, C.Y., Latiff, A.A., Cheng, L.H. & Easa, A.M. (2009). Gelling of microbial transglutaminase cross-linked soy protein in the presence of ribose and sucrose. Food Research International, 42, 1373-1380.
11. Gbogouri, G.A., Linder, M., Fanni, J. & Parmentier, M. (2004). Influence of hydrolysis degree on the functional properties of salmon byproducts hydrolysates. Journal of Food Science, 69, 615-622.
12. Griffin, M., Casadio, R. & Bergamini, C.M. (2002). Transglutaminases: nature′s biological glues. Biochemical Journal, 368, 377-396.
13. Guan, X., Yao, H.Y., Chen, Z.X., Shan, L. & Zhang, M.D. (2007). Some functional properties of oat bran protein concentrate modified by trypsin. Food Chemistry, 101, 163-170.
14. Hayakawa, S. & Nakai, S. (1985). Relationships of hydrophobicity and net charge to the solubility of milk and soy proteins. Journal of Food Science, 50, 486-491.
15. Hiller, B. & Lorenzen, P.C. (2009). Functional properties of milk proteins as affected by enzymatic oligomerisation. Food Research International, 42, 899-908.
16. IDF. (2001). Milk-Determination of Nitrogen Content-Part 1: Kjeldahl Method. IDF Standard 20-1. Brussels: International Dairy Federation.
17. Jiang, S.J. & Zhao, X.H. (2011). Transglutaminase-induced cross-linking and glucosamine conjugation of casein and some functional properties of the modified product. International Dairy Journal, 21, 198-205.
18. Kishimura, H., Tokuda, Y., Yabe, M., Klomklao, S., Benjakul, S. & Ando, S. (2007). Trypsins from the pyloric ceca of jacopever (Sebastes schlegelii) and elkhorn sculpin (Alcichthys alcicornis): isolation and characterization. Food Chemistry, 100, 1490-1495.
19. Klompong, V., Benjakul, S., Kantachote, D. & Shahidi, F. (2007). Antioxidative activity and functional properties of protein hydrolysate of yellow stripe trevally (Selaroides leptolepis) as influenced by the degree of hydrolysis and enzyme type. Food Chemistry, 102, 1317-1327.
20. Kong, X.Z., Zhou, H.M. & Qian, H.F. (2007). Enzymatic preparation and functional properties of wheat gluten hydrolysates. Food Chemistry, 101, 615-620.
21. Laemmli, U.K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685.
22. Lamsal, B.P., Jung, S. & Johnson, L.A. (2007). Rheological properties of soy protein hydrolysates obtained from limited enzymatic hydrolysis. LWT-Food Science and Technology, 40, 1215-1223.
23. Lin, M.J.Y., Humbert, E.S. & Sosulski, F.W. (1974). Certain functional properties of sunflower meal products. Journal of Food Science, 39, 368-370.
24. Liu, M.X. & Damodaran, S. (1999). Effect of transglutaminase-catalyzed polymerization of β-casein on its emulsifying properties. Journal of Agricultural and Food Chemistry, 47, 1514-1519.
25. Lowry, O.H., Rosebrough, N.J., Farr, A.L. & Randall, R.J. (1951). Protein measurement with the folin phenol reagent. Journal of Biological Chemistry, 193, 265-275.
26. Ma, C.Y. & Wood, D.F. (1987). Functional properties of oat proteins modified by acylation, trypsin hydrolysis or linoleate treatment. Journal of the American Oil Chemists′ Society, 64, 1726-1731.
27. Mannheim, A. & Cheryan, M. (1992). Enzyme-modified proteins from corn gluten meal: preparation and functional properties. Journal of American Oil Chemists' Society, 69, 1163-1169.
28. Monogioudi, E., Faccio, G., Lille, M., Poutanen, K., Buchert, J. & Mattinen, M.L. (2011). Effect of enzymatic cross-linking of β-casein on proteolysis by pepsin. Food Hydrocolloids, 25, 71-81.
29. Mutilangi, W.A.M., Panyam, D. & Kilara, A. (1996). Functional properties of hydrolysates from proteolysis of heat-denatured whey protein isolate. Journal of Food Science, 61, 270-275.
30. Panyam, D. & Kilara, A. (1996). Enhancing the functionality of food proteins by enzymatic modification. Trends in Food Science & Technology, 7, 120-125.
31. Pearce, K.N. & Kinsella, J.E. (1978). Emulsifying properties of proteins: evaluation of a turbidimetric technique. Journal of Agricultural and Food Chemistry, 26, 716-723.
32. Roos, N., Lorenzen, P.C., Sick, H., Schrezenmeir, J. & Schlimme, E. (2003). Cross-linking by transglutaminase changes neither the in vitro proteolysis nor the in vivo digestibility of caseinate. Kieler Milchwirtschaftliche Forschungsberichte, 55, 261-276.
33. Rozan, P., Lamghari, R., Linder, M. et al. (1997). In vivo and in vitro digestibility of soybean, lupine, and rapeseed meal proteins after various technological processes. Journal of Agricultural and Food Chemistry, 45, 1762-1769.
34. Tang, C.H., Li, L. & Yang, X.Q. (2006). Influence of transglutaminase-induced cross-linking on in vitro digestibility of soy protein isolate. Journal of Food Biochemistry, 30, 718-731.
35. Tsumura, K., Saito, T., Tsuge, K., Ashida, H., Kugimiya, W. & Inouye, K. (2005). Functional properties of soy protein hydrolysates obtained by selective proteolysis. LWT-Food Science and Technology, 38, 255-261.
36. Wang, J.S., Zhao, M.M., Yang, X.Q. & Jiang, Y.M. (2006). Improvement on functional properties of wheat gluten by enzymatic hydrolysis and ultrafiltration. Journal of Cereal Science, 44, 93-100.
37. Xiong, Y.L., Agyare, K.K. & Addo, K. (2008). Hydrolyzed wheat gluten suppresses transglutaminase-mediated gelation but improves emulsification of pork myofibrillar protein. Meat Science, 80, 535-544.
38. Yin, S.W., Tang, C.H., Cao, J.S., Hu, E.K., Wen, Q.B. & Yang, X.Q. (2008a). Effects of limited enzymatic hydrolysis with trypsin on the functional properties of hemp (Cannabis sativa L.) protein isolate. Food Chemistry, 106, 1004-1013.
39. Yin, S.W., Tang, C.H., Wen, Q.B., Yang, X.Q. & Li, L. (2008b). Functional properties and in vitro trypsin digestibility of red kidney bean (Phaseolus vulgaris L.) protein isolate: effect of high-pressure treatment. Food Chemistry, 110, 938-945.
40. Yust, M.M., Pedroche, J., Millán-Linares, M.C., Alcaide-Hidalgo, J.M. & Millán, F. (2010). Improvement of functional properties of chickpea proteins by hydrolysis with immobilised Alcalase. Food Chemistry, 122, 1212-1217.
41. Zhang, Y.N., Liu, N. & Zhao, X.H. (2011). A study on the preparation and some functional properties of a cross-linked casein-gelatin composite by a microbial transglutaminase. International Journal of Food Science and Technology, 46, 2641-2647.
42. Zhao, G.L., Liu, Y., Zhao, M.M., Ren, J.Y. & Yang, B. (2011). Enzymatic hydrolysis and their effects on conformational and functional properties of peanut protein isolate. Food Chemistry, 127, 1438-1443.