Functional Properties of Water-soluble Proteins from Silver Carp (Hypophthalmichthys molitrix) Conjugated with Five Different Kinds of Sugar

Food and Bioprocess Technology

Volumn 6, Issue 12, 2013, Pages 3596-3603

  You, Juan ^a   Luo, Yongkang ^a   Shen, Huixing ^a  

^a CHINA AGRICULTURAL UNIVERSITY   (China)

Author keywords

Functional properties; Maillard reaction; Silver carp; Sugars; Water soluble protein

Indexed keywords

EMULSIFYING PROPERTY; FUNCTIONAL PROPERTIES; MAILLARD REACTION; MAILLARD REACTION PRODUCTS; SILVER CARP; SODIUM DODECYL SULFATE-POLYACRYLAMIDE GEL ELECTROPHORESIS; SURFACE HYDROPHOBICITY; WATER SOLUBLE PROTEIN;

CHEMICAL REACTIONS; DEXTRAN; ELECTROPHORESIS; GLYCOSYLATION; PROTEINS; SILVER; SODIUM DODECYL SULFATE; SOLUBILITY; SUGARS;

WATERWORKS;

CYPRINIDAE; HYPOPHTHALMICHTHYS MOLITRIX; HYPOPHTHALMICHTHYS NOBILIS;

EID: 84886087284     PISSN: 19355130     EISSN: 19355149     Source Type: Journal    
DOI: 10.1007/s11947-012-1036-x     Document Type: Article

References (31)

1. Achouri, A., Boye, J. I., Yaylayan, V. A., & Yeboah, F. K. (2005). Functional properties of glycated soy 11S glycinin. Journal of Food Science, 70, C269-C274.
2. Bae, J. H., Yoon, S. H., & Lim, S. Y. (2011). Heavy metal contents and chemical compositions of Atlantic (Scomber scombrus), blue (Scomber australasicus), and chub (Scomber japonicus) mackerel muscles. Food Science and Biotechnology, 20, 709-714.
3. Balange, A. K., & Benjakul, S. (2010). Cross-linking activity of oxidised tannic acid towards mackerel muscle proteins as affected by protein types and setting temperatures. Food Chemistry, 120, 268-277.
4. Benjakul, S., Visessanguan, W., Thongkaew, C., & Tanaka, M. (2003). Comparative study on physiochemical changes of muscle proteins from some tropical fish during frozen storage. Food Research International, 36, 787-795.
5. Bourtoom, T., Chinnan, M. S., Jantawat, P., & Sanguandeekul, R. (2009). Recovery and characterization of proteins precipitated from surimi wash-water. LWT- Food Science and Technology, 42, 599-605.
6. Deng, Q., Wang, L., Wei, F., Xie, B., Huang, F., & Huang, W. (2011). Functional properties of protein isolates, globulin and albumin extracted from Ginkgo biloba seeds. Food Chemistry, 124, 1458-1465.
7. Enomoto, H., Li, C.-P., Morizane, K., Ibrahim, H. R., Sugimoto, Y., Ohki, S., et al. (2007). Glycation and phosphorylation of β-lactoglobulin by dry-heating: effect on protein structure and some properties. Journal of Agricultural and Food Chemistry, 55, 2392-2398.
8. Gratacós-Cubarsí, M., & Lametsch, R. (2008). Determination of changes in protein conformation caused by pH and temperature. Meat Science, 80, 545-549.
9. Gu, X., Campbell, L. J., & Euston, S. R. (2009). Influence of sugars on the characteristics of glucono-δ-lactone-induced soy protein isolate gels. Food Hydrocolloids, 23, 314-326.
10. Hu, X.-Z., Cheng, Y.-Q., Fan, J.-F., Lu, Z.-H., Yamaki, K., & Li, L.-T. (2010). Effects of drying method on physicochemical and functional properties of soy protein isolates. Journal of Food Processing and Preservation, 34, 520-540.
11. Jing, H., Yap, M., Wong, P. Y. Y., & Kitts, D. D. (2011). Comparison of physicochemical and antioxidant properties of fructose and inulin modified egg white proteins. Food and Bioprocess Technology, 4(8), 1489-1496.
12. Leelapongwattana, K., Benjakul, S., Visessanguan, W., & Howell, N. K. (2005). Physicochemical and biochemical changes during frozen storage of minced flesh of lizardfish (Saurida micropectoralis). Food Chemistry, 90, 141-150.
13. Liu, P., Huang, M., Song, S., Hayat, K., Zhang, X., Xia, S., et al. (2012a). Sensory characteristics and antioxidant activities of Maillard reaction products from soy protein hydrolysates with different molecular weight distribution. Food and Bioprocess Technology, 5(5), 1775-1789.
14. Liu, Y., Zhao, G., Zhao, M. M., Ren, J., & Yang, B. (2012b). Improvement of functional properties of peanut protein isolate by conjugation with dextran through Maillard reaction. Food Chemistry, 131, 901-906.
15. Nishimura, K., Murakoshi, M., Katayama, S., & Saeki, H. (2011). Antioxidant ability of chicken myofibrillar protein developed by glycosylation and changes in the solubility and thermal stability. Bioscience, Biotechnology, and Biochemistry, 75, 247-254.
16. Omana, D. A., Xu, Y., Moayedi, V., & Betti, M. (2010). Alkali-aided protein extraction from chicken dark meat: chemical and functional properties of recovered proteins. Process Biochemistry, 45, 375-381.
17. Pan, J. F., Shen, H. X., You, J., & Luo, Y. K. (2011). Changes in physiochemical properties of myofibrillar protein from silver carp (Hypophthalmichthys mollitrix) during heat treatment. Journal of Food Biochemistry, 35, 939-952.
18. Qi, J.-R., Yang, X.-Q., & Liao, J.-S. (2009). Improvement of functional properties of acid-precipitated soy protein by the attachment of dextran through Maillard reaction. International Journal of Food Science and Technology, 44, 2296-2302.
19. Saeki, H. (1997). Preparation of neoglycoprotein from carp myofibrillar protein by Maillard reaction with glucose: biochemical properties and emulsifying properties. Journal of Agriculture and Food Chemistry, 45, 680-684.
20. Saeki, H., & Inoue, K. (1997). Improved solubility of carp myofibrillar proteins in low ionic strength medium by glycosylation. Journal of Agriculture and Food Chemistry, 45, 3419-3422.
21. Sankar, T. V., & Ramachandran, A. (2005). Thermal stability of myofibrillar protein from Indian major carps. Journal of the Science of Food and Agriculture, 85, 563-568.
22. Sanmartín, E., Arboleya, J. C., Villamiel, M., & Moreno, F. J. (2009). Recent advances in the recovery and improvement of functional proteins from fish processing by-products: use of protein glycation as an alternative method. Comprehensive Reviews in Food Science and Food Safety, 8, 332-344.
23. Sun, Q., & Luo, Y. K. (2011). Effect of Maillard reaction conditions on radical scavenging activity of porcine haemoglobin hydrolysate-sugar model system. International Journal of Food Science and Technology, 46, 358-364.
24. Sun, Y., Hayakawa, S., Chuamanochan, M., Fujimoto, M., Innun, A., & Izumori, K. (2006). Antioxidant effects of Maillard reaction products obtained from ovalbumin and different D-aldohexoses. Bioscience, Biotechnology, and Biochemistry, 70, 598-605.
25. Takeda, H., Iida, T., Okada, A., Ootsuka, H., Ohshita, T., Masutani, E., et al. (2007). Feasibility study on water solubilization of spawned-out salmon meat by conjugation with alginate oligosaccharide. Fish Science, 73, 924-930.
26. Tang, C. H., & Sun, X. (2011). A comparative study of physicochemical and conformational properties in three vicilins from Phaseolus legumes: implications for the structure-function relationship. Food Hydrocolloids, 25, 315-324.
27. Thongraung, C., & Kangsanan, S. (2010). Influence of pH, NaCl and pre-incubation on utilisation of surimi wash water in generation of antioxidative material by using the Maillard reaction. International Journal of Food Science and Technology, 45, 1696-1702.
28. Wong, B. T., Daya, L., & Augustin, M. A. (2011). Deamidated wheat protein-dextran Maillard conjugates: effect of size and location of polysaccharide conjugated on steric stabilization of emulsions at acidic pH. Food Hydrocolloids, 25, 1424-1432.
29. Wooster, T. J., & Augustin, M. A. (2007). Rheology of whey protein-dextran conjugate films at the air/water interface. Food Hydrocolloids, 21, 1072-1080.
30. Yongsawatdigul, J., & Hemung, B. (2010). Structural changes and functional properties of threadfin bream sarcoplasmic proteins subjected to pH-shifting treatments and lyophilization. Journal of Food Science, 75, 251-257.
31. Yongsawatdigul, J., & Park, J. W. (2003). Thermal denaturation and aggregation of threadfin bream actomyosin. Food Chemistry, 83, 409-416.