Laccase-aided modification: Effects on structure, gel properties and antioxidant activities of α-lactalbumin

LWT

Volumn 80, Issue , 2017, Pages 355-363

  Jiang, Zhanmei ^a,b   Yuan, Xiangying ^a   Yao, Kun ^a   Li, Xueyan ^a   Zhang, Xinliu ^a   Mu, Zhishen ^b   Jiang, Lianzhou ^a   Hou, Juncai ^a  

^a NORTHEAST AGRICULTURAL UNIVERSITY   (China)

^b Mengniu Dary R and D Center   (China)

Author keywords

Antioxidant activities; Ferulic acid; Gel properties; Laccase; Lactalbumin

Indexed keywords

ANTIOXIDANTS; CATALYSIS; PARTICLE SIZE; PARTICLE SIZE ANALYSIS; SIZE EXCLUSION CHROMATOGRAPHY;

ANTI-OXIDANT ACTIVITIES; DPPH RADICAL SCAVENGING ACTIVITIES; FERULIC ACIDS; GEL PROPERTIES; INTRINSIC FLUORESCENCE; LACCASES; POSITIVE CORRELATIONS; SDS-PAGE ANALYSIS;

ENZYMES;

EID: 85014162187     PISSN: 00236438     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.lwt.2017.02.043     Document Type: Article

References (37)

1. Bönisch, M.P., Huss, M., Weitl, K., Kulozik, U., Transglutaminase cross-linking of milk proteins and impact on yoghurt gel properties. International Dairy Journal 17:11 (2007), 1360–1371.
2. Chanarat, S., Benjakul, S., Effect of formaldehyde on protein cross-linking and gel forming ability of surimi from lizardfish induced by microbial transglutaminase. Food Hydrocolloids 30:2 (2013), 704–711.
3. Chandrapala, J., Zisu, B., Palmer, M., Kentish, S., Ashokkumar, M., Effects of ultrasound on the thermal and structural characteristics of proteins in reconstituted whey protein concentrate. Ultrasonics Sonochemistry 18:5 (2011), 951–957.
4. Chen, B., Li, H., Ding, Y., Suo, H., Formation and microstructural characterization of whey protein isolate/beet pectin coacervations by laccase catalyzed cross-linking. LWT - Food Science and Technology 47:1 (2012), 31–38.
5. Davies, K.J., Protein damage and degradation by oxygen radicals. I. general aspects. Journal of Biological Chemistry 262:20 (1987), 9895–9901.
6. Dean, R.T., Shanlin, F.U., Stocker, R., Davies, M.J., Biochemistry and pathology of radical mediated protein oxidation. Biochemical Journal 324 (1997), 1–18.
7. Ercili Cura, D., Lantto, R., Lille, M., Andberg, M., Kruus, K., Buchert, J., Laccase-aided protein modification: Effects on the structural properties of acidified sodium caseinate gels. International Dairy Journal 19:12 (2009), 737–745.
8. Figueroa-Espinoza, M.C., Morel, M.H., Rouau, X., Effect of lysine, tyrosine, cysteine, and glutathione on the oxidative cross-linking of feruloylated arabinoxylans by a fungal laccase. Journal of Agricultural and Food Chemistry 46:7 (1998), 2583–2589.
9. Færgemand, M., Otte, J., Qvist, K.B., Cross-linking of whey proteins by enzymatic oxidation. J Agric Food Chem 46:4 (1998), 1326–1333.
10. Gauche, C., Vieira, J.T.C., Ogliari, P.J., Bordignon-Luiz, M.T., Crosslinking of milk whey proteins by transglutaminase. Process Biochemistry 43:7 (2008), 788–794.
11. Gianfreda, L., Xu, F., Bollag, J.M., Laccases: A useful group of oxidoreductive enzymes. Bioremediation Journal 3:1 (1999), 1–26.
12. Halaouli, S., Asther, M., Kruus, K., Guo, L., Hamdi, M., Sigoillot, J.C., et al. Characterization of a new tyrosinase from Pycnoporus species with high potential for food technological applications. Journal of Applied Microbiology 98:2 (2005), 332–343.
13. Heijnis, W.H., Wierenga, P.A., van Berkel, W.J., Gruppen, H., Directing the oligomer size distribution of peroxidase-mediated cross-linked bovine alpha-lactalbumin. J Agric Food Chem 58:9 (2010), 5692–5697.
14. Hiller, B., Lorenzen, P.C., Functional properties of milk proteins as affected by enzymatic oligomerisation. Food Research International 42:8 (2009), 899–908.
15. Hiller, B., Lorenzen, P.C., Functional properties of milk proteins as affected by Maillard reaction induced oligomerisation. Food Research International 43:4 (2010), 1155–1166.
16. Hu, Y., Liu, W., Yuan, C., Morioka, K., Chen, S., Liu, D., et al. Enhancement of the gelation properties of hairtail (Trichiurus haumela) muscle protein with curdlan and transglutaminase. Food Chem 176 (2015), 115–122.
17. Jung, J., Wicker, L., Laccase mediated conjugation of heat treated beta-lactoglobulin and sugar beet pectin. Carbohydrate Polymers 89:4 (2012), 1244–1249.
18. Jung, J., Wicker, L., β-Lactoglobulin conformation and mixed sugar beet pectin gel matrix is changed by laccase. LWT - Food Science and Technology 55:1 (2014), 9–15.
19. Jus, S., Kokol, V., Guebitz, G.M., Tyrosinase-catalysed coupling of functional molecules onto protein fibres. Enzyme and Microbial Technology 42:7 (2008), 535–542.
20. Kim, S., Cavaco-Paulo, A., Laccase-catalysed protein–flavonoid conjugates for flax fibre modification. Applied Microbiology and Biotechnology 93:2 (2012), 585–600.
21. Labat, E., Morel, M., Rouau, X., Effects of laccase and ferulic acid on wheat flour doughs 1. Cereal Chemistry 77:6 (2000), 823–828.
22. Lantto, R., Puolanne, E., Kalkkinen, N., Buchert, J., Autio, K., Enzyme-aided modification of chicken-breast myofibril proteins: Effect of laccase and transglutaminase on gelation and thermal stability. J Agric Food Chem 53:23 (2005), 9231–9237.
23. Lantto, R., Puolanne, E., Kruus, K., Buchert, J., Autio, K., Tyrosinase-aided protein cross-linking: Effects on gel formation of chicken breast myofibrils and texture and water-holding of chicken breast meat homogenate gels. J Agric Food Chem 55:4 (2007), 1248–1255.
24. Li, J., Zhao, X., Oxidative cross-linking of casein by horseradish peroxidase and its impacts on emulsifying properties and the microstructure of acidified gel. African Journal of Biotechnology 8:20 (2009), 5508–5515.
25. Ma, H., Forssell, P., Partanen, R., Buchert, J., Boer, H., Improving laccase catalyzed cross-linking of whey protein isolate and their application as emulsifiers. J Agric Food Chem 59:4 (2011), 1406–1414.
26. Manu, B.T., Prasada Rao, U.J.S., Role of peroxidase and H2O2 in cross-linking of gluten proteins. Journal of Food Biochemistry 35:6 (2011), 1695–1702.
27. Mattinen, M.L., Kruus, K., Buchert, J., Nielsen, J.H., Andersen, H.J., Steffensen, C.L., Laccase-catalyzed polymerization of tyrosine-containing peptides. FEBS Journal 272:14 (2005), 3640–3650.
28. Minamihata, K., Goto, M., Kamiya, N., Protein heteroconjugation by the peroxidase-catalyzed tyrosine coupling reaction. Bioconjugate chemistry 22:11 (2011), 2332–2338.
29. Onwulata, C.I., Tomasula, P.M., Gelling properties of tyrosinase-treated Dairy proteins. Food and Bioprocess Technology 3:4 (2008), 554–560.
30. Rawel, H.M., Rohn, S., Kruse, H.-P., Kroll, J., Structural changes induced in bovine serum albumin by covalent attachment of chlorogenic acid. Food Chemistry 78:4 (2002), 443–455.
31. Saricay, Y., Wierenga, P., de Vries, R., Nanostructure development during peroxidase catalysed cross-linking of α-lactalbumin. Food Hydrocolloids 33:2 (2013), 280–288.
32. Saricay, Y., Wierenga, P.A., de Vries, R., Changes in protein conformation and surface hydrophobicity upon peroxidase-catalyzed cross-linking of apo-alpha-lactalbumin. J Agric Food Chem 62:38 (2014), 9345–9352.
33. Saricay, Y., Wierenga, P.A., de Vries, R., Rheological properties of dispersions of enzymatically cross-linked apo-α-lactalbumin. Food Hydrocolloids 56 (2016), 344–351.
34. Selinheimo, E., Lampila, P., Mattinen, M.L., Buchert, J., Formation of protein− oligosaccharide conjugates by laccase and tyrosinase. Journal of Agricultural and Food Chemistry 56:9 (2008), 3118–3128.
35. Tantoush, Z., Stanic, D., Stojadinovic, M., Ognjenovic, J., Mihajlovic, L., Atanaskovic-Markovic, M., et al. Digestibility and allergenicity of β-lactoglobulin following laccase-mediated cross-linking in the presence of sour cherry phenolics. Food Chemistry 125:1 (2011), 84–91.
36. Thalmann, C., Lötzbeyer, T., Enzymatic cross-linking of proteins with tyrosinase. European Food Research and Technology 214:4 (2002), 276–281.
37. Yen, G.C., Hsieh, P.P., Antioxidative activity and scavenging effects on active oxygen of xylose-lysine maillard reaction products. Journal of the Science of Food and Agriculture 67:3 (1995), 415–420.