Effects of transglutaminase-induced modification in the presence of oligochitosan of 1 kDa on the structure and gelling properties of caseinat
Song CL, Zhao XHhttps://doi.org/10.17221/423/2015-CJFSCitation:CL S., XH Z. (2016): Effects of transglutaminase-induced modification in the presence of oligochitosan of 1 kDa on the structure and gelling properties of caseinat. Czech J. Food Sci., 34: 564-569.
Caseinate, transglutaminase (TGase), and an oligochitosan of 1 kDa were used to prepare a glycated and cross-linked caseinate (GC-caseinate), aiming to assess potential changes in both the structure and gelling properties of such caseinate. The results of Fourier transform infrared analysis revealed that only GC-caseinate contained saccharide portions in its molecules, evidencing TGase-induced caseinate glycation. Circular dichroism results showed that GC-caseinate possessed a more ordered secondary structure than caseinate. Other results also demonstrated that TGase-induced modification resulted in a lower gelation temperature of GC-caseinate (59°C vs. 68°C) and increased the final tan δ value (0.30 vs. 0.15) compared to caseinate during the development of acidified gels. In addition, the acidified gels from GC-caseinate were detected to have lower water holding capacity (0.720 vs. 0.781 g/g gels), expanded gel network, and larger pore sizes than those from caseinate. It is thus evidenced that the used TGase-induced modification could confer caseinate with ordered secondary structure, expanded gel network but lower water holding capacity.Keywords:
milk proteins; oligosaccharide; enzyme; glycation; cross-linking; propertyReferences:
Anema Skelte G., de Kruif C.G. (Kees) (2012): Lactoferrin binding to transglutaminase cross-linked casein micelles. International Dairy Journal, 26, 83-87 https://doi.org/10.1016/j.idairyj.2011.12.004Creamer L.K., Richardson T., Parry D.A.D. (1981): Secondary structure of bovine αS1- and β-casein in solution. Archives of Biochemistry and Biophysics, 211, 689-696 https://doi.org/10.1016/0003-9861(81)90505-1Darewicz M., Dziuba J. (): The effect of glycosylation on emulsifying and structural properties of bovine β-casein. Nahrung/Food, 45, 15-20 https://doi.org/10.1002/1521-3803(20010101)45:1<15::AID-FOOD15>3.0.CO;2-YDomagała Jacek, Najgebauer-Lejko Dorota D., Wieteska-Śliwa Ilona, Sady Marek, Wszołek Monika, Bonczar Genowefa, Filipczak-Fiutak Magda (2015): The influence of milk protein cross-linking by transglutaminase on the rennet coagulation time and the gel properties. Journal of the Science of Food and Agriculture, , n/a-n/a https://doi.org/10.1002/jsfa.7534Ercili Cura D., Lille M., Partanen R., Kruus K., Buchert J., Lantto R. (2010): Effect of Trichoderma reesei tyrosinase on rheology and microstructure of acidified milk gels. International Dairy Journal, 20, 830-837 https://doi.org/10.1016/j.idairyj.2010.06.008Ercili-Cura Dilek, Lille Martina, Legland David, Gaucel Sébastien, Poutanen Kaisa, Partanen Riitta, Lantto Raija (2013): Structural mechanisms leading to improved water retention in acid milk gels by use of transglutaminase. Food Hydrocolloids, 30, 419-427 https://doi.org/10.1016/j.foodhyd.2012.07.008Færgemand M., Qvist K.B. (1997): Transglutaminase: effect on rheological properties, microstructure and permeability of set style acid skim milk gel. Food Hydrocolloids, 11, 287-292 https://doi.org/10.1016/S0268-005X(97)80058-6Gaygadzhiev Zafir, Corredig Milena, Alexander Marcela (2009): The impact of the concentration of casein micelles and whey protein-stabilized fat globules on the rennet-induced gelation of milk. Colloids and Surfaces B: Biointerfaces, 68, 154-162 https://doi.org/10.1016/j.colsurfb.2008.09.026Guan Jun-Jun, Qiu Ai-Yong, Liu Xiao-Ya, Hua Yu-Fei, Ma Yun-Hui (2006): Microwave improvement of soy protein isolate–saccharide graft reactions. Food Chemistry, 97, 577-585 https://doi.org/10.1016/j.foodchem.2005.05.035HAGA Seiichi, OHASHI Tomio (1984): Heat-induced gelation of a mixture of myosin B and soybean protein.. Agricultural and Biological Chemistry, 48, 1001-1007 https://doi.org/10.1271/bbb1961.48.1001Handa Akihiro, Kuroda Namio (1999): Functional Improvements in Dried Egg White through the Maillard Reaction. Journal of Agricultural and Food Chemistry, 47, 1845-1850 https://doi.org/10.1021/jf9811018Havea Palatasa (2006): Protein interactions in milk protein concentrate powders. International Dairy Journal, 16, 415-422 https://doi.org/10.1016/j.idairyj.2005.06.005Jiang Jiang, Chen Jie, Xiong Youling L. (2009): Structural and Emulsifying Properties of Soy Protein Isolate Subjected to Acid and Alkaline pH-Shifting Processes. Journal of Agricultural and Food Chemistry, 57, 7576-7583 https://doi.org/10.1021/jf901585nJiang Shu-Juan, Zhao Xin-Huai (2010): Transglutaminase-induced cross-linking and glucosamine conjugation in soybean protein isolates and its impacts on some functional properties of the products. European Food Research and Technology, 231, 679-689 https://doi.org/10.1007/s00217-010-1319-2Jiang Shu-Juan, Zhao Xin-Huai (2011): Transglutaminase-induced cross-linking and glucosamine conjugation of casein and some functional properties of the modified product. International Dairy Journal, 21, 198-205 https://doi.org/10.1016/j.idairyj.2010.12.004Johnson W. Curtis (1990): Protein secondary structure and circular dichroism: A practical guide. Proteins: Structure, Function, and Genetics, 7, 205-214 https://doi.org/10.1002/prot.340070302Koh May Wei Winnie, Matia Merino Lara, Dickinson Eric (2002): Rheology of acid-induced sodium caseinate gels containing added gelatin. Food Hydrocolloids, 16, 619-623 https://doi.org/10.1016/S0268-005X(02)00025-5Lucey J. (2004): Formation, structural properties and rheology of acid-coagulated milk gels. In: Fox P.F., McSweemey P.L.H., Cogan T.M., Guinee T.P. (eds): Cheese: Chemistry, Physics and Microbiology. 3rd Ed. Vol. 1. General Aspect. London, Elsevier Academic Press: 105–122.Mao R., Tang J., Swanson B.G. (2001): Water holding capacity and microstructure of gellan gels. Carbohydrate Polymers, 46, 365-371 https://doi.org/10.1016/S0144-8617(00)00337-4Rocha C., Teixeira J.A., Hilliou L., Sampaio P., Gonçalves M.P. (2009): Rheological and structural characterization of gels from whey protein hydrolysates/locust bean gum mixed systems. Food Hydrocolloids, 23, 1734-1745 https://doi.org/10.1016/j.foodhyd.2009.02.005Schneckenburger Tatjana, Lattao Charisma, Pignatello Joseph J., Schaumann Gabriele E., Thiele-Bruhn Sören, Cao Xiaoyan, Mao Jingdong (2012): Preparation and characterization of humic acid cross-linked with organic bridging groups. Organic Geochemistry, 47, 132-138 https://doi.org/10.1016/j.orggeochem.2012.03.014Schorsch C, Carrie H, Norton I.T (2000): Cross-linking casein micelles by a microbial transglutaminase: influence of cross-links in acid-induced gelation. International Dairy Journal, 10, 529-539 https://doi.org/10.1016/S0958-6946(00)00069-8Segura-Campos Maira, Chel-Guerrero Luis, Betancur-Ancona David, Hernandez-Escalante Victor M. (2011): Bioavailability of Bioactive Peptides. Food Reviews International, 27, 213-226 https://doi.org/10.1080/87559129.2011.563395Siamand Rahela, Deeth Hilton C., Al-Saadi Jasim M.S. (2014): Textural and sensory properties of a calcium-induced milk gel. Journal of Food Engineering, 139, 10-12 https://doi.org/10.1016/j.jfoodeng.2014.04.014Song Chun-Li, Zhao Xin-Huai (2013): Rheological, gelling and emulsifying properties of a glycosylated and cross-linked caseinate generated by transglutaminase. International Journal of Food Science & Technology, 48, 2595-2602 https://doi.org/10.1111/ijfs.12255Song C.L., Zhao X.H. (2014a): The preparation of an oligochitosan-glycosylated and cross-linked caseinate obtained by a microbial transglutaminase and its functional properties. International Journal of Dairy Technology, 67: 110–116.Song C.L., Zhao X.H. (2014b): Structure and property modification of an oligochitosan-glycosylated and crosslinked soybean protein generated by microbial transglutaminase. Food Chemistry, 163: 114–119.Tsumura Kazunobu, Saito Tsutomu, Tsuge Keisuke, Ashida Hiroko, Kugimiya Wataru, Inouye Kuniyo (2005): Functional properties of soy protein hydrolysates obtained by selective proteolysis. LWT - Food Science and Technology, 38, 255-261 https://doi.org/10.1016/j.lwt.2004.06.007van Vliet T., van Dijk H. J. M., Zoon P., Walstra P. (1991): Relation between syneresis and rheological properties of particle gels. Colloid and Polymer Science, 269, 620-627 https://doi.org/10.1007/BF00659917