Time domain nuclear magnetic resonance as a method to determine and characterize the water-binding capacity of whey protein microparticles

Food Hydrocolloids

Volumn 54, Issue , 2016, Pages 170-178

  Peters, Jorien P C M ^a   Vergeldt, Frank J ^a   Van As, Henk ^a   Luyten, Hannemieke ^b   Boom, Remko M ^a   van der Goot, Atze Jan ^a  

^a WAGENINGEN UNIVERSITY   (Netherlands)

^b FRIESLANDCAMPINA   (Netherlands)

Author keywords

Centrifugation; Microstructure; Nuclear magnetic resonance; Proteins; Swelling; Water binding capacity

Indexed keywords

EID: 84944259792     PISSN: 0268005X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodhyd.2015.09.031     Document Type: Article

References (29)

1. Ahmed J., Al-Jassar S., Thomas L.A. Comparison in rheological, thermal, and structural properties between Indian Basmati and Egyptian Giza rice flour dispersions as influenced by particle size. Food Hydrocolloids 2015, 48:72-83.
2. Berghout J.A.M., Boom R.M., van der Goot A.J. The potential of aqueous fraction of lupin seeds for high-protein foods. Food Chemistry 2014, 159:64-70.
3. Bertram H.C., Andersen H.J., Karlsson A.H. Comparative study of low-field NMR relaxation measurements and two traditional methods in the determination of water holding capacity of pork. Meat Science 2001, 57(2):125-132.
4. 2 relaxation in meat-an approach in the determination of water-holding capacity. Meat Science 2002, 60(3):279-285.
5. Brøndum J., Munck L., Henckel P., Karlsson A., Tornberg E., Engelsen S.B. Prediction of water-holding capacity and composition of porcine meat by comparative spectroscopy. Meat Science 2000, 55(2):177-185.
6. Colsenet R., Mariette F., Cambert M. NMR relaxation and water self-diffusion studies in whey protein solutions and gels. Journal of Agricultural and Food Chemistry 2005, 53(17):6784-6790.
7. van Duynhoven J., Voda A., Witek M., Van As H. Time-domain NMR applied to food products. Annual reports on NMR spectroscopy 2010, Vol. 69:145-197. Academic Press.
8. Fennema O.R. Food chemistry 1996, 366-370. Taylor & Francis. 3rd ed.
9. Goetz J., Koehler P. Study of the thermal denaturation of selected proteins of whey and egg by low resolution NMR. LWT - Food Science and Technology 2005, 38(5):501-512.
10. Hinrichs R., Götz J., Noll M., Wolfschoon A., Eibel H., Weisser H. Characterisation of the water-holding capacity of fresh cheese samples by means of low resolution nuclear magnetic resonance. Food Research International 2004, 37(7):667-676.
11. Hinrichs R., Götz J., Weisser H. Water-holding capacity and structure of hydrocolloid-gels, WPC-gels and yogurts characterised by means of NMR. Food Chemistry 2003, 82(1):155-160.
12. Jain A., Prakash M., Radha C. Extraction and evaluation of functional properties of groundnut protein concentrate. Journal of Food Science and Technology 2015, 10.1007/s13197-015-1758-7.
13. Kneifel W., Paquin P., Abert T., Richard J.P. Water-holding capacity of proteins with special regard to milk proteins and methodological aspects-a review. Journal of Dairy Science 1991, 74(7):2027-2041.
14. Lambelet P., Berrocal R., Desarzens C., Froehlicher I., Ducret F. Pulsed low-resolution NMR investigations of protein sols and gels. Journal of Food Science 1988, 53(3):943-946.
15. Mariette F. NMR relaxation of dairy products. Modern magnetic resonance 2006, 1697-1701. Springer. G.A. Webb (Ed.).
16. Mitchell J., Gladden L.F., Chandrasekera T.C., Fordham E.J. Low-field permanent magnets for industrial process and quality control. Progress in Nuclear Magnetic Resonance Spectroscopy 2014, 76:1-60.
17. Oakes J. Protein hydration. Nuclear magnetic resonance relaxation studies of the state of water in native bovine serum albumin solutions. Journal of the Chemical Society, Faraday Transactions 1: Physical Chemistry in Condensed Phases 1976, 72:216-227.
18. Oakes J. Thermally denatured proteins. Nuclear magnetic resonance, binding isotherm and chemical modification studies of thermally denatured bovine serum albumin. Journal of the Chemical Society, Faraday Transactions 1: Physical Chemistry in Condensed Phases 1976, 72:228-237.
19. Oztop M.H., Rosenberg M., Rosenberg Y., McCarthy K.L., McCarthy M.J. Magnetic resonance imaging (MRI) and relaxation spectrum analysis as methods to investigate swelling in whey protein gels. Journal of Food Science 2010, 75(8):E508-E515.
20. Peters J.P.C.M., Luyten H., Alting A.C., Boom R.M., van der Goot A.J. Effect of crosslink density on the water-binding capacity of whey protein microparticles. Food Hydrocolloids 2015, 44:277-284.
21. Provencher S.W. A constrained regularization method for inverting data represented by linear algebraic or integral equations. Computer Physics Communications 1982, 27(3):213-227.
22. Provencher S.W., Vogel R.H. Regularization techniques for inverse problems in molecular biology. Numerical treatment of inverse problems in differential and integral equations 1983, Vol 2:304-319. Birkhäuser, Boston.
23. Purwanti N., van der Veen E., van der Goot A.J., Boom R. Stiffening in gels containing whey protein isolate. International Dairy Journal 2013, 28(2):62-69.
24. Straadt I.K., Rasmussen M., Andersen H.J., Bertram H.C. Aging-induced changes in microstructure and water distribution in fresh and cooked pork in relation to water-holding capacity and cooking loss - a combined confocal laser scanning microscopy (CLSM) and low-field nuclear magnetic resonance relaxation study. Meat Science 2007, 75(4):687-695.
25. Sun Q., Xiong C.S.L. Functional and pasting properties of pea starch and peanut protein isolate blends. Carbohydrate Polymer 2014, 101:1134-1139.
26. Walkenström P., Nielsen M., Windhab E., Hermansson A.M. Effects of flow behaviour on the aggregation of whey protein suspensions, pure or mixed with xanthan. Journal of Food Engineering 1999, 42(1):15-26.
27. Walstra P. Physical chemistry of foods 2003, 99. Marcel Dekker, Inc.
28. Yu J., Ahmedna M., Goktepe I. Peanut protein concentrate: production and functional properties as affected by processing. Food Chemistry 2007, 103(1):121-129.
29. Zayas J.F. Functionality of proteins in food 1997, 76-133. Springer Berlin Heidelberg.