Article

Isoenergic modification of whey protein structure by denaturation and crosslinking using transglutaminase

Food & Function, Royal Society of Chemistry (RSC), ISSN 2042-6496

Volume 9, 2, 2018

DOI:10.1039/c7fo01451a, Dimensions: pub.1100202412, PMID: 29327016,

Authors

Stender, Emil G P (1) (2) (3)
Koutina, Glykeria (1) (4) (5) (6)
Almdal, Kristoffer (1) (2) (7)
Hassenkam, Tue (1) (4) (5) (8)
Mackie, Alan (9) (10) (11) (12)
Ipsen, Richard (1) (4) (5) (6)
Svensson, Birte (1) (2) (3)

Affiliations

Organisations

  1. (1) Denmark
  2. (2) Technical University of Denmark, grid.5170.3, DTU
  3. (3) Department of Biotechnology and Biomedicine
  4. (4) Copenhagen
  5. (5) University of Copenhagen, grid.5254.6, KU
  6. (6) Department of Food Science
  7. (7) Department of Micro- and Nanotechnology
  8. (8) Department of Chemistry
  9. (9) Colney
  10. (10) Institute of Food Research
  11. (11) Norwich Research Park, grid.420132.6
  12. (12) School of Food Science and Nutrition

Countries

Denmark

United Kingdom

Continents

Europe

Description

Transglutaminase (TG) catalyzes formation of covalent bonds between lysine and glutamine side chains and has applications in manipulation of food structure. Physical properties of a whey protein mixture (SPC) denatured either at elevated pH or by heat-treatment and followed by TG catalyzed crosslinking, have been characterised using dynamic light scattering, size exclusion chromatography, flourescence spectroscopy and atomic force microscopy. The degree of enzymatic crosslinking appeared higher for pH- than for heat-denatured SPC. The hydrophobic surface properties depended on the treatment, thus heating caused the largest exposure of the hydrophobic core of SPC proteins, which was decreased by crosslinking. The particle size of the treated SPC samples increased upon crosslinking by TG. Moreover, the particle morphology depended on the type of denaturing treatment, thus heat-treated SPC contained fibrillar structures, while pH-denatured SPC remained globular as documented by using atomic force microscopy. Finally, the in vitro digestability of the different SPC samples was assessed under simulated gastric and intestinal conditions. Notably heat-treatment was found to lower the gastric digestion rate and enzymatic crosslinking reduced both the gastric and the intestinal rate of digestion. These characteristics of the various SPC samples provide a useful basis for design of isoenergic model foods applicable in animal and human studies on how food structure affects satiety.

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NORA University Profiles

Technical University of Denmark

University of Copenhagen

Danish Open Access Indicator

2018: Unused

Research area: Science & Technology

Danish Bibliometrics Indicator

2018: Level 1

Research area: Science & Technology

Dimensions Citation Indicators

Times Cited: 9

Field Citation Ratio (FCR): 2.28

Relative Citation ratio (RCR): 1.1