Microwave-assisted cross-linking of milk proteins induced by microbial transglutaminase

Chun-Chi Chen1,2, Jung-Feng Hsieh1,2

  • 1Department of Food Science, Fu Jen Catholic University, Taipei 242, Taiwan.

Scientific Reports
|December 15, 2016
PubMed

Insights

Microbial transglutaminase (MTGase) and microwave irradiation (MI) effectively polymerize milk proteins, forming higher molecular-weight components. Combining MTGase and MI significantly accelerates this polymerization process.

Area of Science:

  • Food Science
  • Biochemistry
  • Protein Chemistry

Background:

  • Milk proteins are susceptible to modification and polymerization.
  • Enzymatic and physical treatments can alter protein structure and function.

Purpose of the Study:

  • To investigate the synergistic effects of microbial transglutaminase (MTGase) and microwave irradiation (MI) on milk protein polymerization.
  • To determine the impact of combined MTGase and MI treatment on the molecular weight and composition of milk proteins.

Main Methods:

  • Milk protein samples were treated with MTGase (7.0 units/mL) at 30°C for 3 hours.
  • Combined treatment involved MTGase and microwave irradiation.
  • Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and two-dimensional gel electrophoresis (2-DE) were used for analysis.

Main Results:

  • MTGase alone induced milk protein polymerization, forming components >130 kDa.
  • SDS-PAGE showed significant reductions in β-lactoglobulin, αs-casein, κ-casein, and β-casein content.
  • Combined MTGase and MI treatment resulted in a 3-fold increase in the polymerization rate compared to MTGase alone.
  • 2-DE confirmed polymerization of multiple milk proteins, including caseins, β-lactoglobulin, and serum albumin, under combined treatment.

Conclusions:

  • The combination of MTGase and MI is a highly effective method for milk protein polymerization.
  • This synergistic approach significantly enhances the rate and extent of protein polymerization compared to MTGase treatment alone.
  • The findings suggest a promising strategy for modifying milk protein functionalities.