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Thermal processing modulates the interaction between whey proteins with variable hydrolysis and polyphenols:

Hui Zhang1, Jinfeng Zhang1, Lu Liu1

  • 1Food College, Northeast Agricultural University, No.600 Changjiang St., Xiangfang Dist, 150030 Harbin, China; Key Laboratory of Dairy Science, Ministry of Education, Northeast Agricultural University, No. 600 Changjiang St., Xiangfang Dist, 150030 Harbin, China.

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Thermal treatment and enzymatic hydrolysis of whey protein isolate (WPI) with epigallocatechin gallate (EGCG) enhance functional properties. Optimized processing improves antioxidant and emulsifying capacities, offering insights for functional food development.

Keywords:
EGCGEnzymatic hydrolysiFunctionalityThermal treatmentWhey protein isolate

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Area of Science:

  • Food Science and Technology
  • Biochemistry
  • Protein Chemistry

Background:

  • Thermal processing is crucial for food safety but can negatively impact protein-polyphenol complex stability and functionality.
  • Whey protein isolate (WPI) and its hydrolysates (WPIHs) are valuable food ingredients, while epigallocatechin gallate (EGCG) is a potent antioxidant polyphenol.
  • Understanding the interaction between WPI/WPIHs and EGCG under thermal stress is vital for developing stable functional foods.

Purpose of the Study:

  • To investigate the effect of thermal treatments (pasteurization, sterilization) on WPI/WPIH-EGCG complex formation and stability.
  • To analyze the binding mechanisms and forces governing WPI/WPIH-EGCG interactions under different hydrolysis degrees and thermal conditions.
  • To evaluate the impact of these interactions on the functional properties (antioxidant, enzyme inhibition, emulsification) of the complexes.

Main Methods:

  • Whey protein isolate (WPI) underwent enzymatic hydrolysis to produce WPIHs with varying degrees of hydrolysis.
  • WPI and WPIHs were complexed with epigallocatechin gallate (EGCG) and subjected to thermal treatments (pasteurization, sterilization).
  • Binding interactions were analyzed using fluorescence spectroscopy (static quenching mechanism), and functional properties were assessed via antioxidant assays (ABTS, DPPH), enzyme inhibition assays (α-glucosidase, α-amylase), and emulsifying property measurements.

Main Results:

  • Thermal treatment induced protein unfolding and aggregation, altering WPI/WPIH structure.
  • Binding of WPI/WPIHs to EGCG followed a static quenching mechanism, primarily driven by hydrophobic interactions, shifting to electrostatic or van der Waals/hydrogen bonds under sterilization depending on hydrolysis degree.
  • Partially hydrolyzed WPI (WPIH1) complexed with EGCG showed significantly enhanced antioxidant activity (ABTS: 94.16%, DPPH: 84.55%), enzyme inhibition (α-glucosidase: 72.17%, α-amylase: 69.70%), and emulsifying properties (47.49% increase), particularly when prepared at 65°C.

Conclusions:

  • Appropriate thermal treatment and enzymatic hydrolysis can stabilize the functional properties of WPI-EGCG complexes.
  • The study elucidates the binding mechanisms between WPI (varying hydrolysis degrees) and EGCG under thermal stress.
  • Findings provide valuable insights for optimizing thermal processing parameters for functional foods incorporating EGCG and whey protein derivatives.