Oat Protein Concentrates with Improved Solubility Produced by an Enzyme-Aided Ultrafiltration Extraction Method

Area of Science:

• Food Science
• Biotechnology

Background:

• Oat protein concentrates are valuable but often have limited solubility.
• Improving the functional properties of oat proteins is crucial for food applications.

Purpose of the Study:

• To develop an enzyme-aided extraction method for highly functional oat protein concentrates.
• To investigate the effect of protein-glutaminase (PG) deamidation on oat protein solubility and functional properties.
• To optimize deamidation parameters using response surface methodology (RSM).

Main Methods:

• Enzyme-aided extraction using slightly alkaline conditions (pH 8.0).
• Ultrafiltration and diafiltration for protein concentration.
• Deamidation of oat proteins using protein-glutaminase (PG) under optimized conditions (pH 8.0, 11.0 U/g protein, 4 h).
• Response surface methodology (RSM) for parameter optimization.

Main Results:

• Two oat protein concentrates were produced: non-deamidated (45.0% protein) and deamidated (52.4% protein).
• Deamidation significantly improved protein solubility, especially at neutral and slightly alkaline pH.
• Both concentrates formed strong heat-induced gels at 10% protein concentration.

Conclusions:

• The developed method effectively produces highly functional oat protein concentrates.
• Enzymatic deamidation with PG is a viable strategy to enhance oat protein solubility.
• The resulting oat protein concentrates exhibit good solubility and gelation properties for food applications.