Production Optimization and Sensory Evaluation of Egg White Protein Hydrolysate with Angiotensin I Converting Enzyme Inhibitory Activity

• Author / Creator

  Li, Qi Yi

• Egg proteins are a well-known rich source of bioactive peptides with inhibitory activity against angiotensin I converting enzyme (ACE), a key enzyme responsible for the regulation of blood pressure. Peptides with ACE inhibitory activity could have potential application for prevention of high blood pressure, a chronic condition affecting about one third of Canadian adults. However, the lack of cost-effective methods of large-scale production and the presence of an unpleasant bitter taste limit the utilization of bioactive peptides and protein hydrolysates in functional food applications. The objectives of this study were to develop a scale-up method to prepare egg white protein hydrolysate with ACE inhibition activity and to investigate the applicability of egg white protein hydrolysate in two different food matrices. The optimal condition for preparing egg white protein hydrolysate was first determined by Taguchi’s method and then applied for scale-up preparation. ACE inhibitory activity and peptide yield of the egg white protein hydrolysates prepared in laboratory scale and large scale were 30 µg hydrolysate/mL and 77.5%, and 55 µg hydrolysate/mL and 53%, respectively. Egg white protein hydrolysate was incorporated into protein bars and protein beverages at up to 20% (w/w) and 2% (w/w), respectively. Protein beverages formulated with up to 1.5% (w/w) protein hydrolysate were found to be acceptable by study participants while all protein bar prototypes were not liked in general. Further research is needed to improve the consumer acceptability of protein hydrolysate.

• Subjects / Keywords

  • Sensory evaluation
  • Optimization
  • Egg white
  • ACE inhibitory activity

• Graduation date

  Fall 2016

• Type of Item

  Thesis

• Degree

  Master of Science

• DOI

  https://doi.org/10.7939/R3N29PF6V

• License

  This thesis is made available by the University of Alberta Libraries with permission of the copyright owner solely for non-commercial purposes. This thesis, or any portion thereof, may not otherwise be copied or reproduced without the written consent of the copyright owner, except to the extent permitted by Canadian copyright law.