吉林大学学报(工学版) ›› 2011, Vol. 41 ›› Issue (02): 579-0584.

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Characterization and stability of ACE inhibitory peptides derived fromegg white protein

LIU Jing-bo,YU Zhi-peng,ZHAO Wen-zhu,YU Yi-ding, LIU Bo-qun,LIN Song-yi   

  1. College of Light Industry and Economics &|Management, Jilin University, Changchun 130062,China
  • Received:2010-03-06 Published:2011-03-01

Abstract:

Bioactive peptides from egg white were prepared by enzymatic hydrolysis with alkaline proteinase. The fraction with AngiotensinConverting Enzyme (ACE) inhibition was purified by gel chromatography. Nineteen active peptides were identified by quadruple linearity ion trap tandem mass spectrometry. Three active peptides: DHPFLF, HAEIN and QIGLF were synthesized and the activities were measured. Results show that QIGLF has the highest activity with the IC50 value of 75.00  μM, and was resistant to digestion by protease of the gastrointestinal tract.

Key words: food processing technology, egg white, angiotensin converting enzyme(ACE) inhibitory peptide, characterization of structure, stability

CLC Number: 

  • TS201.2
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