Stability of Antihypertensive Peptides from Egg White Protein to Chemicals and Enzymes

doi:10.7506/spkx1002-6630-201009006

FOOD SCIENCE ›› 2010, Vol. 31 ›› Issue (9): 23-26.doi: 10.7506/spkx1002-6630-201009006

• Basic Research • Previous Articles Next Articles

Stability of Antihypertensive Peptides from Egg White Protein to Chemicals and Enzymes

YU Zhi-peng，ZHAO Wen-zhu，YU Yi-ding，LIU Bo-qun，LIU Jing-bo*

Laboratory of Nutrition and Functional Food, College of Quartermaster Technology,
Jilin University, Changchun 130062, China

Received:2009-09-27 Online:2010-05-01 Published:2010-12-29
Contact: LIU Jing-bo* E-mail:ljb168@sohu.com

Abstract

Abstract:

The stability of antihypertensive peptides from egg white protein to chemicals was evaluated by Plackett-Burman design and its stability in mimic gastrointestinal environment was also investigated by determining angiotensin converting enzyme activity. Results indicated that pH, temperature, light illumination, stock peptide concentration, Pasteurization treatment, ultrasonic treatment and magnesium ions had no significant effect on the stability of antihypertensive peptides. However, the stability of antihypertensive peptides was sensitive to pepsin and trypsin. The activity of antihypertensive peptides decreased to 13.0 % and 4.0 % from 46.0 %.

Key words: egg white protein, peptide, stability, angiotensin converting enzyme

CLC Number:

TS253.1

YU Zhi-peng，ZHAO Wen-zhu，YU Yi-ding，LIU Bo-qun，LIU Jing-bo*. Stability of Antihypertensive Peptides from Egg White Protein to Chemicals and Enzymes[J]. FOOD SCIENCE, 2010, 31(9): 23-26.

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Stability of Antihypertensive Peptides from Egg White Protein to Chemicals and Enzymes

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