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Research Article

Academia Journal of Agricultural Research 3(12): 361-368, December 2015
DOI: 10.15413/ajar.2015.0183
ISSN: 2315-7739
2015 Academia Publishing

Abstract

 

Angiotensin I converting enzyme inhibitory activity of bee pupae protein hydrolysates
 


Accepted 24th November, 2015
 

Chih-Wei Chen1#, Yu-Chin Chai1#, Chia-Chi Tu2, Ming-Ching Cheng1, Chin-Yin Tseng1 and Chi-Yue Chang 1*


1Department of Health Food, Chung Chou University of Science and Technology, Changhua, Taiwan.
2Department of Boindustry Technology, Da-Yeh University, Changhua, Taiwan.

 

*Corresponding author e-mail: ccwlly@gmail.com


The protein isolates from bee pupae were hydrolyzed by Alcalase and Flavourzyme, and the angiotensin I converting enzyme (ACE) inhibitory activities of the hydrolysates were evaluated. The results indicated that hydrolysis could increase the ACE inhibitory activity; the maximum value of the inhibition was 66.71% (IC50 = 22.70 mg/ml). The hydrolysates with high ACE inhibitory activity were also fractionated by different molecular weight cut-off (MWCO) membrane ultra filtration. The ACE inhibitory activities of the filtrates of MWCO 5~3 kDa, 3~1 kDa and < 1 kDa were found to be 69.77, 61.53 and 96.98%, respectively, and the IC50 were 20.04, 31.78 and 0.66 mg/ml, respectively. The results suggest that the bee pupae hydrolysates can be used as an ingredient for nutraceuticals against hypertension and its related diseases.

Key words: Bee pupae, enzymatic hydrolysis, ultrafiltration, molecular weight cut-off (MWCO), ACE inhibitory activity.
 

This is an open access article published under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

 

Cite this article as:

Chen CW, Chai YU, Tu CC, Cheng MC, Tseng CY, Chang CY (2015). Angiotensin I converting enzyme inhibitory activity of bee pupae protein hydrolysates. Acad. J. Agric. Res. 3(12): 361-368.

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