Production of angiotensin I-converting enzyme inhibitory peptides from soybean protein with Monascus purpureus acid proteinase

2005 ◽  
Vol 40 (6) ◽  
pp. 2191-2196 ◽  
Author(s):  
M. Kuba ◽  
C. Tana ◽  
S. Tawata ◽  
M. Yasuda
Keyword(s):  
Soybean Protein ◽  
Monascus Purpureus ◽  
Acid Proteinase ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Inhibitory Peptides ◽  
Angiotensin I Converting Enzyme

IDENTIFICATION OF ANGIOTENSIN I-CONVERTING ENZYME INHIBITORY PEPTIDES DERIVED FROM THE PEPTIC DIGEST OF SOYBEAN PROTEIN

2002 ◽  
Vol 26 (6) ◽  
pp. 543-554 ◽  
Author(s):  
JIUN-RONG CHEN ◽  
TAKASHI OKADA ◽  
KOJI MURAMOTO ◽  
KUNIO SUETSUNA ◽  
SUH-CHING YANG
Keyword(s):  
Soybean Protein ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Inhibitory Peptides ◽  
Angiotensin I Converting Enzyme

Angiotensin I-converting enzyme inhibitory peptides in red-mold rice made by Monascus purpureus

2009 ◽  
Vol 44 (10) ◽  
pp. 1139-1143 ◽  
Author(s):  
Megumi Kuba ◽  
Kumi Tanaka ◽  
Masayasu Sesoko ◽  
Fumihide Inoue ◽  
Masaaki Yasuda
Keyword(s):  
Monascus Purpureus ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Inhibitory Peptides ◽  
Angiotensin I Converting Enzyme ◽  
Red Mold Rice

P122 Angiotensin I converting enzyme inhibitory peptides are derived from soybean protein

1998 ◽  
Vol 136 ◽  
pp. S79
Author(s):  
Jiun-Rong Chen ◽  
Suh-Ching Yang ◽  
Yao-Ling Lin ◽  
Ming-Jer Shieh
Keyword(s):  
Soybean Protein ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Inhibitory Peptides ◽  
Angiotensin I Converting Enzyme

scholarly journals Effect of Different Proteases on the Degree of Hydrolysis and Angiotensin I-Converting Enzyme-Inhibitory Activity in Goat and Cow Milk

Biomolecules ◽  
2018 ◽  
Vol 8 (4) ◽  
pp. 101 ◽  
Author(s):  
Guowei Shu ◽  
Jie Huang ◽  
Chunju Bao ◽  
Jiangpeng Meng ◽  
He Chen ◽  
...  
Keyword(s):  
Inhibitory Activity ◽  
Goat Milk ◽  
Cow Milk ◽  
Degree Of Hydrolysis ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Ace Inhibitory Activity ◽  
Inhibitory Peptides ◽  
Angiotensin I Converting Enzyme ◽  
Ace Inhibitory

Angiotensin I-converting enzyme (ACE) peptides are bioactive peptides that have important value in terms of research and application in the prevention and treatment of hypertension. While widespread literature is concentrated on casein or whey protein for production of ACE-inhibitory peptides, relatively little information is available on selecting the proper proteases to hydrolyze the protein. In this study, skimmed cow and goat milk were hydrolyzed by four commercial proteases, including alkaline protease, trypsin, bromelain, and papain. Angiotensin I-converting enzyme-inhibitory peptides and degree of hydrolysis (DH) of hydrolysates were measured. Moreover, we compared the difference in ACE-inhibitory activity between cow and goat milk. The results indicated that the DH increased with the increase in hydrolysis time. The alkaline protease-treated hydrolysates exhibited the highest DH value and ACE-inhibitory activity. Additionally, the ACE-inhibitory activity of hydrolysates from goat milk was higher than that of cow milk-derived hydrolysates. Therefore, goat milk is a good source to obtain bioactive peptides with ACE-inhibitory activity, as compared with cow milk. A proper enzyme to produce ACE-inhibitory peptides is important for the development of functional milk products and will provide the theoretical basis for industrial production.

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