In this study, Lepidotrigla microptera were hydrolyzed with four different proteolytic enzymes
(Papain, neutrase, flavourzyme, and alcalase), and their distribution of molecular weights …

Enzymatic hydrolysis of the protein from an edible insect species, the cotton leafworm
Spodoptera littoralis (Lepidoptera) leads to the release of angiotensin I converting enzyme …

Smooth-hound viscera proteins were enzymatically hydrolyzed, using Esperase®, and the
resulting hydrolysate was fractionated by ultrafiltration through four membranes with …

Alcalase, neutral protease, and pepsin were used to hydrolyze the skin of Takifugu flavidus.
The T. flavidus hydrolysates (TFHs) with the maximum degree of hydrolysis (DH) and …

Many angiotensin-I-converting enzyme (ACE) inhibitory peptides are used to prevent and
manage hypertension. In this study, ACE inhibitory peptides were isolated from an insect …

Abstract Angiotensin-I Converting Enzyme (ACE) plays a pivotal role in regulating
hypertension. Inhibition of ACE by potent inhibitors is an excellent approach to treating high …

Short peptides from different sources have been proven to be very efficient inhibitors of
angiotensin I-converting enzyme (ACE), an enzyme with a major role in the regulation of …

Background Many short peptides have proved to exhibit potential anti-hypertensive activity
through the inhibition of the Angiotensin I-converting enzyme (ACE) activity and the …

In order to rapidly and efficiently excavate antihypertensive ingredients in Todarodes
pacificus, its myosin heavy chain was hydrolyzed in silico and the angiotensin-converting …

Candidate peptides with novel angiotensin-I-converting enzyme (ACE) inhibitor activity were
obtained from hydrolysates of Gracilariopsis lemaneiformis by virtual screening method. Our …