Purification and molecular docking study of a novel angiotensin-I converting enzyme (ACE) inhibitory peptide from alcalase hydrolysate of ultrasonic-pretreated silkworm pupa (Bombyx mori) protein

•Ultrasonic pretreatment was used to produce ACE inhibitory peptide from silkworm pupa protein.•ACE inhibitory peptide was identified as Lys-His-Val.•The peptide was stable against gastrointestinal proteases.•The peptide could effectively interact with the active site of ACE. Silkworm pupa (Bombyx m...

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Bibliographic Details
Published in:Process biochemistry (1991) 2015-05, Vol.50 (5), p.876-883
Main Authors: Jia, Junqiang, Wu, Qiongying, Yan, Hui, Gui, Zhongzheng
Format: Article
Language:English
Subjects:
ACE inhibitory peptide
Bombyx mori
Docking
Enzymes
Hydrolysates
Ingredients
Inhibitors
Molecular docking
Peptides
Proteins
Pupa
Purification
Silkworm pupa (Bombyx mori)
Silkworms
Ultrasonic pretreatment
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Summary:•Ultrasonic pretreatment was used to produce ACE inhibitory peptide from silkworm pupa protein.•ACE inhibitory peptide was identified as Lys-His-Val.•The peptide was stable against gastrointestinal proteases.•The peptide could effectively interact with the active site of ACE. Silkworm pupa (Bombyx mori) protein (SPP) was treated by ultrasound, and then was hydrolyzed using alcalase. The hydrolysate with the highest ACE inhibitory activity was obtained at hydrolysis of 50min when SPP was treated at power of 410W/100ml for 32min. The hydrolysate was fractionated by ultrafiltration, and peptide with the highest ACE inhibitory activity was purified from
ISSN:1359-5113
1873-3298
DOI:10.1016/j.procbio.2014.12.030