Structural and functional diversities of the Aplysia Mytilus inhibitory peptide-related peptides

Sasaki, Ken−ichi; Shimizu, Yoriko; Abe, Genbu; Fujisawa, Yuko; Morishita, Fumihiro; Matsushima, Osamu; Furukawa, Yasuo

doi:10.1016/s0196-9781(02)00183-3

Cited by 7 publications

(1 citation statement)

References 14 publications

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“…Like other marine animals, some biactive peptides have been reported from Mytilus mussel protein, such as Mytilus inhibitory peptides [19], antimicrobial peptides [20], and anticoagulant peptide [21]. In addition, an ACE inhibitory peptide has been purified by chromatography method and identified from blue mussel sauce [7].…”

Section: Introductionmentioning

confidence: 99%

Preparation of ACE Inhibitory Peptides fromMytilus coruscusHydrolysate Using Uniform Design

Cheng

Shi

2013

BioMed Research International

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The angiotensin-I-converting enzyme (ACE) inhibitory peptides from mussel, Mytilus coruscus, were investigated and the variable factors, protease concentration, hydrolysis time, pH, and temperature, were optimized using Uniform Design, a new statistical experimental method. The results proved that the hydrolysate of alkali proteases had high ACE-inhibitory activity, especially the alkali protease E1. Optimization by Uniform Design showed that the best hydrolysis conditions for preparation of ACE-inhibitory peptides from Mytilus coruscus were protease concentration of 36.0 U/mL, hydrolysis time of 2.7 hours, pH 8.2, and Temperature at 59.5°C, respectively. The verification experiments under optimum conditions showed that the ACE-inhibitory activity (91.3%) were agreed closely with the predicted activity of 90.7%. The amino acid composition analysis of Mytilus coruscus ACE-inhibitory peptides proved that it had high percent of lysine, leucine, glycine, aspartic acid, and glutamic acid.

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