Purification and identification of peptides with high angiotensin-I converting enzyme (ACE) inhibitory activity from honeybee pupae (Apis mellifera) hydrolysates with in silico gastrointestinal digestion

Yang, Xiaoxue; Chen, Kangni; Liu, Huaigao; Zhang, Yuqi; Luo, Yongkang

doi:10.1007/s00217-018-03223-7

Cited by 15 publications

(8 citation statements)

References 35 publications

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“…The ACE inhibition rate of alcalase hydrolysate IC 50 (5.7 ± 0.15 mg/mL) was the lowest, followed by neutrase hydrolysates IC 50 (6.5 ± 0.13 mg/mL) and flavourzyme hydrolysate IC 50 (6.1 ± 0.11 mg/mL); the ACE inhibition rate of papain IC 50 (6.8 ± 0.16 mg/mL) was the highest. The ACE inhibition rate of the peptides was strongly linked to their molecular weight [15]. Low-molecular-weight peptides are more impressionable and have a critical effect in their ACE-inhibitory activity because they are conducive to combination with the target molecule.…”

Section: Distribution Of Molecular Weights and Ace-inhibitory Activit...mentioning

confidence: 99%

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Purification and Identification of a Novel Angiotensin Converting Enzyme Inhibitory Peptide from the Enzymatic Hydrolysate of Lepidotrigla microptera

Dai

Jin

2022

Foods

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In this study, Lepidotrigla microptera were hydrolyzed with four different proteolytic enzymes (Papain, neutrase, flavourzyme, and alcalase), and their distribution of molecular weights and ACE-inhibitory activity were tested. The alcalase hydrolysates showed the maximum ACE-inhibitory activity. A novel ACE-inhibitory peptide was isolated and purified from Lepidotrigla microptera protein hydrolysate (LMPH) using ultrafiltration, gel filtration chromatography, and preparative high performance liquid chromatography (prep-HPLC). The amino acid sequence of the purified peptide was identified as Phe-Leu-Thr-Ala-Gly-Leu-Leu-Asp (DLTAGLLE), and the IC50 value was 0.13 mg/mL. The ACE-inhibitory activity of DLTAGLLE was stable across a range of temperatures (<100 °C) and pH values (3.0–11.0) and retained after gastrointestinal digestion. DLTAGLLE was further identified as a noncompetitive inhibitor by Lineweaver–Burk plot. The molecular docking simulation showed that DLTAGLLE showed a high binding affinity with ACE sites by seven short hydrogen bonds. As the first reported antihypertensive peptide extracted from alcalase hydrolysate of Lepidotrigla microptera, DLTAGLLE has the potential to develop functional food or novel ACE-inhibitor drugs.

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Section: Distribution Of Molecular Weights and Ace-inhibitory Activit...mentioning

confidence: 99%

“…Edible proteins from plant or animal sources are a focus for the development of novel ACE-inhibitory peptides. Up to now, active peptides with ACE-inhibitory activity have been released from honeybee pupae [15], cassia obtusifolia seeds [16], and red alga [17].…”

Section: Introductionmentioning

confidence: 99%

Purification and Identification of a Novel Angiotensin Converting Enzyme Inhibitory Peptide from the Enzymatic Hydrolysate of Lepidotrigla microptera

Dai

Jin

2022

Foods

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“…96,107 Besides, A. mellifera peptides (generated by neutrase hydrolysis) with ACE inhibition activity were subjected to in silico digestion to simulate the effectiveness of peptides after human digestion. 110…”

Section: Bioinformatic (In Silico) Tools For Insect Peptides Predictionmentioning

confidence: 99%

Current state of insect proteins: extraction technologies, bioactive peptides and allergenicity of edible insect proteins

Ma,

Mondor,

Goycoolea Valencia

et al. 2023

Food Funct.

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“…The production of bioactive peptides resulting from the digestion of A. mellifera larvae and pupae proteins was demonstrated (Tables 1 and 2) by two studies using in vitro and/or in silico approaches, respectively [37,38]. In the first report, one potential antihypertensive peptide (#84, Table 2) was isolated and identified after the hydrolysis of larva proteins through in vitro GI digestion [37].…”

Section: Apis Melliferamentioning

confidence: 99%

“…In the first report, one potential antihypertensive peptide (#84, Table 2) was isolated and identified after the hydrolysis of larva proteins through in vitro GI digestion [37]. In the second report, three novel antihypertensive peptides (#85, #86, #87, Table 2) from pupae hydrolysates were found and evaluated for their resistance to proteolysis through a simulated in silico GI digestion [38]. The antihypertensive properties of the four individual peptides, identified in the two studies, were evaluated through in vitro ACE inhibitory assays.…”

Section: Apis Melliferamentioning

confidence: 99%

Edible Insects as a Novel Source of Bioactive Peptides: A Systematic Review

Teixeira

Villa

Costa

et al. 2023

Foods

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The production of food and feed to meet the needs of the growing world’s population will soon become a serious challenge. In search for sustainable solutions, entomophagy is being proposed as an alternative source of proteins, with economic and environmental advantages when compared to meat. Edible insects are not only a valuable source of important nutrients, but their gastrointestinal digestion also originates small peptides with important bioactive properties. The present work intends to provide an exhaustive systematic review on research articles reporting bioactive peptides identified from edible insects, as demonstrated by in silico, in vitro, and/or in vivo assays. A total of 36 studies were identified following the PRISMA methodology, gathering 211 potentially bioactive peptides with antioxidant, antihypertensive, antidiabetic, antiobesity, anti-inflammatory, hypocholesterolemia, antimicrobial, anti-severe acute respiratory syndrome coronavirus type 2 (SARS-CoV-2), antithrombotic, and immunomodulatory properties, originated from the hydrolysates of 12 different insect species. From these candidates, the bioactive properties of 62 peptides were characterized in vitro and 3 peptides were validated in vivo. Data establishing the scientific basis of the health benefits associated with the consumption of edible insects can be a valuable contribution to overcoming the cultural issues that hinder the introduction of insects in the Western diet.

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Purification and identification of peptides with high angiotensin-I converting enzyme (ACE) inhibitory activity from honeybee pupae (Apis mellifera) hydrolysates with in silico gastrointestinal digestion

Cited by 15 publications

References 35 publications

Purification and Identification of a Novel Angiotensin Converting Enzyme Inhibitory Peptide from the Enzymatic Hydrolysate of Lepidotrigla microptera

Purification and Identification of a Novel Angiotensin Converting Enzyme Inhibitory Peptide from the Enzymatic Hydrolysate of Lepidotrigla microptera

Current state of insect proteins: extraction technologies, bioactive peptides and allergenicity of edible insect proteins

Edible Insects as a Novel Source of Bioactive Peptides: A Systematic Review

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