Production and identification of angiotensin I-converting enzyme (ACE) inhibitory peptides from Mediterranean fish discards

Moreno, Pedro J.; Espejo-Carpio, F. Javier; Guadix, Antonio; Guadix, Emilia M.

doi:10.1016/j.jff.2015.06.062

Cited by 52 publications

(35 citation statements)

References 37 publications

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“…; García‐Moreno et al . ). Therefore, we calculated the contents of hydrophobic and aromatic amino acid residues in dulse PE using the primary structures in this study (Fig.…”

Section: Resultsmentioning

confidence: 97%

Structural Properties of Phycoerythrin from DulsePalmaria palmata

Miyabe

Furuta

Takeda

et al. 2016

Journal of Food Biochemistry

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We found that the red alga dulse (Palmaria palmata) contains a lot of proteins, which is mainly composed of phycoerythrin (PE) and the protein hydrolysates showed high angiotensin I converting enzyme (ACE) inhibitory activities. Therefore, we investigated the structure of dulse PE to discuss its structure‐function relationship. We prepared the chloroplast DNA and analyzed the nucleotide sequences encoding PE by cDNA cloning method. It was clarified that dulse PE has α‐ and β‐subunits and they are composed by 164 amino acids (MW: 17,638) and 177 amino acids (MW: 18,407), respectively. The dulse PE contained conserved cysteine residues for chromophore attachment site. On the alignment of amino acid sequences of dulse PE with those of other red algal PE, the sequence identities were very high (81–92%). In addition, we purified and crystallized the dulse PE, and its crystal structure was determined at 2.09 Å resolution by molecular replacement method. The revealed 3D structure of dulse PE which forms an (αβ)6 hexamer was similar to other red algal PEs. Conversely, it was clarified that the dulse PE proteins are rich in hydrophobic amino acid residues (51.0%), especially aromatic amino acid and proline residues. The data imply that the high ACE inhibitory activity of dulse protein hydrolysates would be caused by the specific amino acid composition and sequence of dulse PE. Practical Applications Dulse is an abundant and underused resource, which contains a lot of phycobiliproteins. Then, the dulse protein hydrolysates strongly inhibited the activity of ACE. Therefore, it has the potential to be an ingredient of functional food.

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“…; García‐Moreno et al . ). Therefore, we calculated the contents of hydrophobic and aromatic amino acid residues in dulse PE using the primary structures in this study (Fig.…”

Section: Resultsmentioning

confidence: 97%

Structural Properties of Phycoerythrin from DulsePalmaria palmata

Miyabe

Furuta

Takeda

et al. 2016

Journal of Food Biochemistry

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“…In fact, previous researches have shown that small sized peptides exhibited the strongest ACE-inhibitory activities [6,28]. Garcia-Moreno et al [29] found that Alcalase and Savinase produced the most potent ACEinhibitory hydrolysates from lentil proteins and also showed the highest yield of shorter peptide sequences from all the studied hydrolysates. ACE-inhibitory peptides generally contain short sequences (between 3 -12 amino acids) due to the fact that the lid structure of ACE restrict the access of large and folded peptides to the active site cleft [30].…”

Section: Fractionation Of Shph By Ultrafiltrationmentioning

confidence: 93%

In silico analysis and antihypertensive effect of ACE-inhibitory peptides from smooth-hound viscera protein hydrolysate: Enzyme-peptide interaction study using molecular docking simulation

Abdelhedi

Nasri

Jridi

et al. 2017

Process Biochemistry

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“…Primary structure of proteins can be accessed from online databases such as UniProtKB/Swiss-Prot or NCBI and the identification process can be carried out by using database search engines (e.g., Mascot) (Dallas et al, 2015;Le-Maux et al, 2015). On the other hand, de novo sequencing approach does not require a protein library and deduces peptide amino acid sequence by calculating mass differences between fragments from the tandem mass spectra (Girgih et al, 2014;Garc ıa-Moreno et al, 2015). For that purpose, generally employed programs are Peaks (Marques et al, 2015) and PepSeq (Liu et al, 2015).…”

Section: Removing Bitternessmentioning

confidence: 99%

Peptides: Production, bioactivity, functionality, and applications

Hajfathalian

Ghelichi

Moreno

et al. 2017

Critical Reviews in Food Science and Nutrition

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138

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Production of peptides with various effects from proteins of different sources continues to receive academic attention. Researchers of different disciplines are putting increasing efforts to produce bioactive and functional peptides from different sources such as plants, animals, and food industry by-products. The aim of this review is to introduce production methods of hydrolysates and peptides and provide a comprehensive overview of their bioactivity in terms of their effects on immune, cardiovascular, nervous, and gastrointestinal systems. Moreover, functional and antioxidant properties of hydrolysates and isolated peptides are reviewed. Finally, industrial and commercial applications of bioactive peptides including their use in nutrition and production of pharmaceuticals and nutraceuticals are discussed.

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Production and identification of angiotensin I-converting enzyme (ACE) inhibitory peptides from Mediterranean fish discards

Cited by 52 publications

References 37 publications

Structural Properties of Phycoerythrin from DulsePalmaria palmata

Structural Properties of Phycoerythrin from DulsePalmaria palmata

In silico analysis and antihypertensive effect of ACE-inhibitory peptides from smooth-hound viscera protein hydrolysate: Enzyme-peptide interaction study using molecular docking simulation

Peptides: Production, bioactivity, functionality, and applications

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