A peptidomic approach to study the contribution of added casein proteins to the peptide profile in Spanish dry-fermented sausages

Mora, Leticia; Escudero, Elizabeth; Aristoy, M‐Concepción

doi:10.1016/j.ijfoodmicro.2015.05.022

Cited by 39 publications

(29 citation statements)

References 38 publications

(16 reference statements)

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“…Regarding the amino acid composition, Glycine and Proline were the two main hydrophobic amino acids present in the peptide sequences identified in AHP ( Table 1 of supplementary material) which is in accordance with the study of Ktari et al (2014) which reported that ACE-inhibitory activity would be related with the number of hydrophobic amino acids present on the peptide sequences probably due to active site of ACE is more accessible by hydrophobic peptides (Lassoued et al, 2016). ACE-inhibitory peptides have also been described by Mora, Escudero, Aristoy and Toldrá (2015) to contain Lysine, Proline or aromatic residues preferably in the three positions closest to the C-terminal site. However, the most abundant amino acids found in RJ peptides were Proline and Serine.…”

Section: Identification Of Ace-inhibitory and Antioxidant Peptides Bysupporting

confidence: 85%

“…The nano LC-MS/MS analysis was done for peptide identification using an Eksigent Nano-LC Ultra 1D Plus system (Eksigent of AB Sciex, CA) coupled to the quadrupole-time-of-flight (Q-ToF) TripleTOF® 5600 system from AB Sciex Instruments (Framingham, MA) that is equipped with a nanoelectrospray ionization source (nano-ESI). Systems parameters were adjusted as previously reported in Mora, Escudero, Aristoy and Toldrá (2015). The AHP fractions and RJ were re-suspended in double distilled water with 0.1% of TFA to obtain a final concentration of 0.2 mg/mL, and 5μl of the supernatant was injected.…”

Section: Peptide Identification By Mass Spectrometrymentioning

confidence: 99%

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Peptide identification in alcalase hydrolysated pollen and comparison of its bioactivity with royal jelly

Maqsoudlou

Mahoonak

Mora

et al. 2019

Food Research International

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Peptides with a similar antioxidant and ACE-inhibitory activity of royal jelly (RJ) generated from Alcalase hydrolysated pollen (AHP) were predicted by Response Surface Methodology (RSM). Later, AHP was prepared and deproteinised to be further analysed using size-exclusion chromatography (SEC). After SEC separation, fractions 49-57, 64-66 and 52-54 of AHP and fractions 43-55 of RJ that showed the highest ACE-inhibitory, DPPH radical scavenging and ferric-reducing power activities, were purified by RP-HPLC. After the separation of fractions 49-57 of AHP, fractions eluting at 3, 4, 5, 37 and 60 min and fractions eluting at 12 to 33 min showed ACE-inhibitory activity higher than 80% whereas fraction eluting at 34 min showed the highest DPPH scavenging activity. 195 peptide sequences were identified by nano-liquid chromatography and mass spectrometry in tandem (nLC-MS/MS). The origins of all identified peptides were herbal proteins and certain similarities with previously described bioactive sequences were discussed.

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Section: Identification Of Ace-inhibitory and Antioxidant Peptides Bysupporting

confidence: 85%

Section: Peptide Identification By Mass Spectrometrymentioning

confidence: 99%

Peptide identification in alcalase hydrolysated pollen and comparison of its bioactivity with royal jelly

Maqsoudlou

Mahoonak

Mora

et al. 2019

Food Research International

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“…As shown in Table 2, numerous BPs have been isolated and identified from fermented meat and meat products. For instance, Mora, Escudero, et al (2015) reported that Spanish dry-fermented sausage fermented by Lb. pentosus and Staphylococcus carnosus before a two-step ripening process (15 to 20 • C for 22 hr and 9 • C for 43 days) could release peptides with ACE-I, antioxidative, antimicrobial, immunomodulating, DPP-IV inhibitory, opioid, and antithrombotic activities.…”

Section: Meatmentioning

confidence: 99%

Bioactive peptides from food fermentation: A comprehensive review of their sources, bioactivities, applications, and future development

Chai

Voo

Chen

2020

Comp Rev Food Sci Food Safe

143

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Bioactive peptides (BPs) are specific protein fragments that exert various beneficial effects on human bodies and ultimately influence health, depending on their structural properties and amino acid composition and sequences. By offering promising solutions to solve diverse health issues, the production, characterization, and applications of food-derived BPs have drawn great interest in the current literature and are of particular interest to the food and pharmaceutical industries. The microbial fermentation of protein from various sources is indubitably a novel way to produce BPs with numerous beneficial health effects. Apart from its lower cost as compared to enzymes, the BPs produced from microbial fermentation can be purified without further hydrolysis. Despite these features, current literature shows dearth of information on the BPs produced from food via microbial fermentation. Hence, there is a strong necessity to explore the BPs obtained from food fermentation for the development of commercial nutraceuticals and functional foods. As such, this review focuses on the production of BPs from different food sources, including the extensively studied milk and milk products, with emphasis on microbial fermentation. The structure-activity (antihypertensive, antioxidant, antimicrobial, opiate-like, anti-inflammatory, anticancer/antiproliferative, antithrombotic, hypolipidemic, hypocholesterolemic, and mineral binding) relationship, potential applications, future development, and challenges of BPs obtained from food fermentation are also discussed.

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“…Peptide identification was done using a nano-liquid chromatography system (Eksigent of AB Sciex, CA) coupled to a quadrupole-time-of-flight (Q-ToF) system (TripleTOF® 5600+, AB Sciex Instruments, Framingham, MA) equipped with a nano-electrospray ionization source (nano-ESI). Systems parameters were adjusted as previously published in Mora et al [15].…”

Section: Identification Of Peptides Using Nesi-lc-ms/msmentioning

confidence: 99%

Peptidomic analysis of bioactive peptides in zebra blenny (Salaria basilisca) muscle protein hydrolysate exhibiting antimicrobial activity obtained by fermentation with Bacillus mojavensis A21

Jemil

Abdelhedi

Mora

et al. 2016

Process Biochemistry

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The present study investigates the antibacterial activity of zebra blenny (Salaria basilisca) protein hydrolysates obtained by fermentation with a proteolytic bacterium, Bacillus mojavensis A21. The hydrolysate exhibited nutritional as well as antibacterial properties. The fermentative zebra blenny protein hydrolysate (FZPH) was fractionated by size exclusion chromatography on a Sephadex G-25 into six major fractions (F1-F6). Fraction F2, which exhibited the highest antibacterial activity against several Gram-positive and Gramnegative bacteria, was further fractionated by reversed-phase high performance liquid chromatography (RP-HPLC). The most active fractions named A and B which exhibited antibacterial activity, were analysed using nano ESI-LC-MS/MS to identify the sequences of the peptides. A total of 28 and 41 peptides, containing 8 to 31 amino acid residues, were identified in sub-fractions A and B, respectively. Further, identified peptides sharing sequences with previously identified peptides were reported. The results of this study suggest that FZPH are good source of natural antimicrobial peptides. Therefore, ZPH could be a beneficial ingredient for nutraceuticals.

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A peptidomic approach to study the contribution of added casein proteins to the peptide profile in Spanish dry-fermented sausages

Cited by 39 publications

References 38 publications

Peptide identification in alcalase hydrolysated pollen and comparison of its bioactivity with royal jelly

Peptide identification in alcalase hydrolysated pollen and comparison of its bioactivity with royal jelly

Bioactive peptides from food fermentation: A comprehensive review of their sources, bioactivities, applications, and future development

Peptidomic analysis of bioactive peptides in zebra blenny (Salaria basilisca) muscle protein hydrolysate exhibiting antimicrobial activity obtained by fermentation with Bacillus mojavensis A21

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