Antibacterial peptides from barbel muscle protein hydrolysates: Activity against some pathogenic bacteria

Sila, Assaâd; Nedjar‐Arroume, Naïma; Hedhili, Karima; Châtaigné, Gabrielle; Balti, Rafik; Nasri, Monçef; Dhulster, Pascal; Bougatef, Ali

doi:10.1016/j.lwt.2013.07.021

Cited by 66 publications

(48 citation statements)

References 30 publications

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“…Similar results were reported in our previous work (Jemil et al, 2016a), in which the second fraction from the G25 separation profile of zebra blenny protein hydrolysate, was found to inhibit five different strains with MIC values ranging from 0.077 to 0.311 mg/mL. Additionally, Sila et al (2014) showed that only three fractions among six obtained after fractionation of barbel protein hydrolysate on a Sephadex G-25 gel filtration chromatography are active and fraction F2 was the most active against tested bacterial species.…”

Section: Fractionation Of Sph By Size Exclusion Chromatographysupporting

confidence: 91%

Novel bioactive peptides from enzymatic hydrolysate of Sardinelle ( Sardinella aurita ) muscle proteins hydrolysed by Bacillus subtilis A26 proteases

Jemil

Abdelhedi

Nasri

et al. 2017

Food Research International

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Sardinelle protein hydrolysate (SPH), prepared by treatment with Bacillus subtilis A26 proteases, was found to exhibit antibacterial, antioxidant and ACE-inhibitory activities. SPH, with a degree of hydrolysis of 4%, was fractionated by size exclusion chromatography on a Sephadex G-25 into five major fractions (F1-F5). F2, which exhibited the highest antibacterial and ACE-inhibitory activities, and F4, which exhibited the highest antibacterial and antioxidant activities, were further fractionated by reverse phase-high performance liquid chromatography (RP-HPLC) and then analysed using nano-ESI-LC-MS/MS to identify the sequences of peptides. Eight peptides were identified in the sub-fraction F2-A, nine peptides in the sub-fraction F4-B, and 45 peptides in F4-C. Identified peptides were found to share sequences with previously described bioactive peptides based on Biopep database. The results of this study suggest that SPH is a good source of natural bioactive peptides. Hence, it can be used as a potential ingredient in nutraceutical field.

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Section: Fractionation Of Sph By Size Exclusion Chromatographysupporting

confidence: 91%

Novel bioactive peptides from enzymatic hydrolysate of Sardinelle ( Sardinella aurita ) muscle proteins hydrolysed by Bacillus subtilis A26 proteases

Jemil

Abdelhedi

Nasri

et al. 2017

Food Research International

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“…Savinase R contains both endoprotease and exoprotease activities, which offer the ability to achieve higher deproteinization degree. Similar compositions were reported for barbel protein hydrolysates [24]. In the same context, Garcia-Mora et al [20] investigated the effectiveness of Alcalase R and Savinase R for the simultaneous release of bioactive peptides and phenolics with antioxidant, angiotensin I converting enzyme (ACE) inhibitory and anti-inflammatory activities.…”

Section: Preparation and Characterization Of Shrimp Waste Protein Hydmentioning

confidence: 65%

Identification and molecular docking of novel ACE inhibitory peptides from protein hydrolysates of shrimp waste

Krichen

Sila

Caron

et al. 2018

Engineering in Life Sciences

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The effect of enzymatic hydrolysis by Savinase on the interfacial properties and antihypertensive activity of shrimp waste proteins was evaluated. The physicochemical characterization, interfacial tension, and surface characteristics of shrimp waste protein hydrolysates (SWPH) using different enzyme/substrate (E/S) (SWPH5 (SWPH using E/S = 5), SWPH15 (SWPH using E/S = 15), and SWPH40 (SWPH using E/S = 40)) were also studied. SWPH5, SWPH15, and SWPH40 had an isoelectric pH around 2.07, 2.17, and 2.54 respectively. SWPH5 exhibited the lowest interfacial tension (68.96 mN/m) followed by SWPH15 (69.36 mN/m) and SWPH40 (70.29 mN/m). The in vitro ACE inhibitory activity of shrimp waste protein hydrolysates showed that the most active hydrolysate was obtained using an enzyme/substrate of 15 U/mg (SWPH15). SWPH15 had a lower IC50 value (2.17 mg/mL) than that of SWPH5 and SWPH40 (3.65 and 5.7 mg/mL, respectively). This hydrolysate was then purified and characterized. Fraction F1 separated by Sephadex G25 column which presents the best ACE inhibition activity was then separated by reversed‐phase high performance liquid chromatography. Four ACE inhibitory peptides were identified and their molecular masses and amino acid sequences were determined using ESI–MS and ESI–MS/MS, respectively. The structures of the most potent peptides were SSSKAKKMP, HGEGGRSTHE, WLGHGGRPDHE, and WRMDIDGDIMISEQEAHQR. The structural modeling of anti‐ACE peptides from shrimp waste through docking simulations results showed that these peptides bound to ACE with high affinity.

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“…We recently isolated 10 new antibacterial peptides from the barbel muscle proteins and their molecular masses and amino acid sequences were determined using ESI-MS and ESI-MS/ MS, respectively (Sila et al, 2014). However, the mode of action of these peptides has not yet been investigated.…”

Section: Antibacterial Activitymentioning

confidence: 99%

“…Barbel protein hydrolysate was obtained by using added enzyme (Alcalase ® ) under controlled digestion. The amino acid sequences of theses antibacterial peptides were identified as Gly-Val-His, Trp-His-Arg, Trp-His-Phe, Pro-Pro-Ser-Ser, Ala-AlaAla-Leu, Ala-Ala-Gly-Gly-Val, Ala-Ala-Val-Lys-Met, Ala-Ser-SerSer (Sila et al, 2014).…”

Section: Introductionmentioning

confidence: 99%

Antibacterial activity of new peptides from barbel protein hydrolysates and mode of action via a membrane damage mechanism against Listeria monocytogenes

Sila

Hedhili

Przybylski

et al. 2014

Journal of Functional Foods

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Antibacterial peptides from barbel muscle protein hydrolysates: Activity against some pathogenic bacteria

Cited by 66 publications

References 30 publications

Novel bioactive peptides from enzymatic hydrolysate of Sardinelle ( Sardinella aurita ) muscle proteins hydrolysed by Bacillus subtilis A26 proteases

Novel bioactive peptides from enzymatic hydrolysate of Sardinelle ( Sardinella aurita ) muscle proteins hydrolysed by Bacillus subtilis A26 proteases

Identification and molecular docking of novel ACE inhibitory peptides from protein hydrolysates of shrimp waste

Antibacterial activity of new peptides from barbel protein hydrolysates and mode of action via a membrane damage mechanism against Listeria monocytogenes

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