Preparation and identification of angiotensin I-converting enzyme inhibitory peptides from sweet potato protein by enzymatic hydrolysis under high hydrostatic pressure

Sweet potato protein hydrolysates (SPPH) with angiotensin I-converting enzyme (ACE) inhibitory activity were prepared by papain, pepsin and alcalase under high hydrostatic pressure (HHP, 100–300 MPa). HHP significantly increased degree of hydrolysis (DH), nitrogen recovery (NR) and molecular weight (MW) <3 kDa fractions contents of SPPH by all three enzymes (P < 0.05). MW < 3 kDa peptide fractions from SPPH by alcalase under 100 MPa showed the highest ACE inhibitory activity (IC₅₀ value 32.24 µg mL⁻¹), and was subjected to purification and identification by semi-preparative RP-HPLC and LC-MS/MS. Fifty-four peptides ranged from 501.28 to 1958.88 Da with 5–18 amino acids were identified and matched sporamin A and B sequences. Five identified peptides with sequences of VSAIW, AIWGA, FVIKP, VVMPSTF and FHDPMLR displayed good ACE inhibitory activity with the contribution of Val, Trp, Phe and Arg. Thus, SPPH by enzymatic hydrolysis under HHP can be potentially used in functional food.     

Sweet potato protein hydrolysates: antioxidant activity and protective effects on oxidative DNA damage

In this study, sweet potato protein (SPP) hydrolysates were prepared by six enzymes (alcalase, proleather FG‐F, AS1.398, neutrase, papain and pepsin). The antioxidant activities and protective effect against oxidative DNA damage of SPP hydrolysates were investigated. Alcalase hydrolysates exhibited the highest hydroxyl radical‐scavenging activity (IC₅₀ 1.74 mg mL^?1) and Fe²⁺‐chelating ability (IC₅₀ 1.54 mg mL^?1) (P < 0.05). Compared with other five hydrolysates, the hydrolysates obtained by alcalase had the most abundant <3‐kDa fractions. In addition, below 3‐kDa fractions of alcalase hydrolysates showed the highest antioxidant activities and protective effects against DNA damage through both scavenging hydroxyl radicals and chelating Fe²⁺, which was probably because of the increase in several antioxidant amino acids, such as His, Met, Cys, Tyr and Phe, as well as the hydrophobic amino acids. The results suggested that enzymatic hydrolysis could be used as an effective technique to produce high value‐added peptides products from SPP.     

The influence of heat treatment of chickpea seeds on antioxidant and fibroblast growth‐stimulating activity of peptide fractions obtained from proteins digested under simulated gastrointestinal conditions

This study presents the effect of heat treatment of chickpea seeds on biological activity of peptides obtained by in vitro gastrointestinal digestion. The most significant antiradical activity against ABTS^+? expressed as IC₅₀ value was observed for 3.5‐ to 7‐kDa peptide fraction from TC hydrolysate (41.01 μg mL^?1). In turn, peptide fraction of 3.5–7.0 kDa obtained from raw chickpea seeds hydrolysate showed the highest antiradical activity against DPPH^? and Fe²⁺ chelating activity with IC₅₀ value of 20.94 and 52.53 μg mL^?1, respectively. The highest Cu²⁺ chelating activity was observed for peptides obtained from TC hydrolysate (IC₅₀ = 56.60 μg mL^?1). Peptide fraction <3.5 kDa from TC hydrolysate demonstrated the most significant reducing power (0.362 A₇₀₀/μg mL^?1). The peptide fraction of 3.5–7 kDa from TC hydrolysate also showed the highest fibroblast growth‐stimulating activity. These results indicated that the heat treatment process has no significant effect on antiradical activity against DPPH^? and Fe²⁺ chelating ability of peptides.     

Production and characterisation of antioxidant peptides from sweet potato protein by enzymatic hydrolysis with radio frequency pretreatment

Effect of radio frequency (RF at 70, 80 and 90 °C) pretreatment on production and characterisation of sweet potato protein hydrolysates (SPPH) prepared using Alcalase (ALC), Protease (PRO) and the combination of ALC + PRO was investigated. RF highly improved degree of hydrolysis (DH) and enhanced antioxidant activity of all SPPH produced by ALC, PRO and the combination as compared to traditional water bath (WB) heating pretreatment (P < 0.05). RF significantly increased molecular weight (MW) <3 kDa peptide fraction from SPPH produced by ALC, and MW <3 kDa peptide fraction from RF80- and RF90-pretreated samples has higher antioxidant activity. Diverse peptides in MW <3 kDa fractions with RF80 and RF90 pretreatments were identified using LC–QTOF–MS/MS, which matched the sequences of sporamins and contained antioxidant amino acids Trp, Tyr, Met, Phe and/or His. There is a great potential application of using SPPH in functional foods as a novel ingredient.     

Effects of physicochemical factors and in vitro gastrointestinal digestion on antioxidant activity of R‐phycoerythrin from red algae Bangia fusco‐purpurea

R‐phycoerythrin (R‐PE) was purified from the red algae Bangia fusco‐purpurea after 35–50% ammonium sulphate fractionation followed by ion‐exchange column chromatography on DEAE‐Sepharose, resulting in a purity (A₅₆₅/A₂₈₀) ratio of 5.1. The circular dichroism spectroscopy results suggested that the structure of R‐PE is predominately helical. The antioxidant activity of R‐PE was studied and revealed changes in conformation and antioxidant activity at different temperatures and pH values. After in vitro‐simulated gastrointestinal (GI) digestion of R‐PE, the scavenging activity of ABTS radical (EC₅₀, 769.9 μg mL^?1), DPPH radical (EC₅₀, 421.9 μg mL^?1), hydroxyl radical (EC₅₀, 32.4 μg mL^?1) and reducing power (A₇₀₀ = 0.5, 625.8 μg mL^?1) were measured. Gel filtration chromatography analysis showed that the molecular weight distribution of the final GI digest that still contained high antioxidant activity was <3 kDa. Our present results indicate that digestion‐resistant antioxidant peptides of R‐PE may be obtained by in vitro GI proteinases degradation.     

Separation of angiotensin I‐converting enzyme inhibitory peptides from bovine connective tissue and their stability towards temperature,pH and digestive enzymes

Bovine collagen was isolated from connective tissue, a by‐product in the meat processing industry and characterised by SDS‐PAGE. Alcalase and papain were employed to generate collagen hydrolysates with different degree of hydrolysis (DH). In vitro angiotensin I‐converting enzyme (ACE) inhibitory activities were evaluated and the two most potent hydrolysates from each enzyme were separated by two‐step purification. Both alcalase‐catalysed and papain‐catalysed hydrolysates exhibited strong ACE inhibitory capacities with IC₅₀ values of 0.17 and 0.35 mg mL^?1, respectively. Purification by ion‐exchange chromatography and gel filtration chromatography revealed higher ACE inhibitory activities in one fraction from each enzyme with IC₅₀ values of 3.95 and 7.29 μg mL^?1. These peptide fractions were characterised as 6‐12 amino acid residues by MALDI‐TOF/MS. The peptides retained their activity (>90%) after exposure to processing temperature and pH and in vitro simulated gastrointestinal digestion. The present results demonstrated that collagen peptides can be utilised for developing high value‐added ingredients, for example ACE inhibitory peptides.     

Improvement of thermal,microwave and ultrasonication pretreatment on the production of antioxidant peptides from sweet potato protein via in vitro gastrointestinal digestion

Effects of thermal (boiling, steaming and autoclaving), microwave and ultrasonication pretreatments on the production of sweet potato protein hydrolysates (SPPH) through in vitro gastrointestinal digestion (GID) were investigated. All pretreatments significantly increased the degree of hydrolysis (DH), antioxidant activities and molecular weight (MW) <3 kDa peptide fractions contents of SPPH in the order of autoclaving > microwave, steaming > boiling > ultrasonication (P < 0.05). Correlation analysis between peptides content and antioxidant activity suggested that antioxidant activity of SPPH mainly attributed to MW <3 kDa peptides. Diverse peptides ranged from 487.24 to 1477.74 Da with 7–13 amino acids were identified in the MW <3 kDa peptides fraction with autoclaving pretreatment and matched sporamins A, A precursor and B sequences from LC–QTOF–MS/MS analysis. Conformational structures of nine peptides were predicted with well-known antioxidant amino acids. There is a high potential for SPPH used as a functional supplement in food system.     

In vitro inhibitory effects of cranberry bean (Phaseolus vulgaris L.) extracts on aldose reductase, α‐glucosidase and α‐amylase

The in vitro inhibitory activities of different seed extracts prepared from cranberry bean mutant SA‐05 and its wild‐type variety Hwachia against aldose reductase, α‐glucosidase and α‐amylase were examined. The results indicated that the polyphenolics‐rich extracts obtained using 800 g kg^?1 methanol and 500 g kg^?1 ethanol demonstrated inhibitory activities against aldose reductase (IC₅₀ of 0.36–0.46 mg mL^?1) and α‐glucosidase (IC₅₀ of 1.32–1.94 mg mL^?1). The 500 g kg^?1 ethanol extracts also showed α‐amylase inhibitory activities (IC₅₀ of 70.11–80.22 μg mL^?1). Subsequent extracts, prepared further with NaCl and H₂O from precipitates of 800 g kg^?1 methanol or 500 g kg^?1 ethanol extracts, exhibited potent α‐amylase inhibitory activities (IC₅₀ of 17.68–38.68 μg mL^?1). A combination of 500 g kg^?1 ethanol extraction plus a subsequent H₂O extraction produced highest polyphenolics and α‐amylase inhibitors. The SA‐05 α‐amylase inhibitor extracts showed greater inhibitory activities than that of Hwachia. Thus, cranberry bean mutant SA‐05 is an advantageous choice for producing anti‐hyperglycaemic compounds.     

Process optimisation and physicochemical characterisation of enzymatic hydrolysates of proteins from co‐products of Atlantic Salmon (Salmo salar) and Yellowtail Kingfish (Seriola lalandi)

The aim of this study was to develop an enzymatic hydrolysis process of protein co‐products for two major commercial fish species in Australia: Atlantic salmon (AS) and Yellowtail kingfish (YTK). The outcomes are to produce high protein recovery of fish protein hydrolysates within controlled molecular weight ranges that display enhanced physicochemical properties of oil binding and emulsification. Three enzymes (Flavourzyme, Neutrase and Alcalase) were applied to processing co‐products. Protein recovery and physicochemical properties were evaluated with increasing hydrolysis time from 30 min to 180 min and ratio of enzyme to substrate (E/S) from 0.5% to 3.0%. In order to achieve a product with optimum emulsifying capacity (50 ± 0.6 m² g^?1), an E/S ratio of 0.6–1.3% Flavourzyme was applied for 30–111 min with a protein recovery of 55%; in order to achieve a product with optimum oil‐binding capacity (8.3 ± 0.3 g oil g hydrolysates^?1), an E/S ratio of 2.3–3.0% Flavourzyme was applied for 25–64 min with a protein recovery of 70%. YTK protein hydrolysates were further membrane‐fractionated into five fractions (>100 kDa, 50–100 kDa, 30–50 kDa, 10–30 kDa and <10 kDa), and of these, the 10–30 kDa exhibited the best properties of oil binding (19 ± 0.3 g oil g hydrolysates^?1) and emulsification (57 ± 0.7 m² g^?1). These results demonstrate the importance of enzymatic hydrolysis of seafood co‐products into high‐value ingredients for food products and processing.     

Identification and characterization of antioxidant peptides from sweet potato protein hydrolysates by Alcalase under high hydrostatic pressure

Sweet potato protein hydrolysates (SPPH) were generated by Alcalase under high hydrostatic pressure (HHP, 100, 200 and 300 MPa). HHP significantly improved the degree of hydrolysis (DH) and antioxidant activity, and increased the < 3 kDa fraction content of SPPH (P < 0.05). SPPH by Alcalase at 300 MPa for 60 min exhibited the highest DH and antioxidant activity and was separated into three fractions by ultrafiltration. The most active fraction FIII (< 3 kDa) was further separated into fifty four fractions by semi-preparative RP-HPLC and measured using the ORAC assay. In addition, more active fractions were examined by LC–MS/MS, and diverse peptides were identified, matching sequences of Sporamins A and B. To evaluate the structure–activity dependences, twenty sequences were synthesized, of which the antioxidant activity was assessed. Five peptides showed good activity: HDSASGQY ≥ YYMVSA ≥ HDSESGQY ~ YYIVS ~ RYYDPL, with the contribution of His and Tyr.Industrial relevanceThis study will give a novel technique for using industrial waste slurry, a byproduct in the process of sweet potato starch manufacturing, which contains various bioactive components (such as protein, minerals, etc.) since most of them are normally discarded. The present study is focused on assessing the effects of enzymatic hydrolysis by Alcalase under high hydrostatic pressure (HHP) on the release of antioxidant peptides from sweet potato protein (SPP). The results of this work provide a potential application of enzymatic hydrolysis assisted by HHP on the development of ingredients from SPP in functional foods.     

Phytosterols in banana (Musa spp.) flower inhibit α‐glucosidase and α‐amylase hydrolysations and glycation reaction

Three phytosterols were isolated from Musa spp. flowers for evaluating their capabilities in inhibiting glucosidase and amylase activities and glycation of protein and sugar. The three phytosterols were identified as β‐sitosterol (PS1), 31‐norcyclolaudenone (PS2) and (24R)‐4α, 14α, 4‐trimethyl‐5α‐cholesta‐8, 25(27)‐dien‐3β‐ol (PS3). IC₅₀ values (the concentration of inhibiting 50% of enzyme activity) of PS1, PS2 and PS3 against α‐glucosidase were 283.67, 11.33 and 43.10 μg mL^?1, respectively. For inhibition of α‐amylase, the IC₅₀ values of PS1, PS2 and PS3 were 52.55, 76.25 and 532.02 μg mL^?1, respectively. PS1 was an uncompetitive inhibitor against α‐amylase with K_m at 5.51 μg mL^?1, while PS2 and PS3 exhibited a mixed‐type inhibition with K_m at 52.36 and 2.49 μg mL^?1, respectively. PS1 and PS2 also significantly inhibited the formation of advanced glycation end products (AGEs) in a BSA–fructose model. The results suggest that banana flower could possess the capability in prevention of the diseases associated with abnormal blood sugar and AGEs levels, such as diabetes.     

Chemical composition,antioxidant activity and anti‐lipase activity of Origanum vulgare and Lippia turbinata essential oils

This study reported the chemical composition, phenolic content, antioxidant and anti‐lipase activity of oregano and Lippia essential oils. The major compounds found in oregano essential oil were γ‐terpinene (32.10%), α‐terpinene (15.10%), p‐cymene (8.00%) and thymol (8.00%). In Lippia essential oil, α‐limonene (76.80%) and 1,8‐cineole (4.95%) represented the major compounds. Oregano essential oil had higher phenolic content (12.47 mg gallic acid mL^?1) and DPPH scavenging activity (IC₅₀ 0.357 μg mL^?1) than Lippia essential oil (7.94 mg gallic acid mL^?1 and IC₅₀ 0.400 μg mL^?1, respectively). Both essential oils had similar antioxidant indexes (about 1.2) determined by Rancimat. Moreover, oregano essential oil had also higher anti‐lipase activity (IC₅₀ 5.09 and 7.26 μg mL^?1). Higher phenolic content in the essential oils was related with higher scavenging and anti‐lipase activities. Oregano and Lippia essential oils could be used as natural antioxidants on food products.     

Angiotensin I‐converting enzyme inhibitory peptides FQPSF and LKYPI identified in Bacillus subtilis A26 hydrolysate of thornback ray muscle

Angiotensin I‐converting enzyme (ACE) inhibitory peptides have been searched in thornback ray (Raja clavata) muscle hydrolysed with Bacillus subtilis A26 proteases until a hydrolysis degree of 18.35%. The hydrolysate showed an IC₅₀ of 0.83 mg mL^?1. To identify peptides responsible for this activity, the extract was eluted through size‐exclusion chromatography and fractions collected. The highest ACE inhibitory activity was found for fractions F2 and F3 which had IC₅₀ of 0.42 and 0.51 mg mL^?1, respectively. These fractions were analysed by nano‐liquid chromatography coupled to tandem mass spectrometry (nLC‐MS/MS). A total of 131 and 108 peptide sequences mainly derived from actin, myosin heavy chain and procollagen alpha 1 chain proteins were identified in fractions F2 and F3, respectively. FQPSF and LKYPI showed the best results with an IC₅₀ of 12.56 and 27.07 μM, respectively. These results prove the potential of thornback ray muscle hydrolysate as a source of ACE inhibitory peptides.     

Optimisation of antioxidant hydrolysate production from sweet potato protein and effect of in vitro gastrointestinal digestion

In this study, response surface methodology (RSM) was applied to optimise antioxidant hydrolysate production from sweet potato protein (SPP). The effects of enzyme‐to‐substrate ratio, pH value and reaction temperature on ·OH radical scavenging activity and Fe²⁺‐chelating activity of antioxidant hydrolysates from SPP were investigated. The maximum ·OH radical scavenging activity (40.10%) and Fe²⁺‐chelating activity (74.37%) of SPP hydrolysates (SPPH) were obtained at an enzyme‐to‐substrate ratio of 4%, pH value of 7.8 and reaction temperature of 57 °C, which was in agreement with the predicted value (40.11% and 74.83%, respectively) estimated by RSM. The simulated in vitro gastrointestinal digestion (GID) dramatically modified molecular weights distribution, increased peptide (<3 kDa) concentration and highly retained antioxidant activity of SPPH, indicating potentially utilisation of SPPH as a functional supplement in food system.     

Antimicrobial activities of high molecular weight water‐soluble chitosans against selected gram‐negative and gram‐positive foodborne pathogens

Antimicrobial activities of high molecular weight water‐soluble chitosans (HMWWS) against selected Gram‐negative and Gram‐positive foodborne pathogens (initial inoculation of ca. 6.5 Log CFU mL^?1) were evaluated. Chitosans with 789 kDa and/or 1017 kDa were dissolved in aspartic acid (AS) to obtain 1–4% w/v solutions. Among HMWWS, only 4% 789 kDa AS chitosan reduced E. coli counts by 2 Log CFU mL^?1 from 7.33 at 0 h to 5.16 Log CFU mL^?1 at 96 h, and they were not effective against S. Typhimurium. Depending on the concentrations, HMWWS completely inhibited V. cholerae, V. vulnificus and V. parahaemolyticus as well as B. cereus and L. monocytogenes after 48 h or 96 h of incubation. Compared with the control (no HMWWS), 2% or 3% 1017 kDa AS chitosans showed about 3 Log CFU mL^?1 lower (4.72–4.86 vs. 7.71) for S. aureus at 96 h of incubation.     

Phytochemicals content,antioxidant and hypoglycaemic activities of commercial nutmeg mace (Myristica fragrans L.) and pimento (Pimenta dioica (L.) Merr.)

Commercially dried powder of nutmeg mace (Myristica fragrans) and pimento (Pimenta dioica) spices was investigated for their high performance liquid chromatography phenolic profile and their antioxidant and hypoglycaemic properties by α‐amylase and α‐glucosidase inhibition tests. Generally, mace showed the most promising activity. An interesting protection of lipid peroxidation with an IC₅₀ value of 7.7 μg mL^?1 was found. A significant result was also obtained in ferric reducing ability power assay if compared to the positive control butylated hydroxytoluene (IC₅₀ value of 68.7 μg mL^?1 vs. 63.2 μg mL^?1, respectively). Mace also exhibited the highest carbohydrate‐hydrolysing enzyme inhibitory activity with IC₅₀ values of 62.1 and 75.7 μg mL^?1 against α‐amylase and α‐glucosidase, respectively. Overall, these results support the use of these spices not only as flavouring agent but also as food preservative and functional ingredients.     

Bifurcaria bifurcata: a key macro‐alga as a source of bioactive compounds and functional ingredients

The aim of this work was to study the proximate composition and the bioactive profile of Bifurcaria bifurcata. It contains 73.31 ± 0.69% of moisture, 8.57 ± 0.11 g per 100 g dry weight (d.w.) of protein, 5.81 ± 0.14 g per 100 g d.w. of lipid content and 30.15 ± 0.00 g per 100 g d.w. of ash. The polyunsaturated fatty acids were the most abundant fatty acid (FA), accounting for 2426.56 mg per 100 g which represents 41.77% of the total FA. The methanolic fraction showed high quantity of polyphenols (220.01 ± 0.010 phloroglucinol equivalents g^?1 extract), DPPH radical reduction capacity (EC₅₀:58.82 μg mL^?1) and oxygen radical absorbent capacity (3151.35 ± 119.33 μmol Trolox equivalents g^?1 extract). The highest antimicrobial effect was observed against Pseudomonas aeruginosa (11.3 ± 1.5 mm) and Saccharomyces cerevisiae (IC₅₀:17.07 μg mL^?1) induced by methanolic and dichloromethane fractions, respectively. Dichloromethane fraction revealed the highest antitumor activity on Caco‐2 and HepG‐2 cells. Bifurcaria bifurcata can be a promising source of bioactive compounds and functional ingredients.     

Phosphorylation of peptidoglycan from Lactobacillus acidophilus and its immunoregulatory function

Peptidoglycan (PG) is available from a wide variety of lactic acid bacteria (LAB) and is the main structure of cell wall components. Phosphorylated modification would bring new properties such as the potential antioxidant activities and antiviral capability to an organic molecule. In the present work, small molecular fragments of PG (derived from Lactobacillus acidophilus) hydrolysed by mutanolysin were phosphorylated under optimal conditions. P‐PG had a monomer molecular structure of GlcNAC[PO₃]–MurNAC–Ala–Glu–Lys–Ala, with a molecular mass of 884 Da and a phosphorus content of 8.9%. P‐PG displayed some immunoregulatory activity in lipopolysaccharides (LPS) stimulated RAW 264.7 macrophages. Compared with the LPS‐stimulated group, the addition of P‐PG inhibited the secretion of GM‐CSF, TNF‐α and IL‐1 in a dose‐dependent manner. The effect of 50 μg mL^?1 of P‐PG was more significant than 50 μg mL^?1 of PG. Lower fluorescence of lysosomes was observed in P‐PG‐treated RAW 264.7 cells may also reveal some immune defence function in the LPS‐induced macrophages.     

Antioxidant activities of the fractionated protein hydrolysates from heat stable defatted rice bran

The hydrolysates from heat stable rice bran (HSDRB) treated by Alcalase 2.4L and Protease 500G were desalted and fractionated by hydrophobicity using a nonpolar, styrene divinylbenzene resin and macroporous adsorption resin DA201‐C. The antioxidant activities of HSDRB hydrolysates (HSDRBH) eluted by 25%, 50%, 75% and 100% ethanol were investigated using 2, 2‐di (4‐tertoctylphenyl)‐1‐picrylhydrazyl free radical‐scavenging activity assay, reducing power assay, ferrous ion‐chelating activity assay and lipid peroxidation inhibition assay. The HSDRBH‐75 had the highest reducing power assay and inhibition ratio of linoleic acid autoxidation, which might be associated with reduced molecular weight, amino acid composition and hydrophobicity. The highest metal‐chelating activity of four different fractions (at the concentration of 4 mg mL^?1) had a positive correlation (r = 0.768, P = 0.116) with the total content of basic amino acid (Lys, Arg, and His) and a negative correlation (r = ?0.886, P = 0.057) with the range of molecular weight (Mw < 1000 Da). The HSDRBH‐75 had the highest antioxidant activities in many assays, which suggests that it may become a good natural antioxidant as a food additive.     

The prevention of fish spoilage by high antioxidant Australian culinary plants: Shewanella putrefaciens growth inhibition

Shewanella putrefaciens is a marine bacterium and a major microbial cause of spoilage in low temperature stored seafood. A survey of fruits and culinary herbs was undertaken on Australian plants with high antioxidant capacities. Twenty‐eight extracts from thirteen plant species were investigated for the ability to inhibit S. putrefaciens growth. Of these, eight extracts (28.6%) substantially inhibited S. putrefaciens growth. The muntries (Kunzea pomifera), lemon aspen (Acronychia acidula) and desert lime (Citrus glauca) extracts were efficient anti‐S. putrefaciens agents, with MIC values ≤3000 μg mL^?1. Of these, the muntries methanolic extract was the most potent growth inhibitor (MIC = 2240 μg mL^?1). The aqueous desert lime extract was also an effective growth inhibitor (MIC of 3857 μg mL^?1), whilst the methanolic bush tomato (Solanum aviculare), aqueous muntries and Davidson's plum (Davidsonia pruriens) extracts displayed moderate S. putrefaciens growth inhibition. All extracts were nontoxic in the Artemia fransiscana bioassay, with LC50 values (>1000 μg mL^?1). Nontargeted HPLC‐QTOF mass spectroscopy (with screening against three compound databases) putatively identified twenty compounds that were present in both inhibitory muntries extracts. The low toxicity of these extracts and their inhibitory bioactivity against S. putrefaciens indicates their potential as natural fish and seafood preservatives.