Angiotensin I-converting enzyme (ACE) inhibitory activities of sardinelle (Sardinella aurita) by-products protein hydrolysates obtained by treatment with microbial and visceral fish serine proteases

Bougatef, Ali; Nedjar‐Arroume, Naïma; Ravallec‐Plé, Rozenn; Leroy, Y.; Guillochon, Didier; Barkia, Ahmed; Nasri, Monçef

doi:10.1016/j.foodchem.2008.03.074

Cited by 199 publications

(135 citation statements)

References 41 publications

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“…The rate of enzymatic hydrolysis was subsequently decreased, until reaching a stationary phase when no apparent hydrolysis took place. This is similar to the typical hydrolysis curve reported by Bougatef et al (2008), Giménez et al (2009) and Klompong et al (2007). According to Benjakul and Morrissey (1997), the rate of enzymatic cleavage of peptide bond controls the overall rate of hydrolysis.…”

Section: Resultssupporting

confidence: 88%

“…Inhibition potencies of alcalase digest of skin (IC 50 0870 μg/ml) and bone (IC 50 0710 μg/ml) gelatin before fractionation were significantly higher than untreated skin (IC 50 01680 μg/ml) and bone (IC 50 01550 μg/ml) gelatin (Table 1). The ACE inhibition activity of skin and bone gelatin hydrolysates in the present study were almost similar with that of alaska pollack skin (IC 50 0629 μg/ml) , skate skin (IC 50 0680 μg/ml) (Lee et al 2011), sardinella byproduct (IC 50 0810 μg/ml) (Bougatef et al 2008) and sea bream scales (IC 50 0570 μg/ml) (Fahmi et al 2004) protein hydrolysates. Results of this study indicated that by increasing the MWCO size, ACE inhibition activity of fractions were increased.…”

Section: Degree Of Hydrolysis (%)supporting

confidence: 78%

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ACE inhibitory activity of pangasius catfish (Pangasius sutchi) skin and bone gelatin hydrolysate

et al. 2012

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Skin and bone gelatins of pangasius catfish (Pangasius sutchi) were hydrolyzed with alcalase to isolate Angiotensin Converting Enzyme (ACE) inhibitory peptides. Samples with the highest degree of hydrolysis (DH) were separated into different fractions with molecular weight cutoff (MWCO) sizes of 10, 3 and 1 kDa, respectively and assayed for ACE inhibitory activity. Skin and bone gelatins had highest DH of 64.87 and 68.48 % after 2 and 1 h incubation, respectively. Results from this study indicated that by decreasing the molecular weight of fractions, ACE inhibitory activity was increased. Therefore, F 3 permeates (MWCO< 1 kDa) of skin (IC 50 03.2 μg/ml) and bone (IC 50 01.3 μg/ml) gelatins possessed higher ACE inhibitory activity compared to their untreated gelatins and corresponding hydrolyzed fractions. In this study, the major amino acids were Glycine followed by Proline with an increased amount of hydrophobic amino acid content in F 3 permeates of skin (4.01 %) and bone (5.79 %) gelatin. Digestion stability against gastrointestinal proteases did not show any remarkable change on ACE inhibition potency of these permeates. It was concluded that alcalase hydrolysis of P. sutchi by-products could be utilized as a part of functional food or ingredients of a formulated drug in order to control high blood pressure.

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Section: Resultssupporting

confidence: 88%

Section: Degree Of Hydrolysis (%)supporting

confidence: 78%

ACE inhibitory activity of pangasius catfish (Pangasius sutchi) skin and bone gelatin hydrolysate

et al. 2012

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“…The protein hydrolysate has been found to possess bioactivity e.g. radical scavenging activity, chelating (Klomklao et al, 2013), antihypertensive (Bougatef et al, 2008) etc. Fish protein hydrolysates such as by-products protein hydrolysate from Persian sturgeon (Ovissipour et al, 2009), threadfin bream (Wiriyaphan, Chitsomboon, & Yongsawadigul, 2012) or meat protein hydrolysates from round scad (Thiansilakul, Benjakul, & Shahidi, (Wu, Chen, & Shiau, 2003) and toothed ponyfish (Klomklao et al, 2013) have been reported to show antioxidative activity.…”

Section: Introductionmentioning

confidence: 99%

Untitled

Klomklao¹,

Benjakul²

2018

Turk. J. Fish. Aquat. Sci.

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Protein hydrolysates from skipjack tuna viscera prepared using Alcalase 2.4 L (VPH) with different degree of hydrolysis (DH: 10%, 20% and 30%) were prepared and determined for their antioxidative activity. VPH with 20% DH had the highest DPPH, ABTS radical scavenging activities and ferrous chelating activity (P<0.05). However, ferric reducing antioxidant activity of hydrolysates increased as DH increased (P<0.05). When VPH with 20% DH was determined for its pH and thermal stability, ABTS radical scavenging activity remained constant or slightly decreased in a wide pH range (2-11) and during heating (100°C) for 180 min. Functional properties of VPH (20% DH) at different concentrations were also investigated. The emulsifying and foaming properties were governed by its concentrations used. Hydrolysis by Alcalase at 20% DH increased protein solubility to above 91% over a wide pH range (3-9). Therefore, VPH could be used as a food additive possessing both antioxidant activity and functional properties.

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“…Recently, the use of alkaline proteases from marine digestive organs, especially trypsin, has increased remarkably since they are both stable and active under harsh conditions, such as at temperatures of 50-60ºC, high pHs, and in the presence of surfactants or oxidizing Page 4 of 27 agents [18]. The enzymes recovered from fish viscera have also been successfully used as seafood processing aids including the acceleration of fish sauce fermentation [19], extraction of carotenoprotein [20], and production of protein hydrolysates [21], [22], [23], [24] and [25].…”

Section: Introductionmentioning

confidence: 99%

“…Alkaline proteases or trypsin have been used to produce protein hydrolysates and the obtained hydrolysates showed bioactive properties such as antioxidant and angiotensin I converting enzyme (ACE) inhibitory properties [21], [22], [23] and [25]. Crude enzyme extract from sardine (Sardina pilchardus) viscera was used to produce protein hydrolysates from heads and viscera of sardinelle compared with Alcalase and provided the potent ACE inhibitory peptides with IC 50 1.2 mg/ml [25].…”

Section: Introductionmentioning

confidence: 99%

Three-phase partitioning and proteins hydrolysis patterns of alkaline proteases derived from fish viscera

Ketnawa

Benjakul

Martínez-Álvarez

et al. 2014

Separation and Purification Technology

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In this study, the recovery alkaline proteases from farmed giant catfish viscera were isolated by using three-phase partitioning (TPP). Factors affecting partitioning efficiency such as salts, solvent types, pH, and incubation temperatures were studied. Furthermore, the application of extracted alkaline proteases on proteins hydrolysis was also determined. The system consisted of crude enzyme extract: t-butanol 1: 0.5 (w/v), 50% sodium citrate, pH 8.0 with incubation temperature of 25ºC provided the highest enzyme recovery (220%). The smear protein bands with molecular weight of 20, 24, and 215 kDa of TPP fractions appeared on the protein stained gel. Two major clear zones (24 and 130 kDa) in the interphase were observed on casein-substrate gel electrophoresis. Extracted alkaline proteases showed relatively high effective in protein hydrolysis. As a result, TPP provided high enzyme recovery and could be applied to other enzymes. The obtained alkaline proteases can be further applied in preparation of protein hydrolysates.

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Angiotensin I-converting enzyme (ACE) inhibitory activities of sardinelle (Sardinella aurita) by-products protein hydrolysates obtained by treatment with microbial and visceral fish serine proteases

Cited by 199 publications

References 41 publications

ACE inhibitory activity of pangasius catfish (Pangasius sutchi) skin and bone gelatin hydrolysate

ACE inhibitory activity of pangasius catfish (Pangasius sutchi) skin and bone gelatin hydrolysate

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Three-phase partitioning and proteins hydrolysis patterns of alkaline proteases derived from fish viscera

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