Antioxidative activity and functional properties of protein hydrolysate of yellow stripe trevally (Selaroides leptolepis) as influenced by the degree of hydrolysis and enzyme type

Klompong, Vilailak; Benjakul, Soottawat; Kantachote, Duangporn; Shahidi, Fereidoon

doi:10.1016/j.foodchem.2006.07.016

Cited by 814 publications

(708 citation statements)

References 44 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%

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%

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

et al. 2012

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“…1). The typical hydrolysis curves were also reported for brownstripe red snapper (Lutjanus vitta) (Khantaphant et al 2011), yellow stripe trevally (Klompong et al 2007), herring (Liceaga- Gesualdo and Li-Chan 1999), salmon muscle (Kristinsson and Rasco 2000b), sardinelle by-products ) and smooth hound muscle ).…”

Section: Preparation Of Sardinelle Protein Hydrolysates Using Varioussupporting

confidence: 58%

“…Fish protein hydrolysates such as skin gelatin hydrolysate from brownstripe red snapper (Khantaphant and Benjakul 2008) or meat protein hydrolysates from yellow travelly (Klompong et al 2007;Klompong et al 2009), round scad (Thiansilakul et al 2007a,b), mackerel (Wu et al 2003), loach (You et al 2010), and smooth hound (Mustelus mustelus) muscle ) have been reported to exhibit antioxidant activity. Fish protein hydrolysates can be used in food systems, comparable to other pertinent protein hydrolysates (Kristinsson and Rasco 2000a).…”

Section: Introductionmentioning

confidence: 99%

Composition, functional properties and in vitro antioxidant activity of protein hydrolysates prepared from sardinelle (Sardinella aurita) muscle

et al. 2011

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Composition, functional properties and in vitro antioxidative activities of protein hydrolysates prepared from muscle of sardinelle (Sardinella aurita) were investigated. Sardinelle protein hydrolysates (SPH) were obtained by treatment with crude enzyme preparations from Bacillus pumilus A1 (SPHA1), Bacillus mojavensis A21 (SPHA21) and crude enzyme extract from sardinelle (Sardinella aurita) viscera (SPHEE). The protein hydrolysates SPHA1, SPHA21 and SPHEE contained high protein content 79.1%, 78.25% and 74.37%, respectively. The protein hydrolysates had an excellent solubility and possessed interfacial properties, which were governed by their concentrations. The antioxidant activities of protein hydrolysates at different concentrations were evaluated using various in vitro antioxidant assays, including 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical method, reducing power assay, chelating activity, β-carotene bleaching and DNA nicking assay. All protein hydrolysates showed varying degrees of antioxidant activity. SPHA21 had the highest DPPH radical scavenging activity (89% at 6 mg/ml) and higher ability to prevent bleaching of β-carotene than SPHA1 and SPHEE (p<0.05). However, SPHEE exhibited the highest metal chelating activity (89% at 1 mg/ml) and the strongest protection against hydroxyl radical induced DNA breakage (p<0.05).

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“…Protein hydrolysate with 15% DH, which exhibited the highest antioxidative activity, compared with those with DHs of 5 and 25% (Klompong et al 2007), were dissolved in distilled water to obtain the various concentration of 0.5, 1.0, 1.5, 2.0, 2.5, 3.0, 3.5, 4.0, 4.5 and 5.0 mg ⁄mL. Antioxidative activity of protein hydrolysates at different concentrations was measured by monitoring the DPPH, FRAP and ABTS assays.…”

Section: Effect Of Concentration Of Protein Hydrolysate On Antioxidatmentioning

confidence: 90%

Antioxidative activity of protein hydrolysate produced by alcalase hydrolysis from shrimp waste (Penaeus monodon and Penaeus indicus)

Dey

Dora

2011

J Food Sci Technol

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Protein hydrolysates prepared by hydrolysis of shrimp waste (Penaeus monodon and Penaeus indicus) for 90 min. using Alcalase enzyme following pH-stat method. Antioxidative activities of SWPH were assessed determining FRAP, ABTS and DPPH radical scavenging activities, which increased linearly with increasing concentration of protein hydrolysate upto 5 mg/ml maintaining good correlation. SWPH showed high stability over wide ranges of pH (2-11) and temperature (up to 100°C for 150 min), in which the activity of more than 80% was retained. Protein hydrolysate solution with a concentration of 5 mg/ml significantly lowered TBA values of Croaker fish fillet and maintained yellowishness of skin colour compared to untreated control sample during 10 days of refrigerated storage at 4°C. SWPH also restricted the increase of PV and FFA values in Croaker fish fillet within acceptable limit.

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Antioxidative activity and functional properties of protein hydrolysate of yellow stripe trevally (Selaroides leptolepis) as influenced by the degree of hydrolysis and enzyme type

Cited by 814 publications

References 44 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

Composition, functional properties and in vitro antioxidant activity of protein hydrolysates prepared from sardinelle (Sardinella aurita) muscle

Antioxidative activity of protein hydrolysate produced by alcalase hydrolysis from shrimp waste (Penaeus monodon and Penaeus indicus)

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