Isolation and characterisation of trypsin from sardinelle (<i>Sardinella aurita</i>) viscera

Khaled, Hayet Ben; Bougatef, Ali; Balti, Rafik; Triki-Ellouz, Yosra; Souissi, Nabil; Nasri, Monçef

doi:10.1002/jsfa.3386

Cited by 39 publications

(40 citation statements)

References 31 publications

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“…The enzyme preparations used were: alkaline proteases from B. pumilus A1 (Fakhfakh-Zouari et al 2010) and B. mojavensis A21 (Haddar et al 2009), and crude enzyme extract from viscera of sardinelle (S. aurita) (Ben khaled et al 2008). All proteolytic enzymes were prepared in our laboratory.…”

Section: Enzymesmentioning

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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Section: Enzymesmentioning

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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“…However, the data reported by other authors were higher than the values achieved in our study, demonstrating that the trypsin from E. anchoita viscera has a superior affinity for BAPNA. The catalytic efficiency (k cat /K m ) of E. anchoita trypsin by-products, 2.11/s mM was close to that of trypsins from the digestive tract of anchovy E. encrasicholus , sardinella (Sardinella aurita ) (Khaled et al, 2008) and the pancreas of small-spotted catshark (Scyliorhinus canicula ) (Blanco et al, 2014), using the same substrate. Trypsin (EC 3.4.21.4) is a member of the serine proteinase family that specifically hydrolyzes proteins and peptides at the carboxyl side of arginine and lysine residues constituting important roles in biological processes (Cao et al, 2000).…”

Section: Kinetic Studymentioning

confidence: 62%

“…These results are in agreement with the increment obtained by Blanco and coworkers (2014) in the pancreas of small-spotted catshark. Other studies described an opposite effect on trypsins isolated from the intestines of sardinella (Khaled et al, 2008) and of triggerfish (Jellouli et al, 2009). Enzymes that resist the denaturation ability of SDS have been reported earlier (Rao et al, 1989).…”

Section: Effect Of Metallo-protease Inhibitor and Surfactant On Trypsmentioning

confidence: 92%

Alkaline trypsin from the viscera and heads of Engraulis anchoita : partial purification and characterization

Lamas¹,

Yeannes²,

Massa³

2017

bta

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Marine by-products contain valuable protein fractions. To ensure a profitable utilization of wastes from the fish industry, the knowledge about their quality and composition is necessary. Fish digestive proteolytic enzymes from cold-adapted ectothermic organisms have found applications in several industries because their temperature requirements and other characteristics differ from those of homologous proteases from warm-blooded animals. Herein, we describe detection, partial purification, and characterization of proteolytic enzymes from the viscera and heads of Engraulis anchoita. Enzymatic activities of the by-products were assayed using azocaseín as a substrate. To characterize the alkali protein fraction, the activity against inhibitors and their molecular weights were studied. The crude protein extract exhibited maximal activity at pH 8.0 and 60EC. Results relative to the substrate-specific Nabenzoyl-DL-arginine-p-nitroanilide and the 25 kDa molecular weight indicated that the recovered protease was trypsin. The activity showed an increment in presence of SDS and a slight decrease when it was incubated with EDTA. Increasing the concentration of NaCl up to 5% did not significantly decrease the protein's activity. The results obtained suggest that by-products of anchovy industry could be used in the detergents industry.

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“…In resemblance with the results of our study, Bougatef et al (2007) asserted that the trypsin from the viscera of sardine at 40 and 50°C remained significantly active even after 250 min of incubation. In addition, Castillo-Yanez et al (2005), Shi et al (2007) and Khaled et al (2008) reported that good thermal stability was observed in fish trypsins incubated at 40°C for 15-45 min, while the enzyme lost all its activity when heated at 60°C for 15 min. The trypsin from hoki fish (Shi et al, 2007) and Sardinella viscera (Khaled et al, 2008) were found to be inactive when heated at 60°C for 30 min.…”

Section: Effect Of Temperature On Activity and Stabilitymentioning

confidence: 99%

“…fishing industry, are recognized as potential source of digestive enzymes, especially proteases with high activity over a wide range of pH and temperature conditions (Castillo-Yanez et al, 2006;Klomklao et al, 2006a;Bougatef et al, 2007;Khaled et al, 2008). Proteases constitute the most important group of industrial enzymes used in the world today (Bougatef et al, 2007;El-Beltagy et al, 2004;Souza et al, 2007), accounting for about 50% of the total industrial enzyme market (Bougatef et al, 2007;Souza et al, 2007).…”

Section: Introductionmentioning

confidence: 99%

Partial purification and characterization of alkaline proteases from the Black Sea anchovy(Engraulis encrasicholus) digestive tract

Temiz¹,

Üstün²,

Turhan³

et al. 2013

Afr. J. Biotechnol.

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Alkaline proteases from the digestive tract of anchovy were partially purified by ammonium sulfate fractionation, dialysis and Sephadex G-75 gel filtration. The purification fold and yield were 6.23 and 4.49%, respectively. The optimum activities of partially purified alkaline proteases were observed at 60°C and at pH 11.0. The alkaline proteases were stable within the temperature range of 40 to 50°C and pH range of 9.0 to 11.0. They were inhibited by the serine-protease inhibitor phenylmethylsulfonyl fluoride (PMSF) and trypsin specific inhibitor benzamidine, but were not inhibited by the β-mercaptoethanol. The enzymes were slightly activated by metal ions such as Na +

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Isolation and characterisation of trypsin from sardinelle (Sardinella aurita) viscera

Cited by 39 publications

References 31 publications

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

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

Alkaline trypsin from the viscera and heads of Engraulis anchoita : partial purification and characterization

Partial purification and characterization of alkaline proteases from the Black Sea anchovy(Engraulis encrasicholus) digestive tract

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