Purification and Characterization of Trypsin from the Intestine of Hybrid Tilapia (<i>Oreochromis niloticus × O.aureus</i>)

Wang, Qin; Gao, Z G; Zhang, Nong; Shi, Yan; Xie, Xiao-Lan; Chen, Qing‐Xi

doi:10.1021/jf903052s

Cited by 27 publications

(19 citation statements)

References 25 publications

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“…This is probably because of enzyme denaturation at very acidic and very high alkaline pH values. Similar values have been reported for spotted goatfish P. maculates (Souza et al, 2007) and hybrid tilapia O. niloticus x O. aureus (Wang et al, 2010).…”

Section: Effect Of Ph On Activity and Stabilitysupporting

confidence: 88%

“…relative activities at 40, 50 and 70°C were about 37, 71 and 52%, respectively, of that at 60°C. Generally, these data shows parallelism with those reported by Kurtovic et al (2006), Bougatef et al (2007), Khantaphant and Benjakul (2010) and Wang et al (2010). The optimal temperature range of trypsin-like proteinases in Indian anchovy was from 50 to 60°C (Siringanet et al, 2007).…”

Section: Effect Of Temperature On Activity and Stabilitysupporting

confidence: 80%

“…Ammonium sulphate precipitation was a simple method and generally introduced as an initial step. The saturated solution selectively precipitates proteins by the salt out mechanism from the crude extract (Klomklao et al, 2006b;Khantaphant and Benjakul, 2010;Wang et al, 2010). Martinez et al (1988) found that ammonium sulphate precipitation (20-70%) of trypsin-like enzyme from anchovy digestive tract resulted in a 2.7-fold increase in purity.…”

Section: Partial Purification Of Alkaline Proteasesmentioning

confidence: 99%

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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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Section: Effect Of Ph On Activity and Stabilitysupporting

confidence: 88%

Section: Effect Of Temperature On Activity and Stabilitysupporting

confidence: 80%

Section: Partial Purification Of Alkaline Proteasesmentioning

confidence: 99%

See 1 more Smart Citation

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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“…Peak trypsin activity occurred at 50 °C, lower than that of other fish species: Astroctosteus tropicus (65 °C; Guerrero-Zarate et al, 2014) and tilapia hybrid (60 °C; Wang et al, 2010).…”

Section: Effect Of Temperaturementioning

confidence: 84%

Characterization of digestive enzymes from captive Brazilian flounder Paralichthys orbignyanus

et al. 2017

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Knowledge of specific enzyme activity, along with animal habits and digestive capacity is essential in formulating an appropriate diet for any species. In this study, we evaluated and characterized the activity of digestive enzymes present in the liver, intestine, and stomach of Paralichthys orbignyanus. The effects of pH and temperature on enzyme activity were also evaluated via the use of specific substrates. The use of specific substrates and inhibitors showed strong evidence of the presence of trypsin (BApNA= 0.51 ± 0.2 mU mg -1 ), chimotrypsin (SApNA= 2.62 ± 1.8 mU mg -1 ), and aminopeptidases (Leu-p-Nan =0.9709 ± 0.83 mU mg -1 ) in the intestine. Optimum pH for the activity of trypsin, chemotrypsin, leucino aminopeptidase, amilase, and pepsin were 9.5, 9.0, 8.0, 7.5, and 3.5, respectively, while optimum temperatures were 50, 50, 50, 40, and 45 °C, respectively. These results provide additional information regarding the biology of Brazilian flounder and can be used as a basis for further studies regarding fish feeding physiology.Keywords: trypsin, protease, digestive tract. Caracterização de enzimas digestivas do linguado brasileiro de cativeiro Paralichthys orbignyanusResumo O conhecimento da atividade enzimática é essencial para formular uma correta dieta específica para espécie, além de estarem correlacionadas com o hábito da alimentação e capacidade digestive. Neste estudo determinamos e caracterizamos a atividade enzimática presente no intestino, estômago e fígado do linguado Paralichthys orbignyanus. Os efeitos da temperatura e pH sobre a atividade enzimática também foram avaliados utilizando substratos específicos. O uso de substratos e inibidores específicos mostrou uma forte evidência da presença da tripsina (BApNA = 0,51 ± 0,2 mU mg-1), quimotripsina (SAPNA = 2,62 ± 1,8 mU mg-1), e as aminopeptidases (Leu-p-Nan = 0,97 ± 0,83 mU mg-1) no intestino. O pH ótimo observado para a atividade de tripsina, quimotripsina, leucino aminopeptidase, amilase e pepsina foi 9,5, 9,0, 8,0, 7,5 e 3,5, respectivamente. A temperatura ótima observada foi 50, 50, 50, 40 e 45 °C, respectivamente. Estes resultados fornecem informações adicionais sobre a biologia do linguado brasileiro e pode ser usado como base para novos estudos sobre fisiologia alimentar.Palavras-chave: tripsina, proteases, trato digestório.Candiotto, F.B. et al.

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“…It is a member of serine proteases that specifically cleave the ester and peptide bonds on the carboxyl sides of arginine and lysine (Simpson ; Wang et al . ). Trypsin is responsible for digestion in the intestine and activation of zymogens of the pancreatic enzymes, including itself, in the biological processes (Rypniewski et al .…”

Section: Introductionmentioning

confidence: 97%

Purification and Characterization of a Trypsin-Like Protease from Flatfish (Paralichthys olivaceus) Intestine

Kim

Jeong

2012

Journal of Food Biochemistry

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A trypsin-like protease was purified from the intestine of flatfish (Paralichthys olivaceus) by gel filtration and anion-exchange chromatography. The molecular weight was estimated to be 29.6 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Flatfish protease had maximal activity at 70C and pH 7.5 using N-a-benzoyl-dl-arginine-r-nitroanilide as substrate. It was stable to heat treatment up to 50C and to pH ranges between 7.0 and 10.0. It was activated by calcium ion and completely inhibited by mercury ion and known serine-protease inhibitors, such as phenylmethylsulfonyl fluoride, tosyl lysine chloromethyl ketone and benzamidine. PRACTICAL APPLICATIONSFlatfish trypsin could be an alternative to commercial trypsins in a wide variety of applications in the food, detergent and pharmaceutical industries. In the food industry, trypsin is used to produce protein hydrolysates, extract flavor, tenderize meat and improve oil extractions. It is also used in detergent, bating of leather and in diabetes diagnosis and therapy. Moreover, it can break down tumors and cancer cells in cancer therapy.

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Purification and Characterization of Trypsin from the Intestine of Hybrid Tilapia (Oreochromis niloticus × O.aureus)

Cited by 27 publications

References 25 publications

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

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

Characterization of digestive enzymes from captive Brazilian flounder Paralichthys orbignyanus

Purification and Characterization of a Trypsin-Like Protease from Flatfish (Paralichthys olivaceus) Intestine

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