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• W2017256469 abstract "An alkaline trypsin was purified from the viscera of zebra blenny (Salaria basilisca) by ammonium sulphate (40−80% saturation) precipitation, Sephadex G-100, Mono Q-Sepharose and ultrafiltration. A yield of 12% with a purification-fold of 4.2 was obtained. The trypsin had an apparent molecular weight of 27 kDa. Soybean trypsin inhibitor and phenylmethylsulfonyl fluoride showed a strong inhibitory effect on the purified trypsin. Trypsin had maximal activity at pH 9.5 and 60 °C for the hydrolysis of Nα-benzoyl-dl-arginine-p-nitroanilide (BAPNA). It was stable at low temperatures and in the pH range of 7.0−12.0. The N-terminal amino acid sequence of the first 12 amino acids of the purified protease was IVGGRECTEPSQ. S. basilisca trypsin, which showed high homology with other fish trypsins, had a charged Arg residue at position 5, where Tyr is common in marine vertebrates and mammalian trypsins. The trypsin kinetic constants, Km and kcat for BAPNA, were 0.6 mM and 1.38 s−1, respectively." @default.
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• W2017256469 date "2012-02-01" @default.
• W2017256469 modified "2023-09-25" @default.
• W2017256469 title "Trypsin from zebra blenny (Salaria basilisca) viscera: Purification, characterisation and potential application as a detergent additive" @default.
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• W2017256469 doi "https://doi.org/10.1016/j.foodchem.2011.07.015" @default.
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