Characterisation of trypsin purified from the viscera of Tunisian barbel (Barbus callensis) and its application for recovery of carotenoproteins from shrimp wastes |
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Authors: | Assaâ d SilaRim Nasri,Mourad JridiRafik Balti,Moncef NasriAli Bougatef |
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Affiliation: | Laboratory of Microbiology and Enzyme Engineering - National School of Engineering, P.O. Box 1173, Sfax 3038, Tunisia |
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Abstract: | Trypsin was purified from the viscera of barbel by precipitation using ammonium sulphate (0-80%), Sephadex G-100, and Mono Q-Sepharose ion exchange chromatography. The trypsin was purified 27-fold, with 79 U/mg specific activity and 31% recovery. The enzyme had a molecular weight of 24 kDa; purified trypsin appeared as a single band on native-PAGE. The optimum pH and temperature for enzyme activity were pH 10.0 and 55 °C with BAPNA used as a substrate. The N-terminal amino acid sequence of the first 12 amino acids of the purified trypsin was IVGGYECTPYSQ. The Michaelis-Menten constant (Km) and catalytic constant (kcat) values of the enzyme were 0.018 mM and 1.21 s−1, respectively. The study also investigated the effects of purified trypsin on the recovery of carotenoproteins from shrimp (Parapenaeus longirostris) shells through hydrolysis using 1.0 U barbel trypsin/g shrimp shells for 1 h at 30 °C. The freeze-dried carotenoproteins recovered contained 71.09% protein, 16.47% lipid, 7.78% ash, and 1.79% chitin. |
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Keywords: | Trypsin Barbus callensis Viscera Purification Carotenoprotein Shrimp waste |
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