Digestive alkaline proteases from thornback ray (Raja clavata): Characteristics and applications

• Published in: International journal of biological macromolecules 2015-09, Vol.80, p.668-675
• Main Authors: Lassoued, Imen, Hajji, Sawssen, Mhamdi, Samiha, Jridi, Mourad, Bayoudh, Ahmed, Barkia, Ahmed, Nasri, Moncef
• Format: Article
• Language: English
• Subjects: Alkaline proteases; Animals; Bacterial Proteins - antagonists & inhibitors; Bacterial Proteins - chemistry; Bacterial Proteins - metabolism; Chitin; Chitin - chemistry; Detergents - pharmacology; Endopeptidases - chemistry; Endopeptidases - metabolism; Enzyme Activation - drug effects; Enzyme Stability; Hydrogen-Ion Concentration; Ions - chemistry; Liquid laundry detergent; Metals - chemistry; Oxidants - pharmacology; Protease Inhibitors - pharmacology; Skates (Fish) - metabolism; Substrate Specificity; Surface-Active Agents - pharmacology; Temperature
• ISSN: 0141-8130; 1879-0003
• DOI: 10.1016/j.ijbiomac.2015.07.038

This study describes the characterization of a crude protease extract from thornback ray (Raja clavata) and its evaluation in liquid detergent and in deproteinizattion of shrimp waste. At least five clear caseinolytic proteases bands were observed in a zymogram. The crude protease showed optimum activity at pH 8.0 and 50°C, and it was highly stable over pH range from 8.0 to 11.0. Proteolytic enzymes were very stable in non-ionic surfactants and in the presence of oxidizing agents, maintaining 70% of their activity after incubation for 1h at 30°C in the presence of 1% sodium perborate. In addition, they showed high stability and compatibility with various liquid laundry-detergents available in the Tunisian market. The crude extract retained 100% of its activity after preincubation for 60min at 30°C in the presence of Nadhif Perfect, Textil and Carrefour laundry detergents. Further, proteases from R. clavata viscera were used for shrimp waste deproteinization in the process of chitin preparation. The percent of protein removal after 3h hydrolysis at 45°C with an enzyme/substrate ratio of 30U/mg of proteins was 74%. These results suggest that enzymatic deproteinization of shrimp wastes by fish endogenous alkaline proteases could be applicable to the chitin production process.