Abstract
The present study describes the characterization of crude protease extract from Arthrobacter arilaitensis Re117 and its evaluation in solid and liquid detergent. One caseinolytic protease clear band was observed in zymogram. The crude alkaline protease showed optimum activity at pH 9.0 and 50°C, and it was highly stable over a wide range of pH from 8.0 to 9.0. Proteolytic enzymes showed extreme stability towards non-ionic surfactants (Tween 80, Tween 20 and Triton X-100) and stimulate activity towards oxidizing agents such as sodium perborate. They also showed high stability and compatibility with various laundry solid detergents from Tunisian market. The protease of A. arilaitensis Re117, was also tested for shrimp waste deproteinization to produce chitin. The protein removal with a ratio E/S of 20 was about 83%. The novelties of the Re117 protease include its high stability to organic solvents and surfactants. These unique properties make it an ideal choice for application in detergent formulations and enzymatic peptide synthesis. In addition, the enzyme may find potential applications in the deproteinization of shrimp wastes to produce chitin.
Highlights
Proteases constitute one of the most important groups of industrial enzymes, and account for at least 60% of all global enzyme sales [1]
The present paper describes some biochemical characterization of the alkaline crude enzyme preparation from A. arilaitensis as well as its compatibility with commercial laundry detergents, oxidants, surfactant agents and organic solvents and its application in the deproteinization of shrimp wastes
Protease Production In this study, protease production by A. arilaitensis strain was first tested in M1 medium containing different carbon sources at a concentration of 10 g/l
Summary
Proteases constitute one of the most important groups of industrial enzymes, and account for at least 60% of all global enzyme sales [1]. They have diverse applications in a wide variety of industries such as detergent, food, pharmaceutical, leather, peptide synthesis, and for the recovery of silver from used X-ray films [2] [3]. It is relevant to search for proteases from new sources presenting high thermal stability, alkaline activity and more compatible with washing systems [8] [9]. These properties have already been observed in trypsin-like enzymes
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