<i>Arthrobacter arilaitensis</i>Re117 as a Source of Solvent-Stable Proteases: Production, Characteristics, Potential Application in the Deproteinization of Shrimp Wastes and Evaluation in Liquid Laundry Commercial Detergents

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&degC, 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.

阿氏节杆菌菌株DA-1的厌氧反硝化研究

阿氏节杆菌(Arthrobacter arilaitensis)菌株DA-1是一株氨氮降解细菌,且在有氧及厌氧条件下均具有反硝化作用。通过对该菌的厌氧反硝化条件进行优化,考察了碳源、C/N、温度和初始pH对其反硝化作用的影响。结果表明,乙酸钠为最佳的反硝化碳源,当C/N为10∶1、温度为30℃、初始pH为7.0时,A.arilaitensis DA-1能获得最高的反硝化效率,在该条件下,向硝酸盐模拟污水(NO3--N浓度为25mg/L)中接入2%(V/V)的A.arilaitensis DA-1菌剂,经过48 h的静置培养,NO3--N的去除量达到了20.13 mg/L,而此时NO2--N积累浓度仅为0.56 mg/L。