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Catalytic, thermodynamic and structural properties of an immobilized and highly thermostable alkaline protease from a haloalkaliphilic actinobacteria, Nocardiopsis alba TATA-5

Thakrar, Foram J., Singh, Satya P.
Bioresource technology 2019 v.278 pp. 150-158
Fourier transform infrared spectroscopy, Nocardiopsis alba, activation energy, alkenes, amines, batch systems, detergents, enzyme bioreactors, esters, half life, immobilized enzymes, metal ions, pH, proteinases, temperature, thermal stability, thermostable enzymes, topography, wastewater
A highly thermostable protease from a haloalkaliphilic actinobacteria was immobilized employing 5 different approaches on 24 carriers. On immobilization, the activation energy and deactivation rate constant decreased, which makes the immobilized protease favourable for applications. Similarly, pH and temperature stability was enhanced, while the Vmax and Km changed upon immobilization. The immobilized enzyme had greater stability in various metal ions and detergents. The structural topography of the immobilized enzyme elucidated by the FTIR suggested the function of aliphatic amines, alkenes and esters since amide I and II bands were affected. Noticeable decrease in the Amide A band suggests interaction between the immobilization carriers and –NH groups of the protease molecule. The suitability of the immobilized protease was established by designing a continuous flow enzyme bioreactor, displaying the enzyme half-life of 916.15 min at 60 °C. The enzyme reactor was highly efficient in the treatment of the municipal and dairy wastewater.