Catalytic, thermodynamic and structural properties of an immobilized and highly thermostable alkaline protease from a haloalkaliphilic actinobacteria, Nocardiopsis alba TATA-5.
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DOI: 10.1016/j.biortech.2019.01.058
Abstract: 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.… read more here.
Keywords: protease; protease haloalkaliphilic; haloalkaliphilic actinobacteria; thermodynamic structural ... See more keywords